PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25683270-8 2015 E2 induced NGB re-allocation in mitochondria where, subsequently to an oxidative stress injury (i.e., 100muM H2O2), NGB interacted with cytochrome c preventing its release into the cytosol and the activation of an apoptotic cascade. Hydrogen Peroxide 109-113 cytochrome c, somatic Homo sapiens 136-148 25720812-3 2015 Western blot data demonstrated that THF inhibited the H2O2-induced up- or down-regulation of cleaved caspase-3, cleaved caspase-9, cleaved poly-ADP-ribose polymerase (PARP), Bax, Bcl-2, and Bcl-xL, and attenuated the H2O2-induced release of cytochrome c from the mitochondria to the cytosol. Hydrogen Peroxide 54-58 cytochrome c, somatic Homo sapiens 241-253 25865416-10 2015 Importantly, kinetic experiments show that CYTC bleaching is faster with ChOOH than with H2O2, suggesting that these hydroperoxides could be relevant substrates for CYTC peroxidase-like activity in biological media. Hydrogen Peroxide 89-93 cytochrome c, somatic Homo sapiens 43-47 25865416-10 2015 Importantly, kinetic experiments show that CYTC bleaching is faster with ChOOH than with H2O2, suggesting that these hydroperoxides could be relevant substrates for CYTC peroxidase-like activity in biological media. Hydrogen Peroxide 89-93 cytochrome c, somatic Homo sapiens 165-169 25865416-10 2015 Importantly, kinetic experiments show that CYTC bleaching is faster with ChOOH than with H2O2, suggesting that these hydroperoxides could be relevant substrates for CYTC peroxidase-like activity in biological media. Hydrogen Peroxide 117-131 cytochrome c, somatic Homo sapiens 43-47 25865416-10 2015 Importantly, kinetic experiments show that CYTC bleaching is faster with ChOOH than with H2O2, suggesting that these hydroperoxides could be relevant substrates for CYTC peroxidase-like activity in biological media. Hydrogen Peroxide 117-131 cytochrome c, somatic Homo sapiens 165-169 25865416-11 2015 Altogether, these results show that CYTC induces homolytic cleavage of lipid-derived hydroperoxides, producing lipid and protein radicals. Hydrogen Peroxide 85-99 cytochrome c, somatic Homo sapiens 36-40 24304286-7 2014 C3HOM effectively prevents the oxidative degradation of cytochrome C induced by hydrogen peroxide (H2O2). Hydrogen Peroxide 80-97 cytochrome c, somatic Homo sapiens 56-68 25352420-8 2015 Furthermore, EAL inhibited H2O2-induced apoptosis by increases in the Bcl-2/Bax ratio, decreases in cytochrome c release, and attenuation of caspase-3, caspase-9 activities, and expressions. Hydrogen Peroxide 27-31 cytochrome c, somatic Homo sapiens 100-112 26424020-7 2015 In addition, 2-APB inhibited the release of mitochondrial cytochrome c to the cytosol induced by H2O2 when 2-APB was applied simultaneously with H2O2 but not 30 min post-treatment. Hydrogen Peroxide 97-101 cytochrome c, somatic Homo sapiens 58-70 26424020-7 2015 In addition, 2-APB inhibited the release of mitochondrial cytochrome c to the cytosol induced by H2O2 when 2-APB was applied simultaneously with H2O2 but not 30 min post-treatment. Hydrogen Peroxide 145-149 cytochrome c, somatic Homo sapiens 58-70 26424020-9 2015 These results suggest that the H2O2-induced initial [Ca(2+)]c elevation, occurring within 30 min and mediated by Ca(2+) release through IP3 receptors and subsequent Ca(2+) influx through SOCs, leads to [Ca(2+)]m elevation, possibly through a mechanism independent of MCU, thereby inducing cytochrome c release and consequent apoptosis. Hydrogen Peroxide 31-35 cytochrome c, somatic Homo sapiens 289-301 30154994-0 2015 Specific methionine oxidation of cytochrome c in complexes with zwitterionic lipids by hydrogen peroxide: potential implications for apoptosis. Hydrogen Peroxide 87-104 cytochrome c, somatic Homo sapiens 33-45 30154994-4 2015 In these complexes, Cyt-c reacts efficiently with H2O2 at submillimolar levels, which oxidizes the sulfur atom of the axial ligand Met80. Hydrogen Peroxide 50-54 cytochrome c, somatic Homo sapiens 20-25 30154994-6 2015 Based on these results, we postulate that the rise of H2O2 concentrations to the submillimolar levels registered during initiation of the apoptotic program may represent one signaling event that triggers the gain in peroxidatic function of the Cyt-c molecules bound to the abundant PE and PC membrane components. Hydrogen Peroxide 54-58 cytochrome c, somatic Homo sapiens 244-249 24716876-3 2014 Experimental data demonstrated that Cyt c was stably immobilized into the molecular hydrogel and retained its inherent bioactive activity toward H2O2. Hydrogen Peroxide 145-149 cytochrome c, somatic Homo sapiens 36-41 24716876-4 2014 The direct redox reaction of Cyt c, followed by the biochemical reaction between Cyt c and H2O2, established a reliable approach to determine H2O2 at an optimized potential with high selectivity over other reactive oxygen species (ROS), oxygen, metal ions, ascobic acid (AA), and so on. Hydrogen Peroxide 91-95 cytochrome c, somatic Homo sapiens 29-34 24716876-4 2014 The direct redox reaction of Cyt c, followed by the biochemical reaction between Cyt c and H2O2, established a reliable approach to determine H2O2 at an optimized potential with high selectivity over other reactive oxygen species (ROS), oxygen, metal ions, ascobic acid (AA), and so on. Hydrogen Peroxide 91-95 cytochrome c, somatic Homo sapiens 81-86 24716876-4 2014 The direct redox reaction of Cyt c, followed by the biochemical reaction between Cyt c and H2O2, established a reliable approach to determine H2O2 at an optimized potential with high selectivity over other reactive oxygen species (ROS), oxygen, metal ions, ascobic acid (AA), and so on. Hydrogen Peroxide 142-146 cytochrome c, somatic Homo sapiens 29-34 24716876-4 2014 The direct redox reaction of Cyt c, followed by the biochemical reaction between Cyt c and H2O2, established a reliable approach to determine H2O2 at an optimized potential with high selectivity over other reactive oxygen species (ROS), oxygen, metal ions, ascobic acid (AA), and so on. Hydrogen Peroxide 142-146 cytochrome c, somatic Homo sapiens 81-86 25798458-8 2015 [Cho][AOT] has been found to enhance the peroxidase activity of Cyt c with maximum activity at C3, observed using 2,2"-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt as the substrate in the presence of hydrogen peroxide. Hydrogen Peroxide 221-238 cytochrome c, somatic Homo sapiens 64-69 25688934-5 2015 Cytochrome C-functionalized electrodes prepared using the induced dual nanoelectrospray process showed bioactivity toward aqueous solutions of hydrogen peroxide below 50 muM. Hydrogen Peroxide 143-160 cytochrome c, somatic Homo sapiens 0-12 25495913-4 2015 With the mimicking sandwich-type reaction, the cascade catalysis amplification strategy was carried out by AOx catalyzing ethanol to acetaldehyde with the concomitant formation of high concentration of H2O2, which was further electrocatalyzed by PtNPs and Cyt c. Hydrogen Peroxide 202-206 cytochrome c, somatic Homo sapiens 256-261 25146667-7 2014 Mitochondrial membrane potential decrease, cytochrome c release, caspases activation, activation of AIF and Endo G were observed in H2O2-treated cells by rhodamine 123 or western blot. Hydrogen Peroxide 132-136 cytochrome c, somatic Homo sapiens 43-55 25117536-11 2014 We suggest that hydrogen peroxide in the presence of cyt c promotes a peroxidation of membrane phospholipids to form lysolipids, the embedding of which stabilizes the edge of the pore and the surface of lipid bilayer. Hydrogen Peroxide 16-33 cytochrome c, somatic Homo sapiens 53-58 24954800-5 2014 In the last ten years, our group has demonstrated the generation of singlet molecular oxygen from reactions involving the decomposition of biologically relevant hydroperoxides, especially from lipid hydroperoxides in the presence of metal ions, peroxynitrite, HOCl and cytochrome c. Hydrogen Peroxide 161-175 cytochrome c, somatic Homo sapiens 269-281 25118932-6 2014 Moreover, COD-B treatment resulted in JNK and p38 phosphorylation, downregulation of Bcl-2, upregulation of Bax, activated caspase-3 and cytochrome C release, which likely responded to freshly produced hydrogen peroxide that accompanied cholesterol oxidation. Hydrogen Peroxide 202-219 cytochrome c, somatic Homo sapiens 137-149 24599562-2 2014 p66Shc generates H(2)O(2) by oxidizing cytochrome c, and its expression has been reported to be elevated in several tumors. Hydrogen Peroxide 17-25 cytochrome c, somatic Homo sapiens 39-51 24304286-7 2014 C3HOM effectively prevents the oxidative degradation of cytochrome C induced by hydrogen peroxide (H2O2). Hydrogen Peroxide 99-103 cytochrome c, somatic Homo sapiens 56-68 24099549-3 2013 In this complex cytochrome c has its native axial Met(80) ligand dissociated from the haem-iron, considerably augmenting the peroxidase capability of the haem group upon H2O2 binding. Hydrogen Peroxide 170-174 cytochrome c, somatic Homo sapiens 16-28 25013541-4 2014 H2O2 produced dramatic injuries in HepG2 cells, represented by classical morphological changes of apoptosis, increased levels of malondialdehyde (MDA) and intracellular reactive oxygen species (ROS), decreased activity of superoxide dismutase (SOD), and increased activities of caspase-9 and caspase-3, release of cytochrome c (Cyt-C) and apoptosis-inducing factor (AIF) from mitochondria, and loss of membrane potential (DeltaPsim). Hydrogen Peroxide 0-4 cytochrome c, somatic Homo sapiens 314-326 25013541-4 2014 H2O2 produced dramatic injuries in HepG2 cells, represented by classical morphological changes of apoptosis, increased levels of malondialdehyde (MDA) and intracellular reactive oxygen species (ROS), decreased activity of superoxide dismutase (SOD), and increased activities of caspase-9 and caspase-3, release of cytochrome c (Cyt-C) and apoptosis-inducing factor (AIF) from mitochondria, and loss of membrane potential (DeltaPsim). Hydrogen Peroxide 0-4 cytochrome c, somatic Homo sapiens 328-333 24099549-7 2013 We propose a mechanism of multiple radical formations in the cytochrome c-phospholipid complexes under H2O2 treatment, consistent with the stabilization of the radical in the G41S mutant, which elicits a greater peroxidase activity from cytochrome c and thus has implications in mitochondrial apoptosis. Hydrogen Peroxide 103-107 cytochrome c, somatic Homo sapiens 61-73 24099549-7 2013 We propose a mechanism of multiple radical formations in the cytochrome c-phospholipid complexes under H2O2 treatment, consistent with the stabilization of the radical in the G41S mutant, which elicits a greater peroxidase activity from cytochrome c and thus has implications in mitochondrial apoptosis. Hydrogen Peroxide 103-107 cytochrome c, somatic Homo sapiens 237-249 24059746-10 2013 Interestingly, following treatment with low doses of H2O2, the silencing of CCDC6 in GC1 cells caused a decrease in the oxidized form of cytochrome c and low detection of Bad, PARP-1 and Caspase 3 proteins. Hydrogen Peroxide 53-57 cytochrome c, somatic Homo sapiens 137-149 23291592-10 2013 The same H2O2-treated cells also showed activated ASK (P-ASK), increased Bax, lowered Bcl-2, cytochrome c release, and elevated caspase 3/7 activity. Hydrogen Peroxide 9-13 cytochrome c, somatic Homo sapiens 93-105 23618181-5 2013 The Cyt c/GNPs/PANS modified electrode gives an improved electrocatalytic activity toward the reduction of hydrogen peroxide (H2O2). Hydrogen Peroxide 107-124 cytochrome c, somatic Homo sapiens 4-9 23618181-5 2013 The Cyt c/GNPs/PANS modified electrode gives an improved electrocatalytic activity toward the reduction of hydrogen peroxide (H2O2). Hydrogen Peroxide 126-130 cytochrome c, somatic Homo sapiens 4-9 23598212-4 2013 Direct electron transfer of Cyt c and the electro-catalytic activity towards the reduction of H2O2 were also achieved. Hydrogen Peroxide 94-98 cytochrome c, somatic Homo sapiens 28-33 22492663-5 2012 In MTS-P5 cells challenged with H(2)O(2) treatment, PARP was still activated, whereas release of cytochrome c or apoptosis-inducing factor and intramitochondrial superoxide generation were suppressed. Hydrogen Peroxide 32-40 cytochrome c, somatic Homo sapiens 97-109 22757651-5 2012 The levels of p-JNK (Thr183/Tyr185) and cytochrome c in cytosol and BAX in heavy membrane (HM), respectively, were increased at 0.5 h and reached the peak at 12 h after stimulation with hydrogen peroxide. Hydrogen Peroxide 186-203 cytochrome c, somatic Homo sapiens 40-52 23429294-3 2013 Here, we evaluate the ability of E2 to modulate the intracellular NGB localization and the NGB interaction with mitochondrial cytochrome c following the H(2)O(2)-induced toxicity. Hydrogen Peroxide 153-161 cytochrome c, somatic Homo sapiens 126-138 23429294-8 2013 As a whole, these data demonstrate that the interception of the intrinsic apoptotic pathway into mitochondria (i.e., the prevention of cytochrome c release) is one of the pivotal mechanisms underlying E2-dependent NGB neuroprotection against H(2)O(2) toxicity. Hydrogen Peroxide 242-250 cytochrome c, somatic Homo sapiens 135-147 23597989-1 2013 We report on a new approach for the electrochemical detection of hydrogen peroxide (H2O2) based on Cytochrome C (Cyt c) immobilized ionic liquid (IL)-functionalized multi-walled carbon nanotubes (MWCNTs) modified glass carbon electrode (GCE). Hydrogen Peroxide 65-82 cytochrome c, somatic Homo sapiens 99-111 23597989-1 2013 We report on a new approach for the electrochemical detection of hydrogen peroxide (H2O2) based on Cytochrome C (Cyt c) immobilized ionic liquid (IL)-functionalized multi-walled carbon nanotubes (MWCNTs) modified glass carbon electrode (GCE). Hydrogen Peroxide 65-82 cytochrome c, somatic Homo sapiens 113-118 23597989-1 2013 We report on a new approach for the electrochemical detection of hydrogen peroxide (H2O2) based on Cytochrome C (Cyt c) immobilized ionic liquid (IL)-functionalized multi-walled carbon nanotubes (MWCNTs) modified glass carbon electrode (GCE). Hydrogen Peroxide 84-88 cytochrome c, somatic Homo sapiens 99-111 23597989-1 2013 We report on a new approach for the electrochemical detection of hydrogen peroxide (H2O2) based on Cytochrome C (Cyt c) immobilized ionic liquid (IL)-functionalized multi-walled carbon nanotubes (MWCNTs) modified glass carbon electrode (GCE). Hydrogen Peroxide 84-88 cytochrome c, somatic Homo sapiens 113-118 23597989-3 2013 Amperometry was used to evaluate the catalytic activity of the cyt c towards H2O2. Hydrogen Peroxide 77-81 cytochrome c, somatic Homo sapiens 63-68 23085196-0 2013 Cytochrome c produces pores in cardiolipin-containing planar bilayer lipid membranes in the presence of hydrogen peroxide. Hydrogen Peroxide 104-121 cytochrome c, somatic Homo sapiens 0-12 23085196-1 2013 Interaction of cytochrome c with cardiolipin in the presence of hydrogen peroxide induces peroxidase activity in cytochrome c and the ability to oxidize membrane lipids. Hydrogen Peroxide 64-81 cytochrome c, somatic Homo sapiens 15-27 23085196-1 2013 Interaction of cytochrome c with cardiolipin in the presence of hydrogen peroxide induces peroxidase activity in cytochrome c and the ability to oxidize membrane lipids. Hydrogen Peroxide 64-81 cytochrome c, somatic Homo sapiens 113-125 23085196-4 2013 Cytochrome c interaction with cardiolipin-containing pBLM in the presence of hydrogen peroxide resulted in the dramatic increase of the conductance, pore production, their growth up to 3.5 nm diameter and subsequent membrane destruction. Hydrogen Peroxide 77-94 cytochrome c, somatic Homo sapiens 0-12 23483946-6 2013 Immunofluorescence and Western blotting showed that H2O2 treatment increased the levels of p-JAK2, p-STAT3, Cytochrome c, Bax and Caspase3 and decreased the levels of Bcl2, whereas melatonin treatment partially reversed these effects. Hydrogen Peroxide 52-56 cytochrome c, somatic Homo sapiens 108-120 22469952-7 2012 Curcumin (20 microM), bleomycin (400 microg/ml) and H2O2 (400 microM) incubation for 24 h decreased the viability of NTera-2 cells, and increased caspase-3, -8 and -9 activities, Bax and cytoplasmic cytochrome c levels and decreased Bcl-2 levels. Hydrogen Peroxide 52-56 cytochrome c, somatic Homo sapiens 199-211 22507899-3 2012 The hallmark of cyt c with peroxidase activity is its partial unfolding accompanied by loosening of the Fe sixth axial bond and an enhanced access of the heme catalytic site to small molecules like H2O2. Hydrogen Peroxide 198-202 cytochrome c, somatic Homo sapiens 16-21 21545835-5 2011 Studies were performed to understand the related mechanisms of radical generation and NADH oxidation by Fe3+cyt c in the presence of H2O2. Hydrogen Peroxide 133-137 cytochrome c, somatic Homo sapiens 108-113 22197224-0 2012 Electrochemical performance of gold nanoparticle-cytochrome c hybrid interface for H2O2 detection. Hydrogen Peroxide 83-87 cytochrome c, somatic Homo sapiens 49-61 22157762-6 2012 These observations demonstrate that mitochondrial import and direct electron transfer from cytochrome c to Rac1 modulates mitochondrial H(2)O(2) production in alveolar macrophages pulmonary fibrosis. Hydrogen Peroxide 136-144 cytochrome c, somatic Homo sapiens 91-103 22157762-4 2012 Furthermore, H(2)O(2) generation mediated by mitochondrial Rac1 requires electron transfer from cytochrome c to a cysteine residue on Rac1 (Cys-178). Hydrogen Peroxide 13-21 cytochrome c, somatic Homo sapiens 96-108 21697135-10 2011 When cells were pretreated with MTP-131, the H(2)O(2)-induced mitochondrial depolarization was prevented; intracellular ROS, LDH release, and apoptosis were significantly decreased; release of cytochrome c from mitochondria to cytoplasm and activation of caspase 3 were inhibited. Hydrogen Peroxide 45-53 cytochrome c, somatic Homo sapiens 193-205 21545835-9 2011 The amount of superoxide radical adduct formed from the oxidation of NADH by the peroxidase activity of Fe3+cyt c increased with NADH and H2O2 concentration. Hydrogen Peroxide 138-142 cytochrome c, somatic Homo sapiens 108-113 21545835-11 2011 A UV-visible spectroscopic study shows that Fe3+cyt c is reduced in the presence of both NADH and H2O2. Hydrogen Peroxide 98-102 cytochrome c, somatic Homo sapiens 48-53 20817949-0 2010 Rate of oxidative modification of cytochrome c by hydrogen peroxide is modulated by Hofmeister anions. Hydrogen Peroxide 50-67 cytochrome c, somatic Homo sapiens 34-46 21297919-8 2011 This suggests that protective effects of vitamin E homologues against tetralinoleoyl cardiolipin peroxidation catalyzed by cytochrome c/hydrogen peroxide are realized largely due to their effects on the peroxidase activity of cytochrome c towards tetralinoleoyl cardiolipin rather than via their scavenging activity. Hydrogen Peroxide 136-153 cytochrome c, somatic Homo sapiens 123-135 21297919-8 2011 This suggests that protective effects of vitamin E homologues against tetralinoleoyl cardiolipin peroxidation catalyzed by cytochrome c/hydrogen peroxide are realized largely due to their effects on the peroxidase activity of cytochrome c towards tetralinoleoyl cardiolipin rather than via their scavenging activity. Hydrogen Peroxide 136-153 cytochrome c, somatic Homo sapiens 226-238 20547138-3 2010 We found that cells treated with 200muM hydrogen peroxide (H(2)O(2)) for 24h exhibited decreased viability and became apoptotic with corresponding Bax up-regulation, Bcl-2 down-regulation, caspase 3 activation and mitochondrial cytochrome c leakage. Hydrogen Peroxide 40-57 cytochrome c, somatic Homo sapiens 228-240 21146631-0 2011 H(2)O(2) disposal in cardiolipin-enriched brain mitochondria is due to increased cytochrome c peroxidase activity. Hydrogen Peroxide 0-8 cytochrome c, somatic Homo sapiens 81-93 21146631-8 2011 Since free oxidized cyt c acquired peroxidase activity towards H(2)O(2) upon interaction with CL in vitro, a contribution of cyt c to H(2)O(2) disposal in mitochondria through CL conferred peroxidase activity is plausible. Hydrogen Peroxide 63-71 cytochrome c, somatic Homo sapiens 20-25 21241762-7 2011 Western blot data revealed that loganin inhibited the H(2)O(2)-induced up-regulation of cleaved poly (ADP-ribose) polymerase (PARP) and cleaved caspase-3, increased the H(2)O(2)-induced decrease in the Bcl-2/Bax ratio, and attenuated the H(2)O(2)-induced release of cytochrome c from mitochondria to the cytosol. Hydrogen Peroxide 54-62 cytochrome c, somatic Homo sapiens 266-278 20655899-7 2010 Additionally, we observed that H(2)O(2)-induced decrease of mitochondrial transmembrane potential, release of cytochrome c and increase of caspase-3 activation were alleviated by HGF pretreatment. Hydrogen Peroxide 31-39 cytochrome c, somatic Homo sapiens 110-122 20817949-6 2010 A minimalist scheme of the interaction of cyt c with hydrogen peroxide can be described by two steps: 1) interaction of hydrogen peroxide with heme iron forming the postulated ferryl intermediate, 2a) oxidation of another molecule of hydrogen peroxide and 2b) parallel oxidation of close amino acid residue(s) and/or heme. Hydrogen Peroxide 53-70 cytochrome c, somatic Homo sapiens 42-47 20817949-6 2010 A minimalist scheme of the interaction of cyt c with hydrogen peroxide can be described by two steps: 1) interaction of hydrogen peroxide with heme iron forming the postulated ferryl intermediate, 2a) oxidation of another molecule of hydrogen peroxide and 2b) parallel oxidation of close amino acid residue(s) and/or heme. Hydrogen Peroxide 120-137 cytochrome c, somatic Homo sapiens 42-47 20817949-6 2010 A minimalist scheme of the interaction of cyt c with hydrogen peroxide can be described by two steps: 1) interaction of hydrogen peroxide with heme iron forming the postulated ferryl intermediate, 2a) oxidation of another molecule of hydrogen peroxide and 2b) parallel oxidation of close amino acid residue(s) and/or heme. Hydrogen Peroxide 120-137 cytochrome c, somatic Homo sapiens 42-47 20817949-1 2010 Cytochrome c (cyt c) and other heme proteins are oxidatively modified in the presence of hydrogen peroxide in a concentration- and time-dependent manner. Hydrogen Peroxide 89-106 cytochrome c, somatic Homo sapiens 0-12 20817949-1 2010 Cytochrome c (cyt c) and other heme proteins are oxidatively modified in the presence of hydrogen peroxide in a concentration- and time-dependent manner. Hydrogen Peroxide 89-106 cytochrome c, somatic Homo sapiens 14-19 19347266-1 2010 It was found that the complex of cytochrome c (Cyt c) and hydrogen peroxide could significantly catalyze the chemiluminescence (CL) reaction from luminol-hydrogen peroxide, and a sensitive, rapid, and simple CL procedure was proposed for the determination of Cyt c in a flow injection system for the first time. Hydrogen Peroxide 58-75 cytochrome c, somatic Homo sapiens 33-45 20352475-10 2010 A mechanism for cyt c release independent of CL peroxidation by H(2)O(2) is feasible. Hydrogen Peroxide 64-72 cytochrome c, somatic Homo sapiens 16-21 20085765-3 2010 This effect was inhibited by overexpression of human Bcl-2, by silencing of cytochrome c, and by ablation of Bax/Bak, indicating that H(2)O(2)-induced apoptosis was mediated by the mitochondrial pathway in Jurkat cells. Hydrogen Peroxide 134-142 cytochrome c, somatic Homo sapiens 76-88 22833778-5 2010 Susceptibility of RPE cells to H(2)O(2) toxicity was determined by lactate dehydrogenase and cytochrome c release, as well as propidium iodide staining. Hydrogen Peroxide 31-39 cytochrome c, somatic Homo sapiens 93-105 20653507-5 2010 Cytochrome c showing peroxidase activity has non-native structure, and shows enhanced access of the heme catalytic site to small molecules, such as H(2)O(2). Hydrogen Peroxide 148-156 cytochrome c, somatic Homo sapiens 0-12 20398641-3 2010 In addition, when Cyt c was incubated with peroxidized PLPC, it was found to be able to decompose hydroperoxides of PLPC into hydroxides. Hydrogen Peroxide 98-112 cytochrome c, somatic Homo sapiens 18-23 20398641-5 2010 Even if it is known to preferentially interact with cardiolipin, this work shows that Cyt c is also able to interact with hydroperoxide species of non-anionic phospholipids. Hydrogen Peroxide 122-135 cytochrome c, somatic Homo sapiens 86-91 19347266-1 2010 It was found that the complex of cytochrome c (Cyt c) and hydrogen peroxide could significantly catalyze the chemiluminescence (CL) reaction from luminol-hydrogen peroxide, and a sensitive, rapid, and simple CL procedure was proposed for the determination of Cyt c in a flow injection system for the first time. Hydrogen Peroxide 58-75 cytochrome c, somatic Homo sapiens 47-52 19347266-1 2010 It was found that the complex of cytochrome c (Cyt c) and hydrogen peroxide could significantly catalyze the chemiluminescence (CL) reaction from luminol-hydrogen peroxide, and a sensitive, rapid, and simple CL procedure was proposed for the determination of Cyt c in a flow injection system for the first time. Hydrogen Peroxide 58-75 cytochrome c, somatic Homo sapiens 259-264 19347266-1 2010 It was found that the complex of cytochrome c (Cyt c) and hydrogen peroxide could significantly catalyze the chemiluminescence (CL) reaction from luminol-hydrogen peroxide, and a sensitive, rapid, and simple CL procedure was proposed for the determination of Cyt c in a flow injection system for the first time. Hydrogen Peroxide 154-171 cytochrome c, somatic Homo sapiens 33-45 19347266-1 2010 It was found that the complex of cytochrome c (Cyt c) and hydrogen peroxide could significantly catalyze the chemiluminescence (CL) reaction from luminol-hydrogen peroxide, and a sensitive, rapid, and simple CL procedure was proposed for the determination of Cyt c in a flow injection system for the first time. Hydrogen Peroxide 154-171 cytochrome c, somatic Homo sapiens 47-52 19347266-1 2010 It was found that the complex of cytochrome c (Cyt c) and hydrogen peroxide could significantly catalyze the chemiluminescence (CL) reaction from luminol-hydrogen peroxide, and a sensitive, rapid, and simple CL procedure was proposed for the determination of Cyt c in a flow injection system for the first time. Hydrogen Peroxide 154-171 cytochrome c, somatic Homo sapiens 259-264 19746447-6 2009 Sequentially, hydrogen peroxide decreased the mitochondrial membrane potential, but increased the levels of cytochrome c and caspase-3 activity. Hydrogen Peroxide 14-31 cytochrome c, somatic Homo sapiens 108-120 19264356-0 2009 Nanoporous gold film encapsulating cytochrome c for the fabrication of a H2O2 biosensor. Hydrogen Peroxide 73-77 cytochrome c, somatic Homo sapiens 35-47 19767621-4 2009 MT-III reduced the hydrogen peroxide- or DNA damage-induced effects on neuronal cells, including the cell death, the activation of caspase-3 and -9, and the release of mitochondrial cytochrome c to the cytoplasm in a dose-dependent manner. Hydrogen Peroxide 19-36 cytochrome c, somatic Homo sapiens 182-194 19683594-3 2009 We have previously observed that the mitochondrial protein, cytochrome c, is capable of catalyzing the formation of the prototypic arachidonoyl amino acid, arachidonoyl glycine, utilizing arachidonoyl CoA and glycine as substrates, in the presence of hydrogen peroxide. Hydrogen Peroxide 251-268 cytochrome c, somatic Homo sapiens 60-72 19430149-0 2009 Amperometric sensor for hydrogen peroxide based on immobilized cytochrome c on binary self-assembled monolayers. Hydrogen Peroxide 24-41 cytochrome c, somatic Homo sapiens 63-75 19430149-1 2009 A sensitive sensor for the determination of hydrogen peroxide (H(2)O(2)) was fabricated by immobilizing cytochrome c (cyt c) on binary self-assembled monolayers (SAMs) of 5-(1,2-dithiolan-3-yl)valeric acid (thioctic acid, T-COOH) and 5-(1,2-dithiolan-3-yl)valeramide (thioctic acid amide, T-NH(2)) on gold electrodes. Hydrogen Peroxide 44-61 cytochrome c, somatic Homo sapiens 104-116 19430149-1 2009 A sensitive sensor for the determination of hydrogen peroxide (H(2)O(2)) was fabricated by immobilizing cytochrome c (cyt c) on binary self-assembled monolayers (SAMs) of 5-(1,2-dithiolan-3-yl)valeric acid (thioctic acid, T-COOH) and 5-(1,2-dithiolan-3-yl)valeramide (thioctic acid amide, T-NH(2)) on gold electrodes. Hydrogen Peroxide 44-61 cytochrome c, somatic Homo sapiens 118-123 19290667-0 2009 Detection of extracellular H2O2 released from human liver cancer cells based on TiO2 nanoneedles with enhanced electron transfer of cytochrome c. Hydrogen Peroxide 27-31 cytochrome c, somatic Homo sapiens 132-144 19290667-4 2009 On the basis of these results, the cyt c-TiO(2) nanocomposits film is capable of sensing H(2)O(2) at a suitable potential, 0.0 V (vs Ag AgCl), where not only common anodic interferences like ascorbic acid, uric acid, 3,4-dihydroxyphenylacetic acid but also a cathodic interference, O(2), are effectively avoided. Hydrogen Peroxide 89-97 cytochrome c, somatic Homo sapiens 35-40 19087893-3 2009 In addition, controlled in situ provision with hydrogen peroxide was performed using [Cp(*)Rh(bpy)(H(2)O)](2+) resulting in improved CytC-catalyzed sulfoxidation of thioanisol This work represents the first step towards the direct-[Cp(*)Rh(bpy)(H(2)O)](2+) catalyzed regeneration of P450 monooxygenases and peroxidases. Hydrogen Peroxide 47-64 cytochrome c, somatic Homo sapiens 133-137 18983994-2 2009 It has been shown that phosphatidic acid (PA) and phosphatidylhydroxyacetone (PHA) were formed in the system under conditions where hydrogen peroxide favours a release of heme iron from cyt c. Hydrogen Peroxide 132-149 cytochrome c, somatic Homo sapiens 186-191 19302811-6 2009 Treatment with 4 mM of H(2)O(2) for 24 or 96 h caused increase in Bax (56%, 227%), cytochrome c (282%, 701%), Smac/DIABLO (155%, 260%), caspase-3 protease activity (51%, 141%), and nuclear and cytosolic p53 (719%, 1581%) levels in the myotubes. Hydrogen Peroxide 23-31 cytochrome c, somatic Homo sapiens 83-95 19223550-3 2009 We provide evidence that LY30-induced increase in intracellular H(2)O(2) up-regulates the expression of TRAIL receptors (DR4 and DR5) in SHEP-1 cells by activating mitogen-activated protein kinases, resulting in a significant amplification of TRAIL-mediated caspase-8 processing and activity, cytosolic translocation of cytochrome c, and cell death. Hydrogen Peroxide 64-72 cytochrome c, somatic Homo sapiens 320-332 19053260-5 2008 We demonstrate that NBD-CL forms high-affinity complexes with cyt c and blocks cyt c-catalyzed oxidation of several peroxidase substrates, cyt c self-oxidation, and, most importantly, inhibits cyt c-dependent oxidation of polyunsaturated tetralinoleoyl CL (TLCL) and accumulation of TLCL hydroperoxides. Hydrogen Peroxide 288-302 cytochrome c, somatic Homo sapiens 62-67 19655415-4 2009 Magnolol inhibited the generation of reactive oxygen species (ROS), loss of mitochondrial membrane potential (Delta psi m) and release of cytochrome c from mitochondria caused by H2O2 into cytosol in HLE B-3 cells. Hydrogen Peroxide 179-183 cytochrome c, somatic Homo sapiens 138-150 19053260-5 2008 We demonstrate that NBD-CL forms high-affinity complexes with cyt c and blocks cyt c-catalyzed oxidation of several peroxidase substrates, cyt c self-oxidation, and, most importantly, inhibits cyt c-dependent oxidation of polyunsaturated tetralinoleoyl CL (TLCL) and accumulation of TLCL hydroperoxides. Hydrogen Peroxide 288-302 cytochrome c, somatic Homo sapiens 79-84 19053260-5 2008 We demonstrate that NBD-CL forms high-affinity complexes with cyt c and blocks cyt c-catalyzed oxidation of several peroxidase substrates, cyt c self-oxidation, and, most importantly, inhibits cyt c-dependent oxidation of polyunsaturated tetralinoleoyl CL (TLCL) and accumulation of TLCL hydroperoxides. Hydrogen Peroxide 288-302 cytochrome c, somatic Homo sapiens 79-84 19053260-5 2008 We demonstrate that NBD-CL forms high-affinity complexes with cyt c and blocks cyt c-catalyzed oxidation of several peroxidase substrates, cyt c self-oxidation, and, most importantly, inhibits cyt c-dependent oxidation of polyunsaturated tetralinoleoyl CL (TLCL) and accumulation of TLCL hydroperoxides. Hydrogen Peroxide 288-302 cytochrome c, somatic Homo sapiens 79-84 18631371-5 2008 In addition, cytochrome-c from the mitochondria was observed in H(2)O(2)-treated IHOK and oral cancer cells, and this was accompanied by the activation of caspase-3 and -9. Hydrogen Peroxide 64-72 cytochrome c, somatic Homo sapiens 13-25 18681888-5 2008 Overexpression of Hsp105alpha and Hsp105beta suppressed the activation of caspase-3 and caspase-9 by preventing the release of cytochrome c from mitochondria in H2O2-treated cells. Hydrogen Peroxide 161-165 cytochrome c, somatic Homo sapiens 127-139 17986381-3 2008 Here we report that cytochrome c catalyzes the synthesis of N-arachidonoyl glycine (NAGly) from arachidonoyl coenzyme A and glycine in the presence of hydrogen peroxide. Hydrogen Peroxide 151-168 cytochrome c, somatic Homo sapiens 20-32 18447324-4 2008 Investigation of the electrocatalytic activity of the Cyt c-modified BDND electrode toward hydrogen peroxide (H2O2) revealed a rapid amperometric response (5 s). Hydrogen Peroxide 91-108 cytochrome c, somatic Homo sapiens 54-59 18447324-4 2008 Investigation of the electrocatalytic activity of the Cyt c-modified BDND electrode toward hydrogen peroxide (H2O2) revealed a rapid amperometric response (5 s). Hydrogen Peroxide 110-114 cytochrome c, somatic Homo sapiens 54-59 18284261-6 2008 The use of {P(2)W(18)O(62)(6-)/cyt c}n films to catalyze hydrogen peroxide reduction was demonstrated. Hydrogen Peroxide 57-74 cytochrome c, somatic Homo sapiens 31-36 18198913-4 2008 The potential of the Ag nanocoral electrodes is exemplified by the construction and characterization of a hydrogen peroxide amperometric sensor based on cytochrome c. Hydrogen Peroxide 106-123 cytochrome c, somatic Homo sapiens 153-165 18334937-10 2008 EGCG reduced the H(2)O(2)-induced generation of reactive oxygen species (ROS), the loss of mitochondrial membrane potential (Deltapsim), and the release of cytochrome c from the mitochondria into the cytosol. Hydrogen Peroxide 17-25 cytochrome c, somatic Homo sapiens 156-168 18371631-5 2007 The Cyt c/GNPs/Chit/MWNTs modified GC electrode gives an improved electrocatalytic activity towards the reduction of hydrogen peroxide (H2O2). Hydrogen Peroxide 117-134 cytochrome c, somatic Homo sapiens 4-9 17972915-6 2007 Erv1 also utilized molecular oxygen as an electron acceptor to generate hydrogen peroxide, which is subsequently reduced to water by cytochrome c peroxidase (Ccp1). Hydrogen Peroxide 72-89 cytochrome c, somatic Homo sapiens 133-145 18554536-4 2008 Nitration of cytochrome c by biological oxidants in vitro can be achieved via different mechanisms, which include reactions with peroxynitrite, nitrite plus hydrogen peroxide, and nitric oxide plus hydrogen peroxide, and result in a loss in its electron transport capacity and in a higher peroxidatic activity. Hydrogen Peroxide 157-174 cytochrome c, somatic Homo sapiens 13-25 18554536-4 2008 Nitration of cytochrome c by biological oxidants in vitro can be achieved via different mechanisms, which include reactions with peroxynitrite, nitrite plus hydrogen peroxide, and nitric oxide plus hydrogen peroxide, and result in a loss in its electron transport capacity and in a higher peroxidatic activity. Hydrogen Peroxide 198-215 cytochrome c, somatic Homo sapiens 13-25 18371631-5 2007 The Cyt c/GNPs/Chit/MWNTs modified GC electrode gives an improved electrocatalytic activity towards the reduction of hydrogen peroxide (H2O2). Hydrogen Peroxide 136-140 cytochrome c, somatic Homo sapiens 4-9 17896956-2 2007 The highest Melatonin concentrations are to be found in the mitochondria, and cytochrome c (cyt c) represents a Melatonin target, since Melatonin is able to oxidise organic molecules in the presence of physiological amounts of hydrogen peroxide (H(2)O(2)). Hydrogen Peroxide 227-244 cytochrome c, somatic Homo sapiens 78-90 17896956-2 2007 The highest Melatonin concentrations are to be found in the mitochondria, and cytochrome c (cyt c) represents a Melatonin target, since Melatonin is able to oxidise organic molecules in the presence of physiological amounts of hydrogen peroxide (H(2)O(2)). Hydrogen Peroxide 227-244 cytochrome c, somatic Homo sapiens 92-97 17504811-6 2007 H2O2 formation was paralleled by, and causally linked to, the loss of mitochondrial membrane potential associated with the mitochondrial release of cytochrome c and AIF, and with the mitochondrial accumulation of Bax. Hydrogen Peroxide 0-4 cytochrome c, somatic Homo sapiens 148-160 17537719-2 2007 Here we report that cytochrome c catalyzes the formation of oleoylglycine from oleoyl-CoA and glycine, in the presence of hydrogen peroxide. Hydrogen Peroxide 122-139 cytochrome c, somatic Homo sapiens 20-32 17537719-6 2007 The functional properties of the reaction closely resemble those observed for the ability of cytochrome c to mediate the synthesis of oleamide from oleoyl-CoA and ammonia, in the presence of hydrogen peroxide (Driscoll, W. J., Chaturvedi., S., and Mueller, G. P. (2007) J. Biol. Hydrogen Peroxide 191-208 cytochrome c, somatic Homo sapiens 93-105 17567446-6 2007 Platelet exposure to exogenous H(2)O(2) results in cytochrome c release and activation of caspases-9. Hydrogen Peroxide 31-39 cytochrome c, somatic Homo sapiens 51-63 17567446-7 2007 In addition, H(2)O(2) induces the activation of caspase-3 and PS exposure by a mechanism dependent on cytochrome c release and caspase-9 activation. Hydrogen Peroxide 13-21 cytochrome c, somatic Homo sapiens 102-114 17288462-8 2007 Fluorescence data obtained for mediated H2O2 turnover also indicated enzymatic activity specifically at photo-cross-linked cyt c structures. Hydrogen Peroxide 40-44 cytochrome c, somatic Homo sapiens 123-128 17276741-1 2007 The detoxifying function of cytochrome c to scavenge O2-* and H2O2 in mitochondria is confirmed experimentally. Hydrogen Peroxide 62-66 cytochrome c, somatic Homo sapiens 28-40 17105166-7 2006 The Cyt-c-DCH18C6 complex in IL provides remarkably high peroxidase activity compared with native Cyt-c, because of enhancement of the affinity for H2O2. Hydrogen Peroxide 148-152 cytochrome c, somatic Homo sapiens 4-9 17105166-7 2006 The Cyt-c-DCH18C6 complex in IL provides remarkably high peroxidase activity compared with native Cyt-c, because of enhancement of the affinity for H2O2. Hydrogen Peroxide 148-152 cytochrome c, somatic Homo sapiens 98-103 16921577-0 2006 Characterization of peroxide-bound heme species generated in the reaction of thermally tolerant cytochrome c552 with hydrogen peroxide. Hydrogen Peroxide 117-134 cytochrome c, somatic Homo sapiens 96-108 17056004-2 2006 The comparison of cytochrome c reduction with accompanying oxygen uptake revealed that hydrogen peroxide was produced within the thylakoid. Hydrogen Peroxide 87-104 cytochrome c, somatic Homo sapiens 18-30 17085975-0 2006 Oxidative modification of cytochrome c by hydrogen peroxide. Hydrogen Peroxide 42-59 cytochrome c, somatic Homo sapiens 26-38 17085975-2 2006 We have investigated the modification of cytochrome c by H2O2. Hydrogen Peroxide 57-61 cytochrome c, somatic Homo sapiens 41-53 17085975-3 2006 When cytochrome c was incubated with H2O2, oligomerization of the protein increased and the formation of carbonyl derivatives and dityrosine was stimulated. Hydrogen Peroxide 37-41 cytochrome c, somatic Homo sapiens 5-17 17056004-1 2006 Hydrogen peroxide production in isolated pea thylakoids was studied in the presence of cytochrome c to prevent disproportionation of superoxide radicals outside of the thylakoid membranes. Hydrogen Peroxide 0-17 cytochrome c, somatic Homo sapiens 87-99 17085975-6 2006 During incubation of deoxyribose with cytochrome c and H2O2, damage to the deoxyribose occurred in parallel with the release of iron from cytochrome c. Hydrogen Peroxide 55-59 cytochrome c, somatic Homo sapiens 138-150 17085975-7 2006 When cytochrome c that had been exposed to H2O2 was analyzed by amino acid analysis, the tyrosine, histidine and methionine residues proved to be particularly sensitive. Hydrogen Peroxide 43-47 cytochrome c, somatic Homo sapiens 5-17 17085975-8 2006 These results suggest that H2O2-mediated cytochrome c oligomerization is due to oxidative damage resulting from free radicals generated by a combination of the peroxidase activity of cytochrome c and the Fenton reaction of free iron released from the oxidatively-damaged protein. Hydrogen Peroxide 27-31 cytochrome c, somatic Homo sapiens 41-53 17085975-8 2006 These results suggest that H2O2-mediated cytochrome c oligomerization is due to oxidative damage resulting from free radicals generated by a combination of the peroxidase activity of cytochrome c and the Fenton reaction of free iron released from the oxidatively-damaged protein. Hydrogen Peroxide 27-31 cytochrome c, somatic Homo sapiens 183-195 16921577-2 2006 Cytochrome c552 (cyt c552), from Thermus thermophirus HB8, bearing a mutation to an alanine at Met69 (M69A) reacts with hydrogen peroxide (H(2)O(2)) to generate a detectable hydroperoxo-ferric heme ([Fe(3+)--OOH]) species at ambient temperature. Hydrogen Peroxide 120-137 cytochrome c, somatic Homo sapiens 0-12 16720736-1 2006 Iso-1-cytochrome c, as any other hemeprotein, is able to react with hydrogen peroxide and to engage in the peroxidase cycle. Hydrogen Peroxide 68-85 cytochrome c, somatic Homo sapiens 6-18 16889691-1 2006 To elaborate the peroxidase activity of cytochrome c in the generation of free radicals from H2O2, the mechanism of DNA cleavage mediated by the cytochrome c/H2O2 system was investigated. Hydrogen Peroxide 93-97 cytochrome c, somatic Homo sapiens 40-52 16889691-1 2006 To elaborate the peroxidase activity of cytochrome c in the generation of free radicals from H2O2, the mechanism of DNA cleavage mediated by the cytochrome c/H2O2 system was investigated. Hydrogen Peroxide 93-97 cytochrome c, somatic Homo sapiens 145-157 16889691-1 2006 To elaborate the peroxidase activity of cytochrome c in the generation of free radicals from H2O2, the mechanism of DNA cleavage mediated by the cytochrome c/H2O2 system was investigated. Hydrogen Peroxide 158-162 cytochrome c, somatic Homo sapiens 40-52 16889691-1 2006 To elaborate the peroxidase activity of cytochrome c in the generation of free radicals from H2O2, the mechanism of DNA cleavage mediated by the cytochrome c/H2O2 system was investigated. Hydrogen Peroxide 158-162 cytochrome c, somatic Homo sapiens 145-157 16889691-2 2006 When plasmid DNA was incubated with cytochrome c and H2O2, the cleavage of DNA was proportional to the cytochrome c and H2O2 concentrations. Hydrogen Peroxide 53-57 cytochrome c, somatic Homo sapiens 103-115 16889691-2 2006 When plasmid DNA was incubated with cytochrome c and H2O2, the cleavage of DNA was proportional to the cytochrome c and H2O2 concentrations. Hydrogen Peroxide 120-124 cytochrome c, somatic Homo sapiens 36-48 16889691-3 2006 Radical scavengers, such as azide, mannitol, and ethanol, significantly inhibited the cytochrome c/H2O2 system-mediated DNA cleavage. Hydrogen Peroxide 99-103 cytochrome c, somatic Homo sapiens 86-98 16889691-5 2006 Incubation of cytochrome c with H2O2 resulted in a time-dependent release of iron ions from the cytochrome c molecule. Hydrogen Peroxide 32-36 cytochrome c, somatic Homo sapiens 14-26 16889691-5 2006 Incubation of cytochrome c with H2O2 resulted in a time-dependent release of iron ions from the cytochrome c molecule. Hydrogen Peroxide 32-36 cytochrome c, somatic Homo sapiens 96-108 16690782-5 2006 Using low-temperature and ambient-temperature electron paramagnetic resonance spectroscopy of H(2)O(2)-induced protein-derived (tyrosyl) radicals and etoposide phenoxyl radicals, respectively, we established that cardiolipin peroxidation and etoposide oxidation by cytochrome c/cardiolipin complex takes place predominantly on protein-derived radicals of cytochrome c. Hydrogen Peroxide 94-102 cytochrome c, somatic Homo sapiens 265-277 16690782-5 2006 Using low-temperature and ambient-temperature electron paramagnetic resonance spectroscopy of H(2)O(2)-induced protein-derived (tyrosyl) radicals and etoposide phenoxyl radicals, respectively, we established that cardiolipin peroxidation and etoposide oxidation by cytochrome c/cardiolipin complex takes place predominantly on protein-derived radicals of cytochrome c. Hydrogen Peroxide 94-102 cytochrome c, somatic Homo sapiens 355-367 16889691-7 2006 Evidence that the iron-specific chelator, desferoxamine (DFX), prevented the DNA cleavage induced by the cytochrome c/H2O2 system supports this mechanism. Hydrogen Peroxide 118-122 cytochrome c, somatic Homo sapiens 105-117 16889691-8 2006 Thus we suggest that DNA cleavage is mediated via the generation of dOH by a combination of the peroxidase reaction of cytochrome c and the Fenton-like reaction of free iron ions released from oxidatively damaged cytochrome c in the cytochrome c/H2O2 system. Hydrogen Peroxide 246-250 cytochrome c, somatic Homo sapiens 213-225 16889691-8 2006 Thus we suggest that DNA cleavage is mediated via the generation of dOH by a combination of the peroxidase reaction of cytochrome c and the Fenton-like reaction of free iron ions released from oxidatively damaged cytochrome c in the cytochrome c/H2O2 system. Hydrogen Peroxide 246-250 cytochrome c, somatic Homo sapiens 213-225 16757556-4 2006 It was recently reported that H(2)O(2) generated by the respiratory chain of the mitochondrion can be efficiently destroyed by the cytochrome c-mediated electron-leak pathway where the electron of ferrocytochrome c migrates directly to H(2)O(2) instead of to cytochrome c oxidase. Hydrogen Peroxide 30-38 cytochrome c, somatic Homo sapiens 131-143 16757556-4 2006 It was recently reported that H(2)O(2) generated by the respiratory chain of the mitochondrion can be efficiently destroyed by the cytochrome c-mediated electron-leak pathway where the electron of ferrocytochrome c migrates directly to H(2)O(2) instead of to cytochrome c oxidase. Hydrogen Peroxide 30-38 cytochrome c, somatic Homo sapiens 202-214 16757556-4 2006 It was recently reported that H(2)O(2) generated by the respiratory chain of the mitochondrion can be efficiently destroyed by the cytochrome c-mediated electron-leak pathway where the electron of ferrocytochrome c migrates directly to H(2)O(2) instead of to cytochrome c oxidase. Hydrogen Peroxide 236-244 cytochrome c, somatic Homo sapiens 131-143 16757556-4 2006 It was recently reported that H(2)O(2) generated by the respiratory chain of the mitochondrion can be efficiently destroyed by the cytochrome c-mediated electron-leak pathway where the electron of ferrocytochrome c migrates directly to H(2)O(2) instead of to cytochrome c oxidase. Hydrogen Peroxide 236-244 cytochrome c, somatic Homo sapiens 202-214 16720736-6 2006 To demonstrate this hypothesis, a redox-inspired strategy was implemented until an iso-1-cytochrome c variant fully stable at catalytic concentrations of hydrogen peroxide was obtained. Hydrogen Peroxide 154-171 cytochrome c, somatic Homo sapiens 89-101 16605268-7 2006 We quantitatively characterized the activation of peroxidase activity of cyt c by CL and hydrogen peroxide. Hydrogen Peroxide 89-106 cytochrome c, somatic Homo sapiens 73-78 16543234-7 2006 In the presence of NO donors, H(2)O(2)-induced oligomeric forms of cyt c positively stained for 3-nitrotyrosine confirming the reactivity of NO toward tyrosyl radicals of cyt c. Hydrogen Peroxide 30-38 cytochrome c, somatic Homo sapiens 67-72 16543234-7 2006 In the presence of NO donors, H(2)O(2)-induced oligomeric forms of cyt c positively stained for 3-nitrotyrosine confirming the reactivity of NO toward tyrosyl radicals of cyt c. Hydrogen Peroxide 30-38 cytochrome c, somatic Homo sapiens 171-176 16687488-6 2006 The H2O2 production induced by antisense CK2alpha was associated with robust caspase-3 activity, nuclear factor-kappaB nuclear translocation, cytochrome c release, and subsequent DNA fragmentation in prostate cancer cells (ALVA-41 and PC-3). Hydrogen Peroxide 4-8 cytochrome c, somatic Homo sapiens 142-154 16605268-15 2006 This suggests that redistribution of CL in the mitochondrial membranes combined with increased production of H(2)O(2) can switch on the peroxidase activity of cyt c and CL oxidation in mitochondria-a required step in execution of apoptosis. Hydrogen Peroxide 109-117 cytochrome c, somatic Homo sapiens 159-164 16040185-8 2006 Enhanced peroxidase activity of nitrated cyt c was responsible for H2O2-induced oxidation of phospholipid membranes and H2O2/NO2--mediated nitration of other proteins. Hydrogen Peroxide 67-71 cytochrome c, somatic Homo sapiens 41-46 16951741-2 2006 The cytochrome c-catalyzed nitration of tyrosine occurred in proportion to the concentration of hydrogen peroxide, nitrite or cytochrome c. Hydrogen Peroxide 96-113 cytochrome c, somatic Homo sapiens 4-16 16951741-5 2006 The rate constant between cytochrome c and hydrogen peroxide within the pH range of 3-8 was the largest at pH 6 (37 degrees C). Hydrogen Peroxide 43-60 cytochrome c, somatic Homo sapiens 26-38 16951741-8 2006 At this pH, the UV as well as visible spectrum of cytochrome c was changed by nitrite, even in the presence of hydrogen peroxide, probably via the formation of a heme iron-nitric oxide complex. Hydrogen Peroxide 111-128 cytochrome c, somatic Homo sapiens 50-62 15949844-5 2006 Hydrogen peroxide production by mGPDH was highly activated by one-electron acceptor, potassium ferricyanide and it was depressed by inhibitors of mGPDH and by cytochrome c. Hydrogen Peroxide 0-17 cytochrome c, somatic Homo sapiens 159-171 16040185-8 2006 Enhanced peroxidase activity of nitrated cyt c was responsible for H2O2-induced oxidation of phospholipid membranes and H2O2/NO2--mediated nitration of other proteins. Hydrogen Peroxide 120-124 cytochrome c, somatic Homo sapiens 41-46 16852515-15 2005 By increasing the concentration of the spin trapping agent, 5,5-dimethyl-1-pyrroline N-oxide (DMPO) in ESR experiments, we showed that cyt c catalyzes a homolytic cleavage of the O-O bond of hydroperoxide and generates a protein cation radical (g = 2.00). Hydrogen Peroxide 191-204 cytochrome c, somatic Homo sapiens 135-140 15964518-7 2005 The H2O2-induced drop in mitochondrial membrane potential and release of cytochrome c were enhanced by calcitriol. Hydrogen Peroxide 4-8 cytochrome c, somatic Homo sapiens 73-85 15981996-3 2005 In mitochondria cytochrome c (cyt c) could represent a melatonin target since it has the capability to oxidize organic molecules in the presence of H2O2, and mitochondria are the main site of H2O2 production in nonphagocytic cells. Hydrogen Peroxide 148-152 cytochrome c, somatic Homo sapiens 16-28 15981996-3 2005 In mitochondria cytochrome c (cyt c) could represent a melatonin target since it has the capability to oxidize organic molecules in the presence of H2O2, and mitochondria are the main site of H2O2 production in nonphagocytic cells. Hydrogen Peroxide 148-152 cytochrome c, somatic Homo sapiens 30-35 15981996-3 2005 In mitochondria cytochrome c (cyt c) could represent a melatonin target since it has the capability to oxidize organic molecules in the presence of H2O2, and mitochondria are the main site of H2O2 production in nonphagocytic cells. Hydrogen Peroxide 192-196 cytochrome c, somatic Homo sapiens 16-28 15981996-3 2005 In mitochondria cytochrome c (cyt c) could represent a melatonin target since it has the capability to oxidize organic molecules in the presence of H2O2, and mitochondria are the main site of H2O2 production in nonphagocytic cells. Hydrogen Peroxide 192-196 cytochrome c, somatic Homo sapiens 30-35 15981996-7 2005 Given the high mitochondrial concentrations of both melatonin and cyt c as well as the continuous generation of H2O2 during respiration, it is entirely possible that mitochondrial cyt c-mediated oxidation of melatonin may be a plausible pathway of its biotransformation in vivo. Hydrogen Peroxide 112-116 cytochrome c, somatic Homo sapiens 180-185 16852515-16 2005 Possible mechanisms for MPS-cyt c catalytic oxidation of hydroperoxides and PAHs are proposed based on the spectroscopic characterizations of the systems. Hydrogen Peroxide 57-71 cytochrome c, somatic Homo sapiens 28-33 15234112-6 2004 Moreover a decrease in mitochondrial membrane potential (Deltapsi(m)), mitochondrial cytochrome c release, caspases activation and DNA fragmentation were largely induced by H2O2 and occurred in both cell lines. Hydrogen Peroxide 173-177 cytochrome c, somatic Homo sapiens 85-97 15876423-8 2005 Additionally, QE protects cells from H(2)O(2)-induced a decrease in the mitochondrial membrane potential and a release of cytochrome c from mitochondria to cytosol by DiOC6 and Western blotting assay, respectively. Hydrogen Peroxide 37-45 cytochrome c, somatic Homo sapiens 122-134 15912211-2 2005 The enhancement of the activity is due to the higher reaction rate of unfolded cytochrome c with hydrogen peroxide, which is the rate-determining step in the peroxidase cycle of cytochrome c (Gebicka, L., 2001, Res Chem Intermed 27, 717-23). Hydrogen Peroxide 97-114 cytochrome c, somatic Homo sapiens 79-91 15912211-2 2005 The enhancement of the activity is due to the higher reaction rate of unfolded cytochrome c with hydrogen peroxide, which is the rate-determining step in the peroxidase cycle of cytochrome c (Gebicka, L., 2001, Res Chem Intermed 27, 717-23). Hydrogen Peroxide 97-114 cytochrome c, somatic Homo sapiens 178-190 14761966-2 2004 Hydrogen peroxide induces a short-lived cyt c-derived tyrosyl radical as detected by the electron spin resonance (ESR) spin-trapping technique. Hydrogen Peroxide 0-17 cytochrome c, somatic Homo sapiens 40-45 15279902-5 2004 Pretreatment with LiCl or Wnt-3a conditioned medium completely inhibited H2O2-induced release of mitochondrial cytochrome c and DNA fragmentation. Hydrogen Peroxide 73-77 cytochrome c, somatic Homo sapiens 111-123 15094365-1 2004 Low (1 x 10(-9)M) concentrations of cytochrome c inhibit H2O2 production in cytochrome c-depleted mitochondria, purified succinate-cytochrome c reductase (SCR) and antimycin A inhibited cytochrome c-depleted HMP. Hydrogen Peroxide 57-61 cytochrome c, somatic Homo sapiens 36-48 15094365-1 2004 Low (1 x 10(-9)M) concentrations of cytochrome c inhibit H2O2 production in cytochrome c-depleted mitochondria, purified succinate-cytochrome c reductase (SCR) and antimycin A inhibited cytochrome c-depleted HMP. Hydrogen Peroxide 57-61 cytochrome c, somatic Homo sapiens 76-88 15094365-1 2004 Low (1 x 10(-9)M) concentrations of cytochrome c inhibit H2O2 production in cytochrome c-depleted mitochondria, purified succinate-cytochrome c reductase (SCR) and antimycin A inhibited cytochrome c-depleted HMP. Hydrogen Peroxide 57-61 cytochrome c, somatic Homo sapiens 76-88 15094365-1 2004 Low (1 x 10(-9)M) concentrations of cytochrome c inhibit H2O2 production in cytochrome c-depleted mitochondria, purified succinate-cytochrome c reductase (SCR) and antimycin A inhibited cytochrome c-depleted HMP. Hydrogen Peroxide 57-61 cytochrome c, somatic Homo sapiens 76-88 15051475-7 2004 The ability of 17beta-E2 to prevent H2O2-induced injury to several oxidant susceptible components of the cellular ATP generating machinery, including abundances of mitochondrial gene transcripts encoding respiratory chain subunits and cytochrome c, the glycolytic pathway enzyme, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and the energy-shuttling creatine kinase (CK) system, and mitochondrial membrane potential (deltapsi(m)) a measure of mitochondrial membrane integrity, were determined 3 hr after oxidative insult. Hydrogen Peroxide 36-40 cytochrome c, somatic Homo sapiens 235-247 15051475-8 2004 Northern blot analysis revealed H2O2-induced reductions in mitochondrial transcripts for nicotinamide adenine dinucleotide dehydrogenase (NADH) subunits 4 and 5 and cytochrome c. Hydrogen Peroxide 32-36 cytochrome c, somatic Homo sapiens 165-177 15094365-2 2004 At higher concentration (2 x 10(-6)M), cytochrome c eliminates pre-existed H2O2 if feeding electrons to it by succinate. Hydrogen Peroxide 75-79 cytochrome c, somatic Homo sapiens 39-51 15094365-6 2004 Similar results are obtained on the elimination of pre-existed H2O2 by cytochrome c. Hydrogen Peroxide 63-67 cytochrome c, somatic Homo sapiens 71-83 14761966-9 2004 The consumption of NO by cyt c was enhanced by addition of H(2)O(2) as verified by inhibition electrochemical detection using an NO electrode. Hydrogen Peroxide 59-67 cytochrome c, somatic Homo sapiens 25-30 14761966-10 2004 The rate of NO consumption in the system containing cyt c/NO/H(2)O(2) was decreased by the spin traps 5,5-dimethyl pyrroline N-oxide and MNP, suggesting NO trapping of the cyt c-derived tyrosyl radical. Hydrogen Peroxide 61-69 cytochrome c, somatic Homo sapiens 52-57 14761966-10 2004 The rate of NO consumption in the system containing cyt c/NO/H(2)O(2) was decreased by the spin traps 5,5-dimethyl pyrroline N-oxide and MNP, suggesting NO trapping of the cyt c-derived tyrosyl radical. Hydrogen Peroxide 61-69 cytochrome c, somatic Homo sapiens 172-177 15025923-10 2004 Cytochrome c/hydrogen peroxide could effectively oxidize purified PS but not phosphatidylcholine in a cell-free model system. Hydrogen Peroxide 13-30 cytochrome c, somatic Homo sapiens 0-12 14747474-1 2004 We studied the mechanism of intra-mitochondrial death initiator caspase-9 activation by a redox response, in which hydrogen peroxide (H(2)O(2)) caused a subtle decrease in the inner membrane potential (Deltapsim) with little evidence of cytochrome c release. Hydrogen Peroxide 115-132 cytochrome c, somatic Homo sapiens 237-249 14973069-4 2004 We provide evidence that exposure of human leukemia cells to low concentrations of RSV (4-8 micro M) inhibits caspase activation, DNA fragmentation, and translocation of cytochrome c induced by hydrogen peroxide or anticancer drugs C2, vincristine, and daunorubicin. Hydrogen Peroxide 194-211 cytochrome c, somatic Homo sapiens 170-182 15777015-1 2004 The release of cytochrome c from mitochondria during apoptosis results in the enhanced production of superoxide radicals, which are converted to H2O2 by Mn-superoxide dismutase. Hydrogen Peroxide 145-149 cytochrome c, somatic Homo sapiens 15-27 14757132-5 2004 In addition to the inhibition of lactate dehydrogenase (LDH) leakage, ebselen inhibited H(2)O(2)-induced cytochrome c release and caspase-3 activation and the resultant apoptosis in HUVECs. Hydrogen Peroxide 88-96 cytochrome c, somatic Homo sapiens 105-117 15777015-0 2004 Activation of cytochrome c to a peroxidase compound I-type intermediate by H2O2: relevance to redox signalling in apoptosis. Hydrogen Peroxide 75-79 cytochrome c, somatic Homo sapiens 14-26 14757132-9 2004 These findings suggest that ebselen attenuates H(2)O(2)-induced endothelial cell death through the inhibition of signaling pathways mediated by p38 MAP kinase, caspase-3, and cytochrome c release. Hydrogen Peroxide 47-55 cytochrome c, somatic Homo sapiens 175-187 14678790-0 2004 Cytochrome c: a catalyst and target of nitrite-hydrogen peroxide-dependent protein nitration. Hydrogen Peroxide 47-64 cytochrome c, somatic Homo sapiens 0-12 14678790-3 2004 We report herein a novel function for cytochrome c as a catalyst for nitrite (NO2-) and hydrogen peroxide (H2O2)-mediated nitration reactions. Hydrogen Peroxide 88-105 cytochrome c, somatic Homo sapiens 38-50 14678790-3 2004 We report herein a novel function for cytochrome c as a catalyst for nitrite (NO2-) and hydrogen peroxide (H2O2)-mediated nitration reactions. Hydrogen Peroxide 107-111 cytochrome c, somatic Homo sapiens 38-50 14678790-7 2004 Extensive tyrosine nitration of Mn-superoxide dismutase occurred when exposed to either cytochrome c or MPx-11 in the presence of H2O2 and NO2-, with no apparent decrease in catalytic activity. Hydrogen Peroxide 130-134 cytochrome c, somatic Homo sapiens 88-100 14654376-3 2003 Exposure of cultured myocytes to 100 micromol/l hydrogen peroxide (H(2)O(2)) increased the number of nuclei stained by the terminal deoxynucleotidyl transferase-mediated dUTP nick-end labeling technique as well as induced internucleosomal DNA fragmentation, loss of mitochondrial membrane potential, cytochrome c release into the cytosol, and activation of caspases-3 and -9, all of which are characteristics of apoptosis. Hydrogen Peroxide 48-65 cytochrome c, somatic Homo sapiens 300-312 14583346-9 2003 Redox catalytic involvement of cyt c in PS oxidation was further supported by our data demonstrating that: (i) specific interactions of cyt c with PS resulted in the formation of EPR-detectable protein-centered tyrosyl radicals of cyt c upon its interaction with H2O2 in the presence of PS-containing liposomes, and (ii) integration of cyt c into cytochrome c null (Cyt c -/-) cells or HL-60 cells specifically stimulates PS oxidation in the presence of H2O2 or t-BuOOH, respectively. Hydrogen Peroxide 263-267 cytochrome c, somatic Homo sapiens 136-141 14583346-9 2003 Redox catalytic involvement of cyt c in PS oxidation was further supported by our data demonstrating that: (i) specific interactions of cyt c with PS resulted in the formation of EPR-detectable protein-centered tyrosyl radicals of cyt c upon its interaction with H2O2 in the presence of PS-containing liposomes, and (ii) integration of cyt c into cytochrome c null (Cyt c -/-) cells or HL-60 cells specifically stimulates PS oxidation in the presence of H2O2 or t-BuOOH, respectively. Hydrogen Peroxide 263-267 cytochrome c, somatic Homo sapiens 31-36 14583346-9 2003 Redox catalytic involvement of cyt c in PS oxidation was further supported by our data demonstrating that: (i) specific interactions of cyt c with PS resulted in the formation of EPR-detectable protein-centered tyrosyl radicals of cyt c upon its interaction with H2O2 in the presence of PS-containing liposomes, and (ii) integration of cyt c into cytochrome c null (Cyt c -/-) cells or HL-60 cells specifically stimulates PS oxidation in the presence of H2O2 or t-BuOOH, respectively. Hydrogen Peroxide 263-267 cytochrome c, somatic Homo sapiens 136-141 14583346-9 2003 Redox catalytic involvement of cyt c in PS oxidation was further supported by our data demonstrating that: (i) specific interactions of cyt c with PS resulted in the formation of EPR-detectable protein-centered tyrosyl radicals of cyt c upon its interaction with H2O2 in the presence of PS-containing liposomes, and (ii) integration of cyt c into cytochrome c null (Cyt c -/-) cells or HL-60 cells specifically stimulates PS oxidation in the presence of H2O2 or t-BuOOH, respectively. Hydrogen Peroxide 263-267 cytochrome c, somatic Homo sapiens 136-141 14583346-9 2003 Redox catalytic involvement of cyt c in PS oxidation was further supported by our data demonstrating that: (i) specific interactions of cyt c with PS resulted in the formation of EPR-detectable protein-centered tyrosyl radicals of cyt c upon its interaction with H2O2 in the presence of PS-containing liposomes, and (ii) integration of cyt c into cytochrome c null (Cyt c -/-) cells or HL-60 cells specifically stimulates PS oxidation in the presence of H2O2 or t-BuOOH, respectively. Hydrogen Peroxide 263-267 cytochrome c, somatic Homo sapiens 347-359 14583346-9 2003 Redox catalytic involvement of cyt c in PS oxidation was further supported by our data demonstrating that: (i) specific interactions of cyt c with PS resulted in the formation of EPR-detectable protein-centered tyrosyl radicals of cyt c upon its interaction with H2O2 in the presence of PS-containing liposomes, and (ii) integration of cyt c into cytochrome c null (Cyt c -/-) cells or HL-60 cells specifically stimulates PS oxidation in the presence of H2O2 or t-BuOOH, respectively. Hydrogen Peroxide 263-267 cytochrome c, somatic Homo sapiens 366-371 14583346-9 2003 Redox catalytic involvement of cyt c in PS oxidation was further supported by our data demonstrating that: (i) specific interactions of cyt c with PS resulted in the formation of EPR-detectable protein-centered tyrosyl radicals of cyt c upon its interaction with H2O2 in the presence of PS-containing liposomes, and (ii) integration of cyt c into cytochrome c null (Cyt c -/-) cells or HL-60 cells specifically stimulates PS oxidation in the presence of H2O2 or t-BuOOH, respectively. Hydrogen Peroxide 454-458 cytochrome c, somatic Homo sapiens 31-36 14583346-9 2003 Redox catalytic involvement of cyt c in PS oxidation was further supported by our data demonstrating that: (i) specific interactions of cyt c with PS resulted in the formation of EPR-detectable protein-centered tyrosyl radicals of cyt c upon its interaction with H2O2 in the presence of PS-containing liposomes, and (ii) integration of cyt c into cytochrome c null (Cyt c -/-) cells or HL-60 cells specifically stimulates PS oxidation in the presence of H2O2 or t-BuOOH, respectively. Hydrogen Peroxide 454-458 cytochrome c, somatic Homo sapiens 136-141 14583346-9 2003 Redox catalytic involvement of cyt c in PS oxidation was further supported by our data demonstrating that: (i) specific interactions of cyt c with PS resulted in the formation of EPR-detectable protein-centered tyrosyl radicals of cyt c upon its interaction with H2O2 in the presence of PS-containing liposomes, and (ii) integration of cyt c into cytochrome c null (Cyt c -/-) cells or HL-60 cells specifically stimulates PS oxidation in the presence of H2O2 or t-BuOOH, respectively. Hydrogen Peroxide 454-458 cytochrome c, somatic Homo sapiens 136-141 14583346-9 2003 Redox catalytic involvement of cyt c in PS oxidation was further supported by our data demonstrating that: (i) specific interactions of cyt c with PS resulted in the formation of EPR-detectable protein-centered tyrosyl radicals of cyt c upon its interaction with H2O2 in the presence of PS-containing liposomes, and (ii) integration of cyt c into cytochrome c null (Cyt c -/-) cells or HL-60 cells specifically stimulates PS oxidation in the presence of H2O2 or t-BuOOH, respectively. Hydrogen Peroxide 454-458 cytochrome c, somatic Homo sapiens 136-141 12850239-9 2003 Taken together, these results suggest that Korean mistletoe lectin-II is a strong inducer of pro-oxidant generation such as H2O2, which mediates the JNK/SAPK activation, cytochrome c release, activation of caspase-9 and caspase 3-like protease, and PARP cleavage in human myeloleukemic U937 cells. Hydrogen Peroxide 124-128 cytochrome c, somatic Homo sapiens 170-182 12748170-0 2003 Evidence for the role of a peroxidase compound I-type intermediate in the oxidation of glutathione, NADH, ascorbate, and dichlorofluorescin by cytochrome c/H2O2. Hydrogen Peroxide 156-160 cytochrome c, somatic Homo sapiens 143-155 12867996-6 2003 On the other hand, while all apoptosis-inducing treatments and treatment with 2 mM H(2)O(2) caused Bax translocation from the cytosol to mitochondria as well as cytochrome c release from mitochondria to the cytosol, treatment with BSO plus cisplatin did not. Hydrogen Peroxide 83-91 cytochrome c, somatic Homo sapiens 161-173 12788227-9 2003 Addition of H(2)O(2) resulted in the release of cytochrome c to the cytosol, and an increase of caspase-3 activity and the expression of caspase-3 subunit. Hydrogen Peroxide 12-20 cytochrome c, somatic Homo sapiens 48-60 12358746-8 2002 Bax plus a BH3 domain peptide stimulate H2O2 production by brain mitochondria due to release of cytochrome c and this stimulation is insensitive to changes in membrane potential. Hydrogen Peroxide 40-44 cytochrome c, somatic Homo sapiens 96-108 12767915-3 2003 Administration of endothelin-1 inhibited the H(2)O(2)-induced release of cytochrome c from mitochondria to the cytosol in cardiac myocytes, indicating the involvement of the mitochondria-dependent pathway in the anti-apoptotic effect of endothelin-1. Hydrogen Peroxide 45-53 cytochrome c, somatic Homo sapiens 73-85 12871144-0 2003 Cytochrome C is a hydrogen peroxide scavenger in mitochondria. Hydrogen Peroxide 18-35 cytochrome c, somatic Homo sapiens 0-12 12615354-11 2003 (4) tPT inhibits cytochrome c oxidation by H(2)O(2), catalyzed by peroxidase. Hydrogen Peroxide 43-51 cytochrome c, somatic Homo sapiens 17-29 12589560-0 2003 Different pathways of radical translocation in yeast cytochrome c peroxidase and its W191F mutant on reaction with H(2)O(2) suggest an antioxidant role. Hydrogen Peroxide 115-123 cytochrome c, somatic Homo sapiens 53-65 12589560-9 2003 H(2)O(2)-dependent formation of CCP-cytochrome c heterodimers was observed for both CCP(MI) and W191F in the presence of ferricytochrome c, the oxidized form of CCP"s donor substrate. Hydrogen Peroxide 0-8 cytochrome c, somatic Homo sapiens 36-48 12435729-0 2003 Effect of cytochrome c on the generation and elimination of O2*- and H2O2 in mitochondria. Hydrogen Peroxide 69-73 cytochrome c, somatic Homo sapiens 10-22 12435729-6 2003 An alternative electron-leak pathway of the respiratory chain is suggested to explain how cytochrome c affects on the generation and elimination of O(2)(*) and H(2)O(2) in mitochondria. Hydrogen Peroxide 160-168 cytochrome c, somatic Homo sapiens 90-102 12435729-7 2003 Enough cytochrome c in the respiratory chain is needed for keeping O(2)(*) and H(2)O(2) at a lower physiological level. Hydrogen Peroxide 79-87 cytochrome c, somatic Homo sapiens 7-19 12500560-2 2002 Further exposure to the ultrasonic field leads to a reverse process of oxidation of the cytochrome c ferro form to the ferri form by hydrogen peroxides and organic peroxides. Hydrogen Peroxide 133-151 cytochrome c, somatic Homo sapiens 88-100 12358536-1 2002 Catalytic reduction of O(2) and H(2)O(2) by new synthetic analogues of the heme/Cu site in cytochrome c and ubiquinol oxidases has been studied in aqueous buffers. Hydrogen Peroxide 32-40 cytochrome c, somatic Homo sapiens 91-103 12177198-8 2002 In response to H2O2, there was cytochrome c release from mitochondria, caspase-3 activation, and apoptosis, all of which occurred earlier and to a much greater extent in rotenone-treated cells; caspase inhibition provided substantial protection. Hydrogen Peroxide 15-19 cytochrome c, somatic Homo sapiens 31-43 11859616-0 2001 [The role of released cytochrome C from mitochondria in the apoptosis of HUVECs induced by hydrogen peroxide]. Hydrogen Peroxide 91-108 cytochrome c, somatic Homo sapiens 22-34 11960609-2 2002 Exposure of the cells to 100 microM H(2)O(2) resulted in intracellular accumulation of peroxides, denaturation of cytochrome c that was identified in the mitochondria and cytosol, release of native cytochrome c to the cytosol and fall in mitochondrial membrane potential (DeltaPsi(m)). Hydrogen Peroxide 36-44 cytochrome c, somatic Homo sapiens 114-126 11960609-2 2002 Exposure of the cells to 100 microM H(2)O(2) resulted in intracellular accumulation of peroxides, denaturation of cytochrome c that was identified in the mitochondria and cytosol, release of native cytochrome c to the cytosol and fall in mitochondrial membrane potential (DeltaPsi(m)). Hydrogen Peroxide 36-44 cytochrome c, somatic Homo sapiens 198-210 11960609-3 2002 Loading of cells with ascorbic acid before exposure to H(2)O(2) resulted in a dose-dependent protective effect against: intracellular accumulation of peroxides, DeltaPsi(m) alteration, cytochrome c denaturation and release. Hydrogen Peroxide 55-63 cytochrome c, somatic Homo sapiens 185-197 11983422-0 2002 Reaction of hydrogen peroxide and peroxidase activity in carboxymethylated cytochrome c: spectroscopic and kinetic studies. Hydrogen Peroxide 12-29 cytochrome c, somatic Homo sapiens 75-87 11859616-1 2001 OBJECTIVE: To explore the role of mitochondria and from which released cytochrome C in the apoptosis of HUVECs induced by H2O2. Hydrogen Peroxide 122-126 cytochrome c, somatic Homo sapiens 71-83 11859616-10 2001 H2O2 could lead to the decrease of mitochondrial cytochrome C concentration, which in turn lead to the increase of cytoplasmic cytochrome C concentration. Hydrogen Peroxide 0-4 cytochrome c, somatic Homo sapiens 49-61 11859616-10 2001 H2O2 could lead to the decrease of mitochondrial cytochrome C concentration, which in turn lead to the increase of cytoplasmic cytochrome C concentration. Hydrogen Peroxide 0-4 cytochrome c, somatic Homo sapiens 127-139 11859616-13 2001 CONCLUSION: H2O2 could induce cytochrome C releasing to cytoplasma which lead to endothelial apoptosis. Hydrogen Peroxide 12-16 cytochrome c, somatic Homo sapiens 30-42 11522638-6 2001 Dose-dependent inhibition of polyamine oxidase, an enzyme that oxidizes acetylated polyamines generated by SSAT and releases toxic by-products such as H(2)O(2) and aldehydes, prevented cytochrome c release, caspase activation, and apoptosis. Hydrogen Peroxide 151-159 cytochrome c, somatic Homo sapiens 185-197 11708064-7 2001 The immobilized cytochrome-c column exhibited oxidation activity which catalyzed N-demethylation of N,N-dimethylaniline, codeine, and dihydrocodeine in the presence of hydrogen peroxide as an oxygenating agent. Hydrogen Peroxide 168-185 cytochrome c, somatic Homo sapiens 16-28 11500038-3 2001 Both hydrogen peroxide and superoxide were found to cause release of cytochrome c from the lipid encapsulated protein, which was detected from the distinct spectral changes due to the formation of the azide complex of cytochrome c in the solution. Hydrogen Peroxide 5-22 cytochrome c, somatic Homo sapiens 69-81 11500038-3 2001 Both hydrogen peroxide and superoxide were found to cause release of cytochrome c from the lipid encapsulated protein, which was detected from the distinct spectral changes due to the formation of the azide complex of cytochrome c in the solution. Hydrogen Peroxide 5-22 cytochrome c, somatic Homo sapiens 218-230 11454657-3 2001 Ibudilast inhibited the H(2)O(2)-induced cytochrome c release, caspase-3 activation, DNA ladder formation and nuclear condensation, suggesting its anti-apoptotic effect. Hydrogen Peroxide 24-32 cytochrome c, somatic Homo sapiens 41-53 11710803-1 2001 In aqueous solution, ascorbate potently prevents bleaching of cytochrome c on exposure to excess H2O2 or t-butyl hydroperoxide. Hydrogen Peroxide 97-101 cytochrome c, somatic Homo sapiens 62-74 11301060-5 2001 These drugs at high concentration (3-10 mM) inhibited in vitro aggregation of cytochrome c by hydrogen peroxide or that of alpha-synuclein by cytochrome c and hydrogen peroxide. Hydrogen Peroxide 94-111 cytochrome c, somatic Homo sapiens 78-90 11315194-10 2001 These observations indicate a direct relationship between hydrogen peroxide and the release of cytochrome c during apoptosis caused by actinomycin D, H7, and daunorubicin. Hydrogen Peroxide 58-75 cytochrome c, somatic Homo sapiens 95-107 10930323-1 2000 The interaction of hydrogen peroxide, ascorbate and microperoxidase-11 (MP11), a ferriheme undecapeptide derived from cytochrome c, has been investigated using spectrophotometry, oxymetry, electron paramagnetic resonance (EPR), and mass spectroscopy techniques. Hydrogen Peroxide 19-36 cytochrome c, somatic Homo sapiens 118-130 11245440-7 2001 Additional characterization of the signaling pathways for hydrogen peroxide-induced apoptosis in MLH1-proficient cells demonstrates the involvement of increased mitochondrial permeability, the release of cytochrome c, and caspase 3 activation. Hydrogen Peroxide 58-75 cytochrome c, somatic Homo sapiens 204-216 11016925-8 2001 Furthermore, cytochrome C release from isolated mitochondria induced by C2 was completely inhibited in the presence of scavengers of hydrogen peroxide. Hydrogen Peroxide 133-150 cytochrome c, somatic Homo sapiens 13-25 11016925-10 2001 Our data suggest a scenario where drug-induced hydrogen peroxide production induces intracellular acidification and release of cytochrome C, independent of the inner membrane pore, thereby creating an intracellular environment permissive for caspase activation. Hydrogen Peroxide 47-64 cytochrome c, somatic Homo sapiens 127-139 10770918-4 2000 The results also demonstrate that mitochondrial cytochrome c is released in the cellular response to H(2)O(2) and that this effect is mediated by a c-Abl-dependent mechanism. Hydrogen Peroxide 101-109 cytochrome c, somatic Homo sapiens 48-60 11196900-4 2000 Some of them catalyzed the oxidation of pinacyanol chloride with hydrogen peroxide in methanol and exhibited higher activities than unmodified cytochrome c and its poly(ethylene glycolated) derivative. Hydrogen Peroxide 65-82 cytochrome c, somatic Homo sapiens 143-155 10802222-4 2000 We also found that traces of hydroperoxides and a high concentration of the target unsaturated fatty acid (LA) needs to be present in a fatty acid mixture before the quasi-lipoxygenase activity of Cyt c becomes apparent. Hydrogen Peroxide 29-43 cytochrome c, somatic Homo sapiens 197-202 10854054-9 2000 Early apoptotic events, such as mitochondrial depolarization, cytochrome c release, and increased intracellular calcium, were demonstrated to be common to both caspase-dependent and -independent H2O2-induced apoptosis. Hydrogen Peroxide 195-199 cytochrome c, somatic Homo sapiens 62-74 10780923-0 2000 A cytochrome c variant resistant to heme degradation by hydrogen peroxide. Hydrogen Peroxide 56-73 cytochrome c, somatic Homo sapiens 2-14 10780923-2 2000 Like peroxidases, cytochrome c is inactivated by hydrogen peroxide. Hydrogen Peroxide 49-66 cytochrome c, somatic Homo sapiens 18-30 10780923-4 2000 RESULTS: Variants of the iso-1-cytochrome c were constructed by site-directed mutagenesis and were found to be more stable in the presence of hydrogen peroxide than the wild type. Hydrogen Peroxide 142-159 cytochrome c, somatic Homo sapiens 31-43 10802222-7 2000 However, we found that Cyt c catalyzed the reaction by which hydroperoxides degrade LA, and thus enhanced the LA-degrading activity of 12-LOX. Hydrogen Peroxide 61-75 cytochrome c, somatic Homo sapiens 23-28 10506125-6 1999 Hemin/hydrogen peroxide similarly induced aggregation of alpha-synuclein, and both cytochrome c/hydrogen peroxide- and hemin/hydrogen peroxide-induced aggregation of alpha-synuclein was partially inhibited by treatment with iron chelator deferoxisamine. Hydrogen Peroxide 96-113 cytochrome c, somatic Homo sapiens 83-95 10563795-8 1999 The mechanism takes into account the findings with mutant cytochrome c oxidases and explains the results of many recent experiments, including the effects of hydrogen peroxide. Hydrogen Peroxide 158-175 cytochrome c, somatic Homo sapiens 58-70 10506125-6 1999 Hemin/hydrogen peroxide similarly induced aggregation of alpha-synuclein, and both cytochrome c/hydrogen peroxide- and hemin/hydrogen peroxide-induced aggregation of alpha-synuclein was partially inhibited by treatment with iron chelator deferoxisamine. Hydrogen Peroxide 96-113 cytochrome c, somatic Homo sapiens 83-95 10506125-7 1999 This indicates that iron-catalyzed oxidative reaction mediated by cytochrome c/hydrogen peroxide might be critically involved in promoting alpha-synuclein aggregation. Hydrogen Peroxide 79-96 cytochrome c, somatic Homo sapiens 66-78 10029200-1 1999 Cytochrome c (cyt c) is found in the mitochondria of all mammalian cells where hydrogen peroxide is produced as a byproduct of the electron transport chain. Hydrogen Peroxide 79-96 cytochrome c, somatic Homo sapiens 0-12 10359739-7 1999 Furthermore, H2O2 elicited translocation of Bax and Bad from cytosol to mitochondria, where these factors formed heterodimers with Bcl-2, which was followed by the release of cytochrome c, activation of CPP32, and cleavage of poly(ADP-ribose) polymerase. Hydrogen Peroxide 13-17 cytochrome c, somatic Homo sapiens 175-187 10404259-1 1999 Cytochrome c peroxidase oxidises hydrogen peroxide using cytochrome c as the electron donor. Hydrogen Peroxide 33-50 cytochrome c, somatic Homo sapiens 0-12 10404259-1 1999 Cytochrome c peroxidase oxidises hydrogen peroxide using cytochrome c as the electron donor. Hydrogen Peroxide 33-50 cytochrome c, somatic Homo sapiens 57-69 9989825-4 1999 Hydrogen peroxide-treatment of T-cells resulted in the formation of mitochondrial permeability transition pores, a rapid decrease of the mitochondrial transmembrane potential delta psi(m) and the release of Cytochrome C. Hydrogen Peroxide 0-17 cytochrome c, somatic Homo sapiens 207-219 10029200-1 1999 Cytochrome c (cyt c) is found in the mitochondria of all mammalian cells where hydrogen peroxide is produced as a byproduct of the electron transport chain. Hydrogen Peroxide 79-96 cytochrome c, somatic Homo sapiens 14-19 7488137-2 1995 Using this and the H2O2-Cyt-c system, we proved that monoepoxide production from linoleic acid was due to hydroxy radical formation by the reaction of Cyt-c with H2O2 and not to the formation of other active oxygen species. Hydrogen Peroxide 162-166 cytochrome c, somatic Homo sapiens 151-156 9766529-8 1998 These results lead to a working hypothesis that arsenite-induced apoptosis is triggered by the generation of hydrogen peroxide through activation of flavoprotein-dependent superoxide-producing enzymes (such as NADPH oxidase), and hydrogen peroxide might play a role as a mediator to induce apoptosis through release of cytochrome c to cytosol, activation of CPP32 protease, and PARP degradation. Hydrogen Peroxide 109-126 cytochrome c, somatic Homo sapiens 319-331 9766529-8 1998 These results lead to a working hypothesis that arsenite-induced apoptosis is triggered by the generation of hydrogen peroxide through activation of flavoprotein-dependent superoxide-producing enzymes (such as NADPH oxidase), and hydrogen peroxide might play a role as a mediator to induce apoptosis through release of cytochrome c to cytosol, activation of CPP32 protease, and PARP degradation. Hydrogen Peroxide 230-247 cytochrome c, somatic Homo sapiens 319-331 9675879-2 1998 The initial reaction rate is linearly dependent on cytochrome c and H2O2 concentration; the reaction follows the Michaelis and Menten kinetics both for H2O2 and hydrogen donors. Hydrogen Peroxide 68-72 cytochrome c, somatic Homo sapiens 51-63 9675879-2 1998 The initial reaction rate is linearly dependent on cytochrome c and H2O2 concentration; the reaction follows the Michaelis and Menten kinetics both for H2O2 and hydrogen donors. Hydrogen Peroxide 152-156 cytochrome c, somatic Homo sapiens 51-63 7488137-1 1995 We established an effective monoepoxide-generating system by combining cytochrome-c (Cyt-c) with a hydrogen peroxide (H2O2)-generating system comprising hypoxanthine (HX), xanthine oxidase (XO) and superoxide dismutase (SOD; HX-XO-SOD-Cyt-c system). Hydrogen Peroxide 99-116 cytochrome c, somatic Homo sapiens 235-240 7488137-1 1995 We established an effective monoepoxide-generating system by combining cytochrome-c (Cyt-c) with a hydrogen peroxide (H2O2)-generating system comprising hypoxanthine (HX), xanthine oxidase (XO) and superoxide dismutase (SOD; HX-XO-SOD-Cyt-c system). Hydrogen Peroxide 118-122 cytochrome c, somatic Homo sapiens 235-240 7488137-2 1995 Using this and the H2O2-Cyt-c system, we proved that monoepoxide production from linoleic acid was due to hydroxy radical formation by the reaction of Cyt-c with H2O2 and not to the formation of other active oxygen species. Hydrogen Peroxide 19-23 cytochrome c, somatic Homo sapiens 24-29 7488137-2 1995 Using this and the H2O2-Cyt-c system, we proved that monoepoxide production from linoleic acid was due to hydroxy radical formation by the reaction of Cyt-c with H2O2 and not to the formation of other active oxygen species. Hydrogen Peroxide 19-23 cytochrome c, somatic Homo sapiens 151-156 9662447-0 1998 Cytochrome c release and caspase activation in hydrogen peroxide- and tributyltin-induced apoptosis. Hydrogen Peroxide 47-64 cytochrome c, somatic Homo sapiens 0-12 9662447-1 1998 The ability of H2O2 and tributyltin (TBT) to trigger pro-caspase activation via export of cytochrome c from mitochondria to the cytoplasm was investigated. Hydrogen Peroxide 15-19 cytochrome c, somatic Homo sapiens 90-102 9662447-2 1998 Treatment of Jurkat T lymphocytes with H2O2 resulted in the appearance of cytochrome c in the cytosol within 2 h. This was at least 1 h before caspase activation was observed. Hydrogen Peroxide 39-43 cytochrome c, somatic Homo sapiens 74-86 9662447-3 1998 TBT caused cytochrome c release already after 5 min, followed by caspase activation within 1 h. Measurement of mitochondrial membrane potential (delta psi(m)) showed that both H2O2 and TBT dissipated delta psi(m), but with different time courses. Hydrogen Peroxide 176-180 cytochrome c, somatic Homo sapiens 11-23 9662447-4 1998 TBT caused a concomitant loss of delta psi(m) and release of cytochrome c, whereas cytochrome c release and caspase activation preceded any apparent delta psi(m) loss in H2O2-treated cells. Hydrogen Peroxide 170-174 cytochrome c, somatic Homo sapiens 83-95 7811298-7 1994 The mitochondrial protein cytochrome c can also stimulate lipid peroxidation in the presence of H2O2. Hydrogen Peroxide 96-100 cytochrome c, somatic Homo sapiens 26-38 7493039-4 1995 Methemoglobin and cytochrome c decomposed hydrogen peroxide slower than microperoxidase but generated free radicals continuously. Hydrogen Peroxide 42-59 cytochrome c, somatic Homo sapiens 18-30 7759524-0 1995 Mechanism of radical production from the reaction of cytochrome c with organic hydroperoxides. Hydrogen Peroxide 79-93 cytochrome c, somatic Homo sapiens 53-65 7759524-5 1995 From these analyses, it was concluded that the alkoxyl radical of the hydroperoxide was the initial radical produced, presumably by homolytic scission of the O-O bond by ferric cytochrome c. Hydrogen Peroxide 70-83 cytochrome c, somatic Homo sapiens 177-189 7811298-10 1994 Since respiring mitochondria generate superoxide radicals and H2O2, catalysis of lipid peroxidation and of the formation of drug-derived radicals by cytochrome c could be a mechanism contributing to mitochondrial damage by drugs. Hydrogen Peroxide 62-66 cytochrome c, somatic Homo sapiens 149-161 8064115-2 1994 This method is based on the measurement of the oxidation rate of reduced cytochrome c by H2O2 in the presence of a mediator and permits the detection of H2O2 generation rates as low as 60 nM min-1. Hydrogen Peroxide 89-93 cytochrome c, somatic Homo sapiens 73-85 8180234-0 1994 Effects of cytochrome c on the oxidation of reduced cytochrome c oxidase by hydrogen peroxide. Hydrogen Peroxide 76-93 cytochrome c, somatic Homo sapiens 11-23 8180234-0 1994 Effects of cytochrome c on the oxidation of reduced cytochrome c oxidase by hydrogen peroxide. Hydrogen Peroxide 76-93 cytochrome c, somatic Homo sapiens 52-64 8180234-1 1994 The oxidation of the redox centres in reduced cytochrome c oxidase by hydrogen peroxide was studied by stopped-flow spectrophotometry in the absence and presence of reduced cytochrome c. Hydrogen Peroxide 70-87 cytochrome c, somatic Homo sapiens 46-58 8064115-2 1994 This method is based on the measurement of the oxidation rate of reduced cytochrome c by H2O2 in the presence of a mediator and permits the detection of H2O2 generation rates as low as 60 nM min-1. Hydrogen Peroxide 153-157 cytochrome c, somatic Homo sapiens 73-85 8385996-14 1993 A significant proportion of the H2O2 production utilizes electrons from cytochrome c in the lighter plasma membrane fractions. Hydrogen Peroxide 32-36 cytochrome c, somatic Homo sapiens 72-84 8377593-2 1993 This methodology utilizes a mixture of cytochrome c and luminol as post-column hydroperoxide group specific luminescent reagents. Hydrogen Peroxide 79-92 cytochrome c, somatic Homo sapiens 39-51 1328238-2 1992 It was found that EDTA was decarboxylated and that cytochrome c, nitro blue tetrazolium, ferric iron, and molecular oxygen were reduced in a reaction mixture containing LiPH2, H2O2, veratryl alcohol, and EDTA. Hydrogen Peroxide 176-180 cytochrome c, somatic Homo sapiens 51-63 1661698-2 1991 The reactions of hydroxyl radicals generated from FeII/H2O2 and CuII/H2O2 redox couples with a variety of proteins (BSA, histones, cytochrome c, lysozyme and protamine) have been investigated by e.s.r. Hydrogen Peroxide 69-73 cytochrome c, somatic Homo sapiens 131-143 1518531-4 1992 NADH-dependent H2O2 production (16 +/- 1 nmol min-1 (mg protein)-1) was confirmed using cytochrome c peroxidase. Hydrogen Peroxide 15-19 cytochrome c, somatic Homo sapiens 88-100 1317004-1 1992 The oxidation of NADH and accompanying reduction of oxygen to H2O2 stimulated by polyvanadate was markedly inhibited by SOD and cytochrome c. Hydrogen Peroxide 62-66 cytochrome c, somatic Homo sapiens 128-140 1317004-5 1992 In the presence of H2O2, all the forms of vanadate were able to oxidize reduced cytochrome c, which was sensitive to mannitol, tris and also catalase, indicating H2O2-dependent generation of hydroxyl radicals. Hydrogen Peroxide 19-23 cytochrome c, somatic Homo sapiens 80-92 1317004-5 1992 In the presence of H2O2, all the forms of vanadate were able to oxidize reduced cytochrome c, which was sensitive to mannitol, tris and also catalase, indicating H2O2-dependent generation of hydroxyl radicals. Hydrogen Peroxide 162-166 cytochrome c, somatic Homo sapiens 80-92 1654817-2 1991 With ferrocytochrome c, oxidation reactions were preceded by a lag phase corresponding to the H2O2-mediated oxidation of cytochrome c to the ferric state; no lag phase was observed with ferricytochrome c. However, brief preincubation of ferricytochrome c with H2O2 increased its catalytic activity prior to progressive inactivation and degradation. Hydrogen Peroxide 94-98 cytochrome c, somatic Homo sapiens 10-22 1654817-6 1991 Our results are consistent with an initial activation of cytochrome c by H2O2 to a catalytically more active species in which a high oxidation state of an oxo-heme complex mediates the oxidative reactions. Hydrogen Peroxide 73-77 cytochrome c, somatic Homo sapiens 57-69 1654818-0 1991 Cytochrome c-catalyzed membrane lipid peroxidation by hydrogen peroxide. Hydrogen Peroxide 54-71 cytochrome c, somatic Homo sapiens 0-12 1654818-1 1991 Cytochrome c(3+)-catalyzed peroxidation of phosphatidylcholine liposomes by hydrogen peroxide (H2O2) was indicated by the production of thiobarbituric acid reactive substances, oxygen consumption, and emission of spontaneous chemiluminescence. Hydrogen Peroxide 76-93 cytochrome c, somatic Homo sapiens 0-12 1654818-1 1991 Cytochrome c(3+)-catalyzed peroxidation of phosphatidylcholine liposomes by hydrogen peroxide (H2O2) was indicated by the production of thiobarbituric acid reactive substances, oxygen consumption, and emission of spontaneous chemiluminescence. Hydrogen Peroxide 95-99 cytochrome c, somatic Homo sapiens 0-12 1654818-6 1991 These results show that reaction of cytochrome c with H2O2 promotes membrane oxidation by more than one chemical mechanism, including formation of high oxidation states of iron at the cytochrome-heme and also by heme iron release at higher H2O2 concentrations. Hydrogen Peroxide 54-58 cytochrome c, somatic Homo sapiens 36-48 1654818-6 1991 These results show that reaction of cytochrome c with H2O2 promotes membrane oxidation by more than one chemical mechanism, including formation of high oxidation states of iron at the cytochrome-heme and also by heme iron release at higher H2O2 concentrations. Hydrogen Peroxide 240-244 cytochrome c, somatic Homo sapiens 36-48 1646752-4 1991 We have assessed how interaction of cyanide and hydrogen peroxide with cytochrome c can lead to further errors in the xanthine oxidase-cytochrome c assay for SOD. Hydrogen Peroxide 48-65 cytochrome c, somatic Homo sapiens 71-83 1646752-4 1991 We have assessed how interaction of cyanide and hydrogen peroxide with cytochrome c can lead to further errors in the xanthine oxidase-cytochrome c assay for SOD. Hydrogen Peroxide 48-65 cytochrome c, somatic Homo sapiens 135-147 1654817-0 1991 Cytochrome c-catalyzed oxidation of organic molecules by hydrogen peroxide. Hydrogen Peroxide 57-74 cytochrome c, somatic Homo sapiens 0-12 1654817-1 1991 Cytochrome c catalyzed the oxidation of various electron donors in the presence of hydrogen peroxide (H2O2), including 2-2"-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS), 4-aminoantipyrine (4-AP), and luminol. Hydrogen Peroxide 83-100 cytochrome c, somatic Homo sapiens 0-12 1654817-1 1991 Cytochrome c catalyzed the oxidation of various electron donors in the presence of hydrogen peroxide (H2O2), including 2-2"-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS), 4-aminoantipyrine (4-AP), and luminol. Hydrogen Peroxide 102-106 cytochrome c, somatic Homo sapiens 0-12 1663899-0 1991 Purification of cytochrome c peroxidase for monitoring H2O2 production. Hydrogen Peroxide 55-59 cytochrome c, somatic Homo sapiens 16-28 1663899-1 1991 One of the most precise methods of determining hydrogen peroxide (H2O2) formation by biological systems is based on measuring the rate of enzyme-substrate complex formation between H2O2 and cytochrome c peroxidase (CCP). Hydrogen Peroxide 47-64 cytochrome c, somatic Homo sapiens 190-202 1663899-1 1991 One of the most precise methods of determining hydrogen peroxide (H2O2) formation by biological systems is based on measuring the rate of enzyme-substrate complex formation between H2O2 and cytochrome c peroxidase (CCP). Hydrogen Peroxide 66-70 cytochrome c, somatic Homo sapiens 190-202 1663899-1 1991 One of the most precise methods of determining hydrogen peroxide (H2O2) formation by biological systems is based on measuring the rate of enzyme-substrate complex formation between H2O2 and cytochrome c peroxidase (CCP). Hydrogen Peroxide 181-185 cytochrome c, somatic Homo sapiens 190-202 1663899-8 1991 Cytochrome c not only introduces an artifact when determining PI, but is also may act as a hydrogen donor for CCP when monitoring H2O2 formation, thus decreasing the sensitivity of this method. Hydrogen Peroxide 130-134 cytochrome c, somatic Homo sapiens 0-12 2383696-2 1990 This system involved separation of phospholipids from LDL-total lipids with normal phase silica gel HPLC and post-column detection of hydroperoxide-dependent chemiluminescence produced by luminol oxidation during the reaction of hydroperoxide with cytochrome c-haeme. Hydrogen Peroxide 134-147 cytochrome c, somatic Homo sapiens 248-260 35620405-5 2022 In addition, NO.20 inhibited H2O2-induced mitochondrial dysfunctions: it alleviated mitochondrial membrane potential loss and cytochrome c release, decreased the Bax/Bcl-2 ratio, and reduced caspase-3 expression. Hydrogen Peroxide 29-33 cytochrome c, somatic Homo sapiens 126-138 34455147-4 2021 While Cyt c treated under mild conditions with hydrogen peroxide was preferentially degraded by the proteasome, NO2Y74- and NO2Y97-Cyt c species did not show an increased degradation rate with respect to native Cyt c. Hydrogen Peroxide 47-64 cytochrome c, somatic Homo sapiens 6-11 34821923-4 2021 As proof-of-concept a visible colorimetric read-out was shown using an enzyme, cytochrome c (reduced in 16 h), and the visualizing reagent 3,3",5,5"-tetramethylbenzidine (TMB) (oxidized in 2.5 h) for the detection of dithionite and hydrogen peroxide, respectively, without any external energy input. Hydrogen Peroxide 232-249 cytochrome c, somatic Homo sapiens 79-91 2801234-4 1989 In the CL-HPLC method, a cytochrome c-luminol mixture was used as a hydroperoxide-specific luminescent reagent, and the quantification of hydroperoxide was performed by detecting chemiluminescence due to the luminol oxidation caused by the oxidant produced during the lipid hydroperoxides with heme. Hydrogen Peroxide 68-81 cytochrome c, somatic Homo sapiens 25-37 2539579-7 1989 Treatment of colostrum with an enzymatic system (xanthine + xanthine oxidase) known to destroy ascorbate"s cytochrome c-reducing activity yielded paradoxical results, decreasing colostral cytochrome c reduction in a dose-related manner, while increasing its H2O2-depleting activity. Hydrogen Peroxide 258-262 cytochrome c, somatic Homo sapiens 188-200 2840965-5 1988 During the reaction of myeloperoxidase with H2O2, rapid reduction of added cytochrome c was observed. Hydrogen Peroxide 44-48 cytochrome c, somatic Homo sapiens 75-87 2535790-4 1989 This is interpreted as the effect of cytochrome c redox cycling by reaction with H2O2, modifying oxy-radical generation in the reaction medium. Hydrogen Peroxide 81-85 cytochrome c, somatic Homo sapiens 37-49 2828112-3 1988 In this report we demonstrate that the build up in concentration of H2O2 during most reactions in which superoxide anion is being produced is not enough to affect the rate of cytochrome c reduction. Hydrogen Peroxide 68-72 cytochrome c, somatic Homo sapiens 175-187 2853113-0 1988 Iron release from metmyoglobin, methaemoglobin and cytochrome c by a system generating hydrogen peroxide. Hydrogen Peroxide 87-104 cytochrome c, somatic Homo sapiens 51-63 2853113-1 1988 The reaction of H2O2 with resting metmyoglobin (MetMb), methaemoglobin (MetHb) and cytochrome-c (Cyt-c) was studied in the Soret and visible regions. Hydrogen Peroxide 16-20 cytochrome c, somatic Homo sapiens 83-95 2853113-1 1988 The reaction of H2O2 with resting metmyoglobin (MetMb), methaemoglobin (MetHb) and cytochrome-c (Cyt-c) was studied in the Soret and visible regions. Hydrogen Peroxide 16-20 cytochrome c, somatic Homo sapiens 97-102 2853113-4 1988 Cytochrome-c, methaemoglobin and metmyoglobin during interaction with H2O2 at a concentration of 200 microM release 40%, 20% and 3%, respectively, of molecular iron after 10 min. Hydrogen Peroxide 70-74 cytochrome c, somatic Homo sapiens 0-12 3040473-0 1987 A stopped-flow study of the reaction of cytochrome c peroxidase with hydroperoxides. Hydrogen Peroxide 69-83 cytochrome c, somatic Homo sapiens 40-52 2828540-0 1987 Hydroperoxide-dependent folic acid degradation by cytochrome c. Hydrogen Peroxide 0-13 cytochrome c, somatic Homo sapiens 50-62 2828540-1 1987 Folic acid is degraded by cytochrome c in the presence of hydrogen peroxide/tert-butyl hydroperoxide at the C9-N10 bond. Hydrogen Peroxide 58-75 cytochrome c, somatic Homo sapiens 26-38 3040473-1 1987 Transient kinetic measurements show that cytochrome c peroxidase reacts with excess of hydroperoxides to produce compound ES in two phases. Hydrogen Peroxide 87-101 cytochrome c, somatic Homo sapiens 41-53 2983613-4 1985 Similarly, depletion of the mitochondria of their cytochrome c also inhibited formation of H2O2, which was restored by addition of cytochrome c. Hydrogen Peroxide 91-95 cytochrome c, somatic Homo sapiens 50-62 3002276-1 1985 PGBx, a derivative of prostaglandin B1, stimulated the oxidation of cytochrome c in the presence of H2O2. Hydrogen Peroxide 100-104 cytochrome c, somatic Homo sapiens 68-80 3002276-3 1985 Depletion of H2O2 and oxidation of cytochrome c followed similar time courses, suggesting that H2O2 was consumed in the reaction. Hydrogen Peroxide 95-99 cytochrome c, somatic Homo sapiens 35-47 3002276-5 1985 Low concentrations of ethyl or t-butyl hydroperoxide initially stimulated the oxidation of cytochrome c; this stimulation disappeared before completion of the oxidation, but was restored when the hydroperoxide concentration was renewed, suggesting that these hydroperoxides were probably also consumed in the reaction. Hydrogen Peroxide 39-52 cytochrome c, somatic Homo sapiens 91-103 3002276-5 1985 Low concentrations of ethyl or t-butyl hydroperoxide initially stimulated the oxidation of cytochrome c; this stimulation disappeared before completion of the oxidation, but was restored when the hydroperoxide concentration was renewed, suggesting that these hydroperoxides were probably also consumed in the reaction. Hydrogen Peroxide 259-273 cytochrome c, somatic Homo sapiens 91-103 3002276-8 1985 This conformational change caused a shift of the Soret absorption peak from 410 to 406 nm and may be responsible for the enhanced oxidizability of the cytochrome c by H2O2. Hydrogen Peroxide 167-171 cytochrome c, somatic Homo sapiens 151-163 3002276-11 1985 Thus the inhibition of lipid peroxidation by cytochrome c and PGBx may involve either the removal of hydroperoxides or deviation of electron transfer away from the pathway for lipid peroxidation. Hydrogen Peroxide 101-115 cytochrome c, somatic Homo sapiens 45-57 3025026-0 1987 Oxidation of reduced cytochrome c by hydrogen peroxide. Hydrogen Peroxide 37-54 cytochrome c, somatic Homo sapiens 21-33 3000943-5 1985 Although H2O2 cannot be measured directly in the presence of cytochrome c because it is consumed in reoxidizing reduced cytochrome c, its presence can be detected indirectly by the ability of catalase to improve the apparent yield of reduced cytochrome c. Hydrogen Peroxide 9-13 cytochrome c, somatic Homo sapiens 61-73 3000943-5 1985 Although H2O2 cannot be measured directly in the presence of cytochrome c because it is consumed in reoxidizing reduced cytochrome c, its presence can be detected indirectly by the ability of catalase to improve the apparent yield of reduced cytochrome c. Hydrogen Peroxide 9-13 cytochrome c, somatic Homo sapiens 120-132 3000943-5 1985 Although H2O2 cannot be measured directly in the presence of cytochrome c because it is consumed in reoxidizing reduced cytochrome c, its presence can be detected indirectly by the ability of catalase to improve the apparent yield of reduced cytochrome c. Hydrogen Peroxide 9-13 cytochrome c, somatic Homo sapiens 120-132 3000943-6 1985 We found that the relative amounts of extracellular H2O2 and O2- that could be measured in the environment of stimulated neutrophils varied with the stimulus and that catalase protected reduced cytochrome c from H2O2 oxidation when some stimuli were used but not with others. Hydrogen Peroxide 212-216 cytochrome c, somatic Homo sapiens 194-206 2985578-2 1985 Cytochrome c peroxidase and cytochrome c form a noncovalent electron transfer complex in the course of the peroxidase-catalyzed reduction of H2O2. Hydrogen Peroxide 141-145 cytochrome c, somatic Homo sapiens 0-12 2985578-2 1985 Cytochrome c peroxidase and cytochrome c form a noncovalent electron transfer complex in the course of the peroxidase-catalyzed reduction of H2O2. Hydrogen Peroxide 141-145 cytochrome c, somatic Homo sapiens 28-40 2983613-4 1985 Similarly, depletion of the mitochondria of their cytochrome c also inhibited formation of H2O2, which was restored by addition of cytochrome c. Hydrogen Peroxide 91-95 cytochrome c, somatic Homo sapiens 131-143 2983016-0 1985 The degradation of cytochrome c by hydrogen peroxide. Hydrogen Peroxide 35-52 cytochrome c, somatic Homo sapiens 19-31 2983016-1 1985 Cytochrome c is degraded by a large excess of hydrogen peroxide, leading to opening of the heme porphyrin ring and loss of the Soret absorption bands. Hydrogen Peroxide 46-63 cytochrome c, somatic Homo sapiens 0-12 2983016-6 1985 The in vivo degradation of cytochrome c by excess hydrogen peroxide may interfere with respiration, accelerate aging, and enhance the metabolism of carcinogens. Hydrogen Peroxide 50-67 cytochrome c, somatic Homo sapiens 27-39 3013978-2 1985 In contrast, ferrocytochrome c is oxidized in the Fe-EDTA-H2O2 system, without loss of any cytochrome c. Hydrogen Peroxide 58-62 cytochrome c, somatic Homo sapiens 18-30 6328811-0 1984 The formation of the primary hydrogen peroxide compound (compound I) of Pseudomonas cytochrome c peroxidase as a function of pH. Hydrogen Peroxide 29-46 cytochrome c, somatic Homo sapiens 84-96 6091557-0 1984 Redox state of cytochrome c in the presence of the 6-hydroxydopamine/oxygen couple: oscillations dependent on the presence of hydrogen peroxide or superoxide. Hydrogen Peroxide 126-143 cytochrome c, somatic Homo sapiens 15-27 6331511-2 1984 The reactions between cytochrome c peroxidase and fluoride or hydrogen peroxide are not significantly affected by complex formation with cytochrome c. Hydrogen Peroxide 62-79 cytochrome c, somatic Homo sapiens 22-34 6732243-0 1984 An analysis of the H2O2-mediated crosslinking of lens crystallins catalyzed by the heme-undecapeptide from cytochrome c. Hydrogen Peroxide 19-23 cytochrome c, somatic Homo sapiens 107-119 6732243-2 1984 It has been demonstrated that activation of H2O2 to more-potent oxidant species via the heme-undecapeptide from cytochrome c produces alterations in lens crystallin polypeptides similar to the changes found in cataract. Hydrogen Peroxide 44-48 cytochrome c, somatic Homo sapiens 112-124 2987504-4 1985 Even in the absence of liposomes or proteoliposomes, a cytochrome c-induced breakdown of dye was observed in the presence of hydrogen peroxide. Hydrogen Peroxide 125-142 cytochrome c, somatic Homo sapiens 55-67 6328811-3 1984 However, there is a bell-shaped pH dependence for the overall catalytic reaction using H2O2 as oxidizing substrate and cytochrome c-551 as reducing substrate with maximum turnover rate of pH 6. Hydrogen Peroxide 87-91 cytochrome c, somatic Homo sapiens 119-131 6269604-0 1981 Chemiluminescence in the reaction of cytochrome c with hydrogen peroxide. Hydrogen Peroxide 55-72 cytochrome c, somatic Homo sapiens 37-49 6301376-1 1983 This work reveals two biochemical effects of hydrogen peroxide treatment on hemoglobin, myoglobin, and cytochrome c. Hydrogen Peroxide 45-62 cytochrome c, somatic Homo sapiens 103-115 6299288-0 1983 Reduction of cytochrome c by hydrogen peroxide and its inhibition by superoxide dismutase. Hydrogen Peroxide 29-46 cytochrome c, somatic Homo sapiens 13-25 6290481-0 1982 The cytochrome c peroxidase-catalyzed oxidation of ferrocytochrome c by hydrogen peroxide. Hydrogen Peroxide 72-89 cytochrome c, somatic Homo sapiens 4-16 6290481-2 1982 Initial velocities for the cytochrome c peroxidase-catalyzed oxidation of ferrocytochrome c by hydrogen peroxide have been measured as functions of both the ferrocytochrome c (0.27-104 microM) and hydrogen peroxide (0.25-200 microM) concentrations at 25 degrees C, 0.01 M ionic strength, and pH 7 in a cacodylate/KNO3 buffer system Eadie-Hofstee plots of the initial velocity as a function of ferrocytochrome c concentration at constant hydrogen peroxide are nonlinear. Hydrogen Peroxide 95-112 cytochrome c, somatic Homo sapiens 27-39 6290481-2 1982 Initial velocities for the cytochrome c peroxidase-catalyzed oxidation of ferrocytochrome c by hydrogen peroxide have been measured as functions of both the ferrocytochrome c (0.27-104 microM) and hydrogen peroxide (0.25-200 microM) concentrations at 25 degrees C, 0.01 M ionic strength, and pH 7 in a cacodylate/KNO3 buffer system Eadie-Hofstee plots of the initial velocity as a function of ferrocytochrome c concentration at constant hydrogen peroxide are nonlinear. Hydrogen Peroxide 197-214 cytochrome c, somatic Homo sapiens 27-39 6290481-2 1982 Initial velocities for the cytochrome c peroxidase-catalyzed oxidation of ferrocytochrome c by hydrogen peroxide have been measured as functions of both the ferrocytochrome c (0.27-104 microM) and hydrogen peroxide (0.25-200 microM) concentrations at 25 degrees C, 0.01 M ionic strength, and pH 7 in a cacodylate/KNO3 buffer system Eadie-Hofstee plots of the initial velocity as a function of ferrocytochrome c concentration at constant hydrogen peroxide are nonlinear. Hydrogen Peroxide 197-214 cytochrome c, somatic Homo sapiens 27-39 6284205-0 1982 Cytochrome c oxidase binding of hydrogen peroxide. Hydrogen Peroxide 32-49 cytochrome c, somatic Homo sapiens 0-12 6284205-1 1982 Oxidized cytochrome c oxidase can bind hydrogen peroxide, as evidenced by changes in its spectrum and its ability to use hydrogen peroxide as an electron acceptor in cytochrome c oxidation. Hydrogen Peroxide 39-56 cytochrome c, somatic Homo sapiens 9-21 6284205-1 1982 Oxidized cytochrome c oxidase can bind hydrogen peroxide, as evidenced by changes in its spectrum and its ability to use hydrogen peroxide as an electron acceptor in cytochrome c oxidation. Hydrogen Peroxide 39-56 cytochrome c, somatic Homo sapiens 166-178 6284205-1 1982 Oxidized cytochrome c oxidase can bind hydrogen peroxide, as evidenced by changes in its spectrum and its ability to use hydrogen peroxide as an electron acceptor in cytochrome c oxidation. Hydrogen Peroxide 121-138 cytochrome c, somatic Homo sapiens 9-21 6284205-1 1982 Oxidized cytochrome c oxidase can bind hydrogen peroxide, as evidenced by changes in its spectrum and its ability to use hydrogen peroxide as an electron acceptor in cytochrome c oxidation. Hydrogen Peroxide 121-138 cytochrome c, somatic Homo sapiens 166-178 6307294-0 1983 The rapid H2O2-mediated nonphotodynamic crosslinking of lens crystallins generated by the heme-undecapeptide from cytochrome C: potential implications for cataractogenesis in man. Hydrogen Peroxide 10-14 cytochrome c, somatic Homo sapiens 114-126 6307294-2 1983 We report here that exposure of lens crystallin to H2O2 within the concentration range reported for human aqueous humor, produces crosslinking of crystallin polypeptides within 10 minutes in the presence of the heme-undecapeptide from cytochrome c. Hydrogen Peroxide 51-55 cytochrome c, somatic Homo sapiens 235-247 6307298-0 1983 The H2O2-mediated oxidation of NADPH to NADP+ catalyzed by the heme-undecapeptide from cytochrome C. Hydrogen Peroxide 4-8 cytochrome c, somatic Homo sapiens 87-99 6893995-8 1981 H2O2 production was markedly inhibited by superoxide dismutase or cytochrome c (scavengers of superoxide anion) but not by scavengers of singlet oxygen or hydroxyl radical. Hydrogen Peroxide 0-4 cytochrome c, somatic Homo sapiens 66-78 6269598-9 1981 Cytochrome c3 catalyzes the electrochemical reduction of molecular oxygen from the two-electron pathways via hydrogen peroxide to the four-electron pathway at the mercury electrode in neutral phosphate buffer solution. Hydrogen Peroxide 109-126 cytochrome c, somatic Homo sapiens 0-12 6258556-1 1980 The increase in light emission of hydroperoxide-supplemented cytochrome c observed on addition of lipid vesicles was related to the degree of unsaturation of the fatty acids of the phospholipids: dipalmitoyl phosphatidylcholine was without effect, whereas dioleoyl phosphatidylcholine and soya-bean phosphatidylcholine enhanced chemiluminescence 2- and 3-fold respectively. Hydrogen Peroxide 34-47 cytochrome c, somatic Homo sapiens 61-73 6253329-0 1980 Crosslinking of cytochrome c to peroxidase: covalent complex catalyzes oxidation of cytochrome c1 by H2O2. Hydrogen Peroxide 101-105 cytochrome c, somatic Homo sapiens 16-28 6258556-5 1980 Chemiluminescence of lipid vesicles supplemented with cytochrome c and hydroperoxide showed similar kinetic patterns with H2O2 and primary (ethyl) and tertiary (t-butyl and cumene) hydroperoxides. Hydrogen Peroxide 122-126 cytochrome c, somatic Homo sapiens 54-66 6248357-0 1980 Low level chemiluminescence of the cytochrome c-catalyzed decomposition of hydrogen peroxide. Hydrogen Peroxide 75-92 cytochrome c, somatic Homo sapiens 35-47 6250533-0 1980 Low-level chemiluminescence of hydroperoxide-supplemented cytochrome c. Hydrogen Peroxide 31-44 cytochrome c, somatic Homo sapiens 58-70 6250533-4 1980 Hydroperoxide-supplemented ferricytochrome c consumed O(2) at a rate of 1.0mumol/min per mumol of cytochrome c; the rate of O(2) uptake was linearly related to the concentration of cytochrome c. Hydrogen Peroxide 0-13 cytochrome c, somatic Homo sapiens 32-44 6250533-4 1980 Hydroperoxide-supplemented ferricytochrome c consumed O(2) at a rate of 1.0mumol/min per mumol of cytochrome c; the rate of O(2) uptake was linearly related to the concentration of cytochrome c. Hydrogen Peroxide 0-13 cytochrome c, somatic Homo sapiens 98-110 184842-6 1976 The proportion of the cytochrome c which is reduced during the second stage is oxidizable by either nitrate or H2O2 and is reduced again when the nitrate or H2O2 have been depleted. Hydrogen Peroxide 111-115 cytochrome c, somatic Homo sapiens 22-34 199157-7 1977 In the presence of H(2)O(2), human neutrophil myeloperoxidase oxidized ferrocytochrome c. Thus, in the cytochrome c assay for superoxide dismutase, the oxidation of ferrocytochrome c by myeloperoxidase mimicked the inhibition of reduction of ferricytochrome c by superoxide dismutase. Hydrogen Peroxide 19-27 cytochrome c, somatic Homo sapiens 76-88 190225-4 1977 The inhibition of cytochrome c reduction by catalase led us to explore the possibility that H2O2 might reduce oxidized cytochrome c at pH 9. Hydrogen Peroxide 92-96 cytochrome c, somatic Homo sapiens 18-30 190225-4 1977 The inhibition of cytochrome c reduction by catalase led us to explore the possibility that H2O2 might reduce oxidized cytochrome c at pH 9. Hydrogen Peroxide 92-96 cytochrome c, somatic Homo sapiens 119-131 190225-5 1977 We show that H2O2 does reduce oxidized cytochrome c at that pH but not at pH 7. Hydrogen Peroxide 13-17 cytochrome c, somatic Homo sapiens 39-51 190225-7 1977 These experiments serve to confirm our interpretation of the effect of catalase on the reduction of oxidized cytochrome c in the photolytic experiments, thus establishing that H2O2 was also formed. Hydrogen Peroxide 176-180 cytochrome c, somatic Homo sapiens 109-121 215951-0 1978 Application of the cytochrome c adjective reaction to the histochemical demonstration of sulfated mucopolysaccharides--with special reference to leucopatent blue-hydrogen peroxide as substrates. Hydrogen Peroxide 162-179 cytochrome c, somatic Homo sapiens 19-31 184842-6 1976 The proportion of the cytochrome c which is reduced during the second stage is oxidizable by either nitrate or H2O2 and is reduced again when the nitrate or H2O2 have been depleted. Hydrogen Peroxide 157-161 cytochrome c, somatic Homo sapiens 22-34 184842-7 1976 We conclude that the observed two-stage reduction of cytochrome c results from the presence of an oxidant, probably H2O2, produced by reaction of formate dehydrogenase with O2. Hydrogen Peroxide 116-120 cytochrome c, somatic Homo sapiens 53-65 238609-0 1975 A kinetic study of the endogenous reduction of the oxidized sites in the primary cytochrome c peroxidase-hydrogen peroxide compound. Hydrogen Peroxide 105-122 cytochrome c, somatic Homo sapiens 81-93 238609-1 1975 The primatry compound formed in the reaction between H2O2 and cytochrome c peroxidase is oxidized two equivalents above the native enzyme. Hydrogen Peroxide 53-57 cytochrome c, somatic Homo sapiens 62-74 4368557-0 1974 Cytochrome c peroxidase catalyzed oxidation of ferrocyanide by hydrogen peroxide. Hydrogen Peroxide 63-80 cytochrome c, somatic Homo sapiens 0-12 4368558-0 1974 Cytochrome c peroxidase catalyzed oxidation of ferrocyanide by hydrogen peroxide. Hydrogen Peroxide 63-80 cytochrome c, somatic Homo sapiens 0-12 5575162-0 1971 Consecutive oxidation and reduction of cytochrome c in the presence of hydrogen peroxide and copper histidine. Hydrogen Peroxide 71-88 cytochrome c, somatic Homo sapiens 39-51 5366837-0 1969 Chemiluminescence in reactions of cytochrome c and haematin with hydrogen peroxide. Hydrogen Peroxide 65-82 cytochrome c, somatic Homo sapiens 34-46 18907696-0 1947 A polarographic study on the catalytic effect of the catalase, peroxidase and cytochrome C ferments on the cathodic reduction of hydrogen peroxide. Hydrogen Peroxide 129-146 cytochrome c, somatic Homo sapiens 78-90 166656-2 1975 A number of reagents, some of which are electronic analogs of hydrogen peroxide, will replace it in the reactions of cytochrome c peroxidase. Hydrogen Peroxide 62-79 cytochrome c, somatic Homo sapiens 117-129 33567991-6 2021 Compared with vehicle-treated aged hMSCs (Vehicle-OMSCs),SRT1720-OMSCs showed alleviated apoptosis level, significantly decreased caspase-3 and caspase-9 activation, and reduced release of cytochrome c when subjected to H2O2 treatment. Hydrogen Peroxide 220-224 cytochrome c, somatic Homo sapiens 189-201 33354856-8 2021 These results suggest that cytochrome c blocks p14-3-3iota so as to inhibit caspase-like proteases, which in turn promote cell death upon H2 O2 -treatment. Hydrogen Peroxide 138-143 cytochrome c, somatic Homo sapiens 27-39 34000512-5 2021 We demonstrate that SARS-Cov-2 spike protein peptide 674-685 competes with the antibody against 179-190 fragment of alpha7 nAChR subunit for the binding to alpha7-expressing cells and mitochondria and prevents the release of cytochrome c from isolated mitochondria in response to 0.5 mM H2O2 but does not protect intact U373 cells against apoptogenic effect of H2O2. Hydrogen Peroxide 287-291 cytochrome c, somatic Homo sapiens 225-237 34000512-5 2021 We demonstrate that SARS-Cov-2 spike protein peptide 674-685 competes with the antibody against 179-190 fragment of alpha7 nAChR subunit for the binding to alpha7-expressing cells and mitochondria and prevents the release of cytochrome c from isolated mitochondria in response to 0.5 mM H2O2 but does not protect intact U373 cells against apoptogenic effect of H2O2. Hydrogen Peroxide 361-365 cytochrome c, somatic Homo sapiens 225-237 32898419-7 2020 Meanwhile, the radioexcited conduction band electrons react with high-level H2O2 within cancer cells to yield more ROS, and the secondary electrons are trapped by H2O molecules to produce hydrated electrons capable of reducing highly oxidized species such as cytochrome c. Hydrogen Peroxide 76-80 cytochrome c, somatic Homo sapiens 259-271 33529629-0 2021 Early modification of cytochrome c by hydrogen peroxide triggers its fast degradation. Hydrogen Peroxide 38-55 cytochrome c, somatic Homo sapiens 22-34 33529629-2 2021 Incubation of cyt c with an excess of hydrogen peroxide leads to a suicide inactivation of the protein, which is accompanied by heme destruction and covalent modification of numerous amino acid residues. Hydrogen Peroxide 38-55 cytochrome c, somatic Homo sapiens 14-19 33529629-3 2021 Although steady-state reactions of cyt c with an excess of hydrogen peroxide represent non-physiological conditions, they might be used for analysis of the first-modified amino acid in in vivo. Hydrogen Peroxide 59-76 cytochrome c, somatic Homo sapiens 35-40 33529629-6 2021 Analysis of a size of folded fraction of cyt c upon limited incubation with hydrogen peroxide indicates that the early oxidation of amino acids triggers an accelerated destruction of cyt c. Hydrogen Peroxide 76-93 cytochrome c, somatic Homo sapiens 41-46 33529629-6 2021 Analysis of a size of folded fraction of cyt c upon limited incubation with hydrogen peroxide indicates that the early oxidation of amino acids triggers an accelerated destruction of cyt c. Hydrogen Peroxide 76-93 cytochrome c, somatic Homo sapiens 183-188 33545736-7 2021 Additionally, the distributions of Bax, Bcl-xL, and cytochrome c mediated by H2O2 in the mitochondria and the cytosol were also modulated by PCA treatment. Hydrogen Peroxide 77-81 cytochrome c, somatic Homo sapiens 52-64 33147521-7 2020 Stimulating apoptosis of U373 cells by H2O2 disrupted alpha7-VDAC complexes and favored formation of alpha7-Bax complexes accompanied by cytochrome c release from mitochondria. Hydrogen Peroxide 39-43 cytochrome c, somatic Homo sapiens 137-149 32780285-9 2020 Eventually, the relative proteins expression levels of p53, cleaved caspase-9/3, cytochrome c, Fas-L, Fas, FADD and caspase-8 were substantially up-regulated in H2O2-triggered HepG2 cells, and Bax/Bcl-2 ratio and the relative protein expression levels of PARP were dramatically down-regulated. Hydrogen Peroxide 161-165 cytochrome c, somatic Homo sapiens 81-93 32706242-6 2020 Furthermore, the Cyt c worked normally under hypoxia conditions and could decompose H2O2 to O2 (with peroxidase-/catalase-like activity), resulting in synergistically improved therapeutic efficiency. Hydrogen Peroxide 84-88 cytochrome c, somatic Homo sapiens 17-22 31180563-8 2019 H2O2 increased the reactive oxygen species and malondialdehyde levels in C2C12 myoblasts, which was caused by mitochondrial dysfunction, decreased expression of cytochrome c and apoptosis-inducing factor from cytosolic and mitochondrial fractions, and activated expression of caspase-3 and caspase-9; however, treatment with baicalin reversed these effects. Hydrogen Peroxide 0-4 cytochrome c, somatic Homo sapiens 161-173 32781572-6 2020 S47E Cytc also resulted in lower cell death upon H2O2 treatment. Hydrogen Peroxide 49-53 cytochrome c, somatic Homo sapiens 5-9 31060395-12 2019 The inhibitory effect of DPHC on H2O2-induced apoptosis was associated with a reduced Bax/Bcl-2 ratio, the protection of the activation of caspase-9 and -3 and the inhibition of poly (ADP-ribose) polymerase cleavage, which was associated with the blockage of cytochrome c release to the cytoplasm. Hydrogen Peroxide 33-37 cytochrome c, somatic Homo sapiens 259-271 32529856-3 2022 An electrochemical, enzymatic biosensor based on cytochrome c (cyt c) was selected to measure reactive oxygen species (ROS), including hydrogen peroxide and super oxides, due to the stability of signal over time. Hydrogen Peroxide 135-152 cytochrome c, somatic Homo sapiens 49-61 32529856-3 2022 An electrochemical, enzymatic biosensor based on cytochrome c (cyt c) was selected to measure reactive oxygen species (ROS), including hydrogen peroxide and super oxides, due to the stability of signal over time. Hydrogen Peroxide 135-152 cytochrome c, somatic Homo sapiens 63-68 32402583-9 2020 Additionally, an intracellular calcium rise and subsequent mitochondrial membrane potential collapse, P53 phosphorylation, reduced BcL-2/Bax ratio in the mitochondrial membrane, release cytochrome c from mitochondria, leading to the subsequent activation of caspase 3 activation by H2O2 were all markedly suppressed in the presence of luteolin. Hydrogen Peroxide 282-286 cytochrome c, somatic Homo sapiens 186-198 31076999-5 2019 In addition, NGN inhibited H2O2-induced mitochondrial dysfunctions, including lowered membrane potential, decreased Bcl-2/Bax ratio, cytochrome c release, and the cleavage of caspase-3. Hydrogen Peroxide 27-31 cytochrome c, somatic Homo sapiens 133-145 31676852-5 2019 In vitro, COX activity, caspase-3 activity, and heme degradation in the presence of H2O2 were decreased with phosphomimetic Cytc compared to wild-type. Hydrogen Peroxide 84-88 cytochrome c, somatic Homo sapiens 124-128 30797456-3 2019 In this system, Cyt c was hydrolyzed by trypsin, and the resulting heme-peptide fragment exhibited peroxidase-like activity for catalytic decomposition of H2O2 into hydroxyl radical ( OH). Hydrogen Peroxide 155-159 cytochrome c, somatic Homo sapiens 16-21 30797456-8 2019 In addition, this strategy was successfully applied for quantitative detection of Cyt c in cell lysates of H2O2 or etoposide (anticancer drug)-induced apoptotic cells, providing great potential application for cell-based oxidation pressure determination and screening of anticancer drugs. Hydrogen Peroxide 107-111 cytochrome c, somatic Homo sapiens 82-87 30515391-4 2018 Further, SAC treatment dose dependently inhibited H2O2 induced apoptosis via decreasing the Bax/Bcl-2 ratio, restoring mitochondrial membrane potential ( Psim), inhibiting mitochondrial cytochrome c release, and inhibiting proteolytic cleavage of caspase-3. Hydrogen Peroxide 50-54 cytochrome c, somatic Homo sapiens 186-198 30541920-0 2019 Cytochrome c autocatalyzed carbonylation in the presence of hydrogen peroxide and cardiolipins. Hydrogen Peroxide 60-77 cytochrome c, somatic Homo sapiens 0-12 30541920-4 2019 Here, we examined the kinetics of the H2O2-mediated peroxidase activity of cyt c both in the presence and absence of tetraoleoyl cardiolipin (TOCL)- and tetralinoleoyl cardiolipin (TLCL)-containing liposomes to evaluate the role of cyt c-CL complex formation in the induction and stimulation of cyt c peroxidase activity. Hydrogen Peroxide 38-42 cytochrome c, somatic Homo sapiens 75-80 30541920-4 2019 Here, we examined the kinetics of the H2O2-mediated peroxidase activity of cyt c both in the presence and absence of tetraoleoyl cardiolipin (TOCL)- and tetralinoleoyl cardiolipin (TLCL)-containing liposomes to evaluate the role of cyt c-CL complex formation in the induction and stimulation of cyt c peroxidase activity. Hydrogen Peroxide 38-42 cytochrome c, somatic Homo sapiens 232-237 30541920-4 2019 Here, we examined the kinetics of the H2O2-mediated peroxidase activity of cyt c both in the presence and absence of tetraoleoyl cardiolipin (TOCL)- and tetralinoleoyl cardiolipin (TLCL)-containing liposomes to evaluate the role of cyt c-CL complex formation in the induction and stimulation of cyt c peroxidase activity. Hydrogen Peroxide 38-42 cytochrome c, somatic Homo sapiens 232-237 30585261-7 2018 The cGMP analog 8-Br-cGMP blocked H2O2-induced apoptotic cell death; reduction of caspase-3 enzyme, cytochrome c release, and caspase-8 and -9. Hydrogen Peroxide 34-38 cytochrome c, somatic Homo sapiens 100-112 29365138-6 2018 The NADPH-dependent reduction of cytochrome c or cytochrome b5 by purified Nox4 DH domain was found regulated by the H2O2 concentration, and C546L and C547L mutants showed lower rates of the hemeprotein reduction. Hydrogen Peroxide 117-121 cytochrome c, somatic Homo sapiens 33-45 29902531-8 2018 HE alleviated H2O2-induced loss of mitochondrial membrane potential (MMP), blocked the releases of cytochrome C and apoptosis inducing factor (AIF) from mitochondria, and thus inhibited mitochondria-mediated cell apoptosis. Hydrogen Peroxide 14-18 cytochrome c, somatic Homo sapiens 99-111 28322801-1 2018 Membrane-permeabilizing activity of cytochrome c (cyt c) in the presence of hydrogen peroxide associated with its functioning as peroxidase is considered relevant to initiation of the mitochondrial pathway of apoptosis. Hydrogen Peroxide 76-93 cytochrome c, somatic Homo sapiens 36-48 28322801-1 2018 Membrane-permeabilizing activity of cytochrome c (cyt c) in the presence of hydrogen peroxide associated with its functioning as peroxidase is considered relevant to initiation of the mitochondrial pathway of apoptosis. Hydrogen Peroxide 76-93 cytochrome c, somatic Homo sapiens 50-55 28322801-2 2018 Here, we present evidence that the choice of a fluorescent dye for measuring cyt c/H2O2-induced dye leakage from liposomes by fluorescence de-quenching is of major importance. Hydrogen Peroxide 83-87 cytochrome c, somatic Homo sapiens 77-82 28322801-5 2018 Based on the concentration dependences of the cyt c/H2O2-induced calcein leakage, the optimal conditions for the assay were found. Hydrogen Peroxide 52-56 cytochrome c, somatic Homo sapiens 46-51 29530984-3 2018 Herein, we report that cytochrome c, in the presence of either cardiolipin (CL), O2 and H2O2, or oxidized CL and O2, catalyzes the oxidation of the plasmalogen vinyl ether linkage, promoting its hydrolytic cleavage and resultant production of 2-AA-lysolipids and highly reactive alpha-hydroxy fatty aldehydes. Hydrogen Peroxide 88-92 cytochrome c, somatic Homo sapiens 23-35 29687711-6 2018 In addition, the Cyt c@ZIF-8/GO nanocomposites can be utilized up to four cycles with virtually no loss of activity and may be further applied on H2O2 biosensing systems. Hydrogen Peroxide 146-150 cytochrome c, somatic Homo sapiens 17-22 29048162-0 2017 Cytochrome c as a Peroxidase: Activation of the Precatalytic Native State by H2O2-Induced Covalent Modifications. Hydrogen Peroxide 77-81 cytochrome c, somatic Homo sapiens 0-12 29287127-0 2018 Cytochrome c Catalyzes the Hydrogen Peroxide-Assisted Oxidative Desulfuration of 2-Thiouridines in Transfer RNAs. Hydrogen Peroxide 27-44 cytochrome c, somatic Homo sapiens 0-12 29287127-7 2018 The cyt c/H2 O2 -mediated oxidative damage of S2U-tRNA may have biological relevance through alteration of the cellular functions of transfer RNA. Hydrogen Peroxide 10-15 cytochrome c, somatic Homo sapiens 4-9 29048162-1 2017 In addition to serving as respiratory electron shuttle, ferri-cytochrome c (cyt c) acts as a peroxidase; i.e., it catalyzes the oxidation of organic substrates by H2O2. Hydrogen Peroxide 163-167 cytochrome c, somatic Homo sapiens 62-74 26990284-5 2017 In response to several stimuli, p66Shc migrates into mitochondria where it catalyses electron transfer from cytochrome c to oxygen resulting in hydrogen peroxide formation. Hydrogen Peroxide 144-161 cytochrome c, somatic Homo sapiens 108-120 28411556-7 2017 In addition, H2O2, (100-1000microM) reduced the total AChE content and modified its isoform profile (mainly 50-, 70-, and 132-kDa) H2O2 from 100microM to 1000microM induced cytochrome c release confirming cell death by apoptosis. Hydrogen Peroxide 13-17 cytochrome c, somatic Homo sapiens 173-185 28398720-4 2017 Compared with native Cyt c, the immobilized Cyt c displayed increased apparent substrate affinity (Michaelis constant Km reduced by ~50%), ~128% increased enzymatic activity, and 1.4-fold increased sensitivity in the enzymatic electrochemical detection of H2O2. Hydrogen Peroxide 256-260 cytochrome c, somatic Homo sapiens 44-49 28611589-6 2017 Remarkably, a reduction in PGC-1alpha resulted in the reduction of mitochondrial membrane potential, intracellular ATP content and intracellular H2O2 generation, leading to the translocation of cytochrome c (cyt c) to the cytoplasm in the MPP+-induced PD cell model. Hydrogen Peroxide 145-149 cytochrome c, somatic Homo sapiens 194-206 28611589-6 2017 Remarkably, a reduction in PGC-1alpha resulted in the reduction of mitochondrial membrane potential, intracellular ATP content and intracellular H2O2 generation, leading to the translocation of cytochrome c (cyt c) to the cytoplasm in the MPP+-induced PD cell model. Hydrogen Peroxide 145-149 cytochrome c, somatic Homo sapiens 208-213 28398720-5 2017 The immobilized Cyt c-coated screen-printed electrode was applied for the fast detection of residual H2O2 in microliter food samples such as milk and beer, making it promising for the development of efficient biosensors. Hydrogen Peroxide 101-105 cytochrome c, somatic Homo sapiens 16-21 27624939-2 2016 p66 translocates to the mitochondria and oxidizes cytochrome c to yield H2O2, which in turn initiates cell death. Hydrogen Peroxide 72-76 cytochrome c, somatic Homo sapiens 50-62 26709389-0 2016 Sulfite Oxidase Activity of Cytochrome c: Role of Hydrogen Peroxide. Hydrogen Peroxide 50-67 cytochrome c, somatic Homo sapiens 28-40 27270708-3 2016 The above features resemble the naturally occurring enzyme cytochrome c peroxidase (CCP) which is known to catalytically oxidize Cyt(II) c in the presence of H2O2. Hydrogen Peroxide 158-162 cytochrome c, somatic Homo sapiens 59-71 26724537-3 2016 It was found that cyt c hardly catalyzes H2O2-mediated TMB oxidation to produce a blue solution. Hydrogen Peroxide 41-45 cytochrome c, somatic Homo sapiens 18-23 27186967-8 2016 IL-10 restored anti-apoptotic proteins expression and suppressed cytochrome c release in H2O2-induced apoptosis. Hydrogen Peroxide 89-93 cytochrome c, somatic Homo sapiens 65-77 26709389-13 2016 In addition, the amount of DMPO-SO3- formed by the peroxidase activity of Fe3+ cyt c also increased with sulfite and H2O2 concentration. Hydrogen Peroxide 117-121 cytochrome c, somatic Homo sapiens 79-84 26327303-1 2015 Herein, we report a novel method for H2O2 detection based on a single plasmonic nanoprobe via cytochrome c (Cyt c)-mediated plasmon resonance energy transfer (PRET). Hydrogen Peroxide 37-41 cytochrome c, somatic Homo sapiens 108-113 26881470-3 2016 The intermediate product O2 - from the hydrolysis of metal superoxides is converted by cytochrome c to O2 and by superoxide dismutase (SOD) to 1/2 mol O2 and 1/2 mol H2O2, which is then converted by catalase (CAT) to 1/2 mol O2. Hydrogen Peroxide 166-170 cytochrome c, somatic Homo sapiens 87-99 26327303-0 2015 A single nanoparticle-based sensor for hydrogen peroxide (H2O2) via cytochrome c-mediated plasmon resonance energy transfer. Hydrogen Peroxide 39-56 cytochrome c, somatic Homo sapiens 68-80 26327303-0 2015 A single nanoparticle-based sensor for hydrogen peroxide (H2O2) via cytochrome c-mediated plasmon resonance energy transfer. Hydrogen Peroxide 58-62 cytochrome c, somatic Homo sapiens 68-80 26769665-8 2016 In the H2O2-induced H9c2 cardiomyocytes, which mimicked the I/R injury in vivo, VEGF-C pre-treatment decreased the LDH release and MDA content, blocked H2O2-induced apoptosis by inhibiting the pro-apoptotic protein Bax expression and its translocation to the mitochondrial membrane, and consequently attenuated H2O2-induced decrease of mitochondrial membrane potential and increase of cytochrome c release from mitochondria. Hydrogen Peroxide 7-11 cytochrome c, somatic Homo sapiens 385-397 26884825-6 2015 The addition of H2O2 resulted in the release of cytochrome c to the cytosol, and an increase of Caspase-3 cleavage. Hydrogen Peroxide 16-20 cytochrome c, somatic Homo sapiens 48-60 26327303-1 2015 Herein, we report a novel method for H2O2 detection based on a single plasmonic nanoprobe via cytochrome c (Cyt c)-mediated plasmon resonance energy transfer (PRET). Hydrogen Peroxide 37-41 cytochrome c, somatic Homo sapiens 94-106 26327303-2 2015 Dynamic spectral changes were observed in the fingerprint quenching dip of a single plasmonic nanoprobe in response to changes in the redox state of Cyt c, induced by H2O2. Hydrogen Peroxide 167-171 cytochrome c, somatic Homo sapiens 149-154