PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25881547-7 2015 Because Ccp1 appears to sense ONOO(H) in cells, we examined its reaction with ONOO(H) in vitro and found that peroxynitrous acid (ONOOH) rapidly (k2>10(6)M(-1)s(-1)) oxidizes purified Ccp1 to an intermediate with spectral and ferrocytochrome-oxidizing properties indistinguishable from those of its well-characterized compound I formed with H2O2. Hydrogen Peroxide 344-348 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 8-12 30145880-2 2018 In vitro oxidation of recombinant Ccp1 by H2O2 in the absence of its reducing substrate, ferrocytochrome c, gives rise to similar proteoforms, indicating uncoupling of Ccp1 oxidation and reduction in mitochondria. Hydrogen Peroxide 42-46 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 34-38 30145880-5 2018 Moreover, a decrease in recombinant Ccp1 oxidation by H2O2 in vitro in the presence of glutathione supports a protective role for hole hopping to this antioxidant. Hydrogen Peroxide 54-58 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 36-40 26261310-9 2015 Thus, thiol peroxidase deficiency requires dosage compensation of CCP1 and UTH1 via chromosome XI aneuploidy, wherein these proteins support hydroperoxide removal with the reducing equivalents generated by the electron transport chain. Hydrogen Peroxide 141-154 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 66-70 26212209-1 2015 Previously, we constructed, expressed, and purified 46 charge-reversal mutants of yeast cytochrome c peroxidase (CcP) and determined their electronic absorption spectra, their reaction with H2O2, and their steady-state catalytic properties [ Pearl , N. M. et al. Hydrogen Peroxide 190-194 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 88-111 26212209-1 2015 Previously, we constructed, expressed, and purified 46 charge-reversal mutants of yeast cytochrome c peroxidase (CcP) and determined their electronic absorption spectra, their reaction with H2O2, and their steady-state catalytic properties [ Pearl , N. M. et al. Hydrogen Peroxide 190-194 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 113-116 25881547-0 2015 Peroxynitrite and hydrogen peroxide elicit similar cellular stress responses mediated by the Ccp1 sensor protein. Hydrogen Peroxide 18-35 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 93-97 25881547-4 2015 Previously, we reported that H2O2 challenge increases these activities in wild-type cells and in cells producing the hyperactive mutant H2O2 sensor Ccp1(W191F) but not in Ccp1-knockout cells (ccp1Delta). Hydrogen Peroxide 29-33 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 148-152 25881547-4 2015 Previously, we reported that H2O2 challenge increases these activities in wild-type cells and in cells producing the hyperactive mutant H2O2 sensor Ccp1(W191F) but not in Ccp1-knockout cells (ccp1Delta). Hydrogen Peroxide 136-140 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 148-152 28451256-0 2017 LC-MS/MS suggests that hole hopping in cytochrome c peroxidase protects its heme from oxidative modification by excess H2O2. Hydrogen Peroxide 119-123 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 39-62 28451256-1 2017 We recently reported that cytochrome c peroxidase (Ccp1) functions as a H2O2 sensor protein when H2O2 levels rise in respiring yeast. Hydrogen Peroxide 72-76 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 26-49 28451256-1 2017 We recently reported that cytochrome c peroxidase (Ccp1) functions as a H2O2 sensor protein when H2O2 levels rise in respiring yeast. Hydrogen Peroxide 72-76 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 51-55 28451256-1 2017 We recently reported that cytochrome c peroxidase (Ccp1) functions as a H2O2 sensor protein when H2O2 levels rise in respiring yeast. Hydrogen Peroxide 97-101 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 26-49 28451256-1 2017 We recently reported that cytochrome c peroxidase (Ccp1) functions as a H2O2 sensor protein when H2O2 levels rise in respiring yeast. Hydrogen Peroxide 97-101 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 51-55 28451256-2 2017 The availability of its reducing substrate, ferrocytochrome c (CycII), determines whether Ccp1 acts as a H2O2 sensor or peroxidase. Hydrogen Peroxide 105-109 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 90-94 28451256-3 2017 For H2O2 to serve as a signal it must modify its receptor so we employed high-performance LC-MS/MS to investigate in detail the oxidation of Ccp1 by 1, 5 and 10 M eq. of H2O2 in the absence of CycII to prevent peroxidase activity. Hydrogen Peroxide 4-8 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 141-145 28451256-3 2017 For H2O2 to serve as a signal it must modify its receptor so we employed high-performance LC-MS/MS to investigate in detail the oxidation of Ccp1 by 1, 5 and 10 M eq. of H2O2 in the absence of CycII to prevent peroxidase activity. Hydrogen Peroxide 170-174 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 141-145 28451256-4 2017 We observe strictly heme-mediated oxidation, implicating sequential cycles of binding and reduction of H2O2 at Ccp1"s heme. Hydrogen Peroxide 103-107 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 111-115 28451256-10 2017 This unprecedented analysis unveils the remarkable capacity of a polypeptide to direct hole hopping away from its active site, consistent with heme labilization being a key outcome of Ccp1-mediated H2O2 signaling. Hydrogen Peroxide 198-202 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 184-188 25422453-8 2014 We hypothesized that Ccp1"s heme is labilized by hyperoxidation of the protein during the burst in H2O2 production as cells begin to respire. Hydrogen Peroxide 99-103 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 21-25 25941976-2 2015 Both enzymes catalyze the peroxidation of cytochrome c. Like CcP, LmP reacts with H2O2 to form Compound I, which consists of a ferryl heme and a Trp radical, Fe(IV) O;Trp( +). Hydrogen Peroxide 82-86 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 61-64 25422453-9 2014 To test this hypothesis, recombinant Ccp1 was hyperoxidized with excess H2O2 in vitro, which accelerated heme transfer to apomyoglobin added as a surrogate heme acceptor. Hydrogen Peroxide 72-76 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 37-41 25422453-11 2014 We conclude that Ccp1 responds to respiration-derived H2O2 via a previously unidentified mechanism involving H2O2-activated heme transfer to apoCta1. Hydrogen Peroxide 54-58 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 17-21 25422453-11 2014 We conclude that Ccp1 responds to respiration-derived H2O2 via a previously unidentified mechanism involving H2O2-activated heme transfer to apoCta1. Hydrogen Peroxide 109-113 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 17-21 23832496-1 2013 Here we describe paramagnetic NMR analysis of the low- and high-spin forms of yeast cytochrome c peroxidase (CcP), a 34 kDa heme enzyme involved in hydroperoxide reduction in mitochondria. Hydrogen Peroxide 148-161 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 84-107 24382195-7 2014 In contrast, young ccp1(W191F) cells accumulate little H2O2, possess depressed Sod2 activity, enabling their O2( -) level to spike and deactivate aconitase, which, ultimately, leads to greater mitochondrial oxidative damage, early GSH depletion, and a shorter lifespan than wild-type cells. Hydrogen Peroxide 55-59 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 19-23 24964148-1 2014 Yeast cytochrome c peroxidase (CcP) is a heme enzyme that reduces hydroperoxides using the electrons provided by its physiological partner cytochrome c (Cc). Hydrogen Peroxide 66-80 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 6-29 24964148-1 2014 Yeast cytochrome c peroxidase (CcP) is a heme enzyme that reduces hydroperoxides using the electrons provided by its physiological partner cytochrome c (Cc). Hydrogen Peroxide 66-80 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 31-34 23831190-4 2013 Here we provide substantial biochemical evidence that the heme enzyme Ccp1 (cytochrome c peroxidase), which is targeted to the intermembrane space, functions primarily as a mitochondrial H2O2 sensing and signaling protein in Saccharomyces cerevisiae. Hydrogen Peroxide 187-191 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 70-74 23831190-5 2013 Key evidence for a sensing role for Ccp1 is the significantly higher H2O2 accumulation in ccp1-null cells(ccp1Delta) vs ccp1(W191F) cells producing the catalytically inactive Ccp1(W191F) variant. Hydrogen Peroxide 69-73 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 36-40 23831190-5 2013 Key evidence for a sensing role for Ccp1 is the significantly higher H2O2 accumulation in ccp1-null cells(ccp1Delta) vs ccp1(W191F) cells producing the catalytically inactive Ccp1(W191F) variant. Hydrogen Peroxide 69-73 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 90-94 23831190-5 2013 Key evidence for a sensing role for Ccp1 is the significantly higher H2O2 accumulation in ccp1-null cells(ccp1Delta) vs ccp1(W191F) cells producing the catalytically inactive Ccp1(W191F) variant. Hydrogen Peroxide 69-73 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 106-110 23831190-6 2013 In fact, intracellular H2O2 levels (ccp1Delta>wildtype >ccp1(W191F)) correlate inversely with the activity of the mitochondrial (and peroxisomal) heme catalase, Cta1 (ccp1Delta<wildtype <ccp1(W191F)). Hydrogen Peroxide 23-27 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 36-40 23831190-6 2013 In fact, intracellular H2O2 levels (ccp1Delta>wildtype >ccp1(W191F)) correlate inversely with the activity of the mitochondrial (and peroxisomal) heme catalase, Cta1 (ccp1Delta<wildtype <ccp1(W191F)). Hydrogen Peroxide 23-27 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 62-66 23831190-8 2013 Notably, Ccp1(W191F) is a more persistent H2O2 signaling protein than wild-type Ccp1, and this enhanced mitochondrial H2O2 signaling decreases the mitochondrial fitness of ccp1(W191F) cells. Hydrogen Peroxide 42-46 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 9-13 23831190-8 2013 Notably, Ccp1(W191F) is a more persistent H2O2 signaling protein than wild-type Ccp1, and this enhanced mitochondrial H2O2 signaling decreases the mitochondrial fitness of ccp1(W191F) cells. Hydrogen Peroxide 118-122 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 9-13 23831190-8 2013 Notably, Ccp1(W191F) is a more persistent H2O2 signaling protein than wild-type Ccp1, and this enhanced mitochondrial H2O2 signaling decreases the mitochondrial fitness of ccp1(W191F) cells. Hydrogen Peroxide 118-122 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 172-176 23831190-10 2013 Combined, our results strongly implicate Ccp1, independent of its peroxidase activity, in mitochondrial H2O2 sensing and signaling to maintain reactive oxygen species homeostasis. Hydrogen Peroxide 104-108 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 41-45 23832496-1 2013 Here we describe paramagnetic NMR analysis of the low- and high-spin forms of yeast cytochrome c peroxidase (CcP), a 34 kDa heme enzyme involved in hydroperoxide reduction in mitochondria. Hydrogen Peroxide 148-161 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 109-112 21820401-1 2011 Cytochrome c (Cc) and cytochrome c peroxidase (CcP) form a physiological complex in the inter-membrane space of yeast mitochondria, where CcP reduces hydrogen peroxide to water using the electrons provided by ferrous Cc. Hydrogen Peroxide 150-167 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 22-45 23022490-0 2013 Apolar distal pocket mutants of yeast cytochrome c peroxidase: hydrogen peroxide reactivity and cyanide binding of the TriAla, TriVal, and TriLeu variants. Hydrogen Peroxide 63-80 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 38-61 21820401-1 2011 Cytochrome c (Cc) and cytochrome c peroxidase (CcP) form a physiological complex in the inter-membrane space of yeast mitochondria, where CcP reduces hydrogen peroxide to water using the electrons provided by ferrous Cc. Hydrogen Peroxide 150-167 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 47-50 21820401-1 2011 Cytochrome c (Cc) and cytochrome c peroxidase (CcP) form a physiological complex in the inter-membrane space of yeast mitochondria, where CcP reduces hydrogen peroxide to water using the electrons provided by ferrous Cc. Hydrogen Peroxide 150-167 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 138-141 12957710-1 2003 Cytochrome c peroxidase (CcP) uses hydrogen peroxide as an electron acceptor to oxidize cytochrome c (Cc) in the mitochondrial intermembrane space. Hydrogen Peroxide 35-52 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 0-23 17011626-1 2006 Yeast cytochrome c peroxidase (CCP) efficiently catalyzes the reduction of H(2)O(2) to H(2)O by ferrocytochrome c in vitro. Hydrogen Peroxide 75-83 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 6-29 17011626-1 2006 Yeast cytochrome c peroxidase (CCP) efficiently catalyzes the reduction of H(2)O(2) to H(2)O by ferrocytochrome c in vitro. Hydrogen Peroxide 75-83 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 31-34 17011626-6 2006 However, the detoxification function of CCP protected respiring mitochondria when cells were challenged with H(2)O(2). Hydrogen Peroxide 109-117 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 40-43 17011626-9 2006 Challenge with H(2)O(2) caused increased CCP, superoxide dismutase and catalase antioxidant enzyme activities (but not glutathione reductase activity) in exponentially growing cells and decreased antioxidant activities in stationary-phase cells. Hydrogen Peroxide 15-23 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 41-44 12957710-1 2003 Cytochrome c peroxidase (CcP) uses hydrogen peroxide as an electron acceptor to oxidize cytochrome c (Cc) in the mitochondrial intermembrane space. Hydrogen Peroxide 35-52 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 25-28 12957710-4 2003 However, CCP1-disrupted cells were more sensitive to H2O2 than wild-type cells. Hydrogen Peroxide 53-57 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 9-13 12957710-6 2003 We found that expression of CCP1 gene increases under respiratory culture conditions and by treatments with H2O2. Hydrogen Peroxide 108-112 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 28-32 12957710-7 2003 These results hint that the biological function of CcP is to reduce H2O2 generated during aerobic respiratory process. Hydrogen Peroxide 68-72 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 51-54 12044899-1 2002 Cytochrome c peroxidase (CcP) is a yeast mitochondrial enzyme that catalyzes the reduction of hydrogen peroxide to water by ferrocytochrome c. It was the first heme enzyme to have its crystallographic structure determined and, as a consequence, has played a pivotal role in developing ideas about structural control of heme protein reactivity. Hydrogen Peroxide 94-111 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 0-23 12427011-0 2002 Radical formation at Tyr39 and Tyr153 following reaction of yeast cytochrome c peroxidase with hydrogen peroxide. Hydrogen Peroxide 95-112 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 66-89 12121764-2 2002 KatGs, CCP and APXs contain identical amino acid triads in the heme pocket (distal Arg/Trp/His and proximal His/Trp/Asp), but differ dramatically in their reactivities towards hydrogen peroxide and various one-electron donors. Hydrogen Peroxide 176-193 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 7-10 12044899-1 2002 Cytochrome c peroxidase (CcP) is a yeast mitochondrial enzyme that catalyzes the reduction of hydrogen peroxide to water by ferrocytochrome c. It was the first heme enzyme to have its crystallographic structure determined and, as a consequence, has played a pivotal role in developing ideas about structural control of heme protein reactivity. Hydrogen Peroxide 94-111 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 25-28 12044899-2 2002 Genetic engineering of the active site of CcP, along with structural, spectroscopic, and kinetic characterization of the mutant proteins has provided considerable insight into the mechanism of hydrogen peroxide activation, oxygen-oxygen bond cleavage, and formation of the higher-oxidation state intermediates in heme enzymes. Hydrogen Peroxide 193-210 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 42-45 9390453-8 1997 We show that restoration of methylotrophic growth in the suppressor strains is strongly correlated with increased levels of the alternative H2O2-destroying enzyme, cytochrome c peroxidase. Hydrogen Peroxide 140-144 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 164-187 11562206-0 2001 A distal histidine mutant (H52Q) of yeast cytochrome c peroxidase catalyzes the oxidation of H(2)O(2) instead of its reduction. Hydrogen Peroxide 93-101 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 42-65 11562206-3 2001 In the presence of H(2)O(2), wild-type CcP, adsorbed on a graphite electrode, shows a strong catalytic reduction wave commencing at about 0.8V (pH 5.4); by contrast, H52Q does not exhibit this activity but instead shows a catalytic oxidation current at potentials in the region of 0.9 V. The oxidation current is partly suppressed in the presence of tetranitromethane (a superoxide scavenger) and is not observed for other mutants studied, including H52A. Hydrogen Peroxide 19-27 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 39-42 1332763-0 1992 Effect of Asp-235-->Asn substitution on the absorption spectrum and hydrogen peroxide reactivity of cytochrome c peroxidase. Hydrogen Peroxide 71-88 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 103-126 8286338-0 1994 Fluorescence investigation of yeast cytochrome c peroxidase oxidation by H2O2 and enzyme activities of the oxidized enzyme. Hydrogen Peroxide 73-77 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 36-59 8286338-2 1994 Compound I and more highly oxidized forms of CCP were formed by adding 1, 3, and 10 equiv of H2O2 to 5 microM protein at pH 7.0 in the absence of exogenous reducing substrates. Hydrogen Peroxide 93-97 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 45-48 8286338-4 1994 CCP oxidized with 10-fold excess H2O2 exhibited 65 +/- 1% relative fluorescence, indicating loss of 2.4 +/- 0.1 tryptophans. Hydrogen Peroxide 33-37 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 0-3 8286338-9 1994 The fluorescence decrease with time paralleled the decrease in activity of H2O2-oxidized CCP using both ferrocytochrome c and ferrocyanide as substrates, indicating that tryptophan and activity loss occurred on similar time scales. Hydrogen Peroxide 75-79 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 89-92 8214607-0 1993 Electrocatalytic reduction of hydrogen peroxide at a stationary pyrolytic graphite electrode surface in the presence of cytochrome c peroxidase: a description based on a microelectrode array model for adsorbed enzyme molecules. Hydrogen Peroxide 30-47 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 120-143 8214607-1 1993 Electrochemical reduction of H2O2 at pyrolytic graphite disc electrodes of radius 2.5 mm occurs at readily accessible potentials (600 mV versus the standard hydrogen electrode) in the presence of yeast cytochrome c peroxidase. Hydrogen Peroxide 29-33 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 202-225 1654930-6 1991 The activation energy of immobilised CcP was greater in the presence of both H2O2 [16.6 kJ mol-1] and m-chloroperoxybenzoic acid [37.9 kJ mol-1] than for soluble CcP [11.4 and 23.4 kJ mol-1, respectively]. Hydrogen Peroxide 77-81 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 37-40 16347719-7 1988 However, cytochrome c peroxidase (CCP; EC 1.11.1.5) increased to very high levels in cells which decomposed H(2)O(2). Hydrogen Peroxide 108-116 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 9-32 1648292-3 1991 The enzyme responsible for H2O2 degradation is probably the mitochondrial enzyme cytochrome c peroxidase (CCP), which was present at very high activities. Hydrogen Peroxide 27-31 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 81-104 1648292-3 1991 The enzyme responsible for H2O2 degradation is probably the mitochondrial enzyme cytochrome c peroxidase (CCP), which was present at very high activities. Hydrogen Peroxide 27-31 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 106-109 1648292-5 1991 Thus, reducing equivalents for H2O2 degradation by CCP must be provided by the respiratory chain. Hydrogen Peroxide 31-35 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 51-54 1648292-8 1991 Energetic aspects of mitochondrial H2O2 decomposition via CCP and the physiological function of CCP in yeasts are discussed. Hydrogen Peroxide 35-39 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 58-61 1823652-6 1991 The hydrogen peroxide produced during growth of the mutants on mixed substrates is detoxified by cytochrome-c peroxidase and other peroxidases. Hydrogen Peroxide 4-21 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 97-120 2156573-1 1990 The bimolecular reaction between Escherichia coli-produced cytochrome-c peroxidase (CcP(MI)) and hydrogen peroxide is identical to that of native yeast cytochrome-c peroxidase (CcP) and hydrogen peroxide in the neutral pH region. Hydrogen Peroxide 97-114 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 59-82 2156573-1 1990 The bimolecular reaction between Escherichia coli-produced cytochrome-c peroxidase (CcP(MI)) and hydrogen peroxide is identical to that of native yeast cytochrome-c peroxidase (CcP) and hydrogen peroxide in the neutral pH region. Hydrogen Peroxide 97-114 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 84-87 2156573-1 1990 The bimolecular reaction between Escherichia coli-produced cytochrome-c peroxidase (CcP(MI)) and hydrogen peroxide is identical to that of native yeast cytochrome-c peroxidase (CcP) and hydrogen peroxide in the neutral pH region. Hydrogen Peroxide 97-114 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 152-175 2156573-1 1990 The bimolecular reaction between Escherichia coli-produced cytochrome-c peroxidase (CcP(MI)) and hydrogen peroxide is identical to that of native yeast cytochrome-c peroxidase (CcP) and hydrogen peroxide in the neutral pH region. Hydrogen Peroxide 97-114 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 177-180 2156573-1 1990 The bimolecular reaction between Escherichia coli-produced cytochrome-c peroxidase (CcP(MI)) and hydrogen peroxide is identical to that of native yeast cytochrome-c peroxidase (CcP) and hydrogen peroxide in the neutral pH region. Hydrogen Peroxide 186-203 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 59-82 2156573-1 1990 The bimolecular reaction between Escherichia coli-produced cytochrome-c peroxidase (CcP(MI)) and hydrogen peroxide is identical to that of native yeast cytochrome-c peroxidase (CcP) and hydrogen peroxide in the neutral pH region. Hydrogen Peroxide 186-203 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 84-87 2156573-1 1990 The bimolecular reaction between Escherichia coli-produced cytochrome-c peroxidase (CcP(MI)) and hydrogen peroxide is identical to that of native yeast cytochrome-c peroxidase (CcP) and hydrogen peroxide in the neutral pH region. Hydrogen Peroxide 186-203 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 177-180 2156573-3 1990 A second mutant enzyme, E. coli-produced cytochrome-c peroxidase mutant with phenylalanine at position 191 (CcP(MI, F191)), has a pH-independent bimolecular rate constant for the hydrogen peroxide reaction of 65 microM-1.s-1, 40% larger than for CcP or CcP(MI). Hydrogen Peroxide 179-196 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 41-64 2156573-3 1990 A second mutant enzyme, E. coli-produced cytochrome-c peroxidase mutant with phenylalanine at position 191 (CcP(MI, F191)), has a pH-independent bimolecular rate constant for the hydrogen peroxide reaction of 65 microM-1.s-1, 40% larger than for CcP or CcP(MI). Hydrogen Peroxide 179-196 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 108-111 2156573-3 1990 A second mutant enzyme, E. coli-produced cytochrome-c peroxidase mutant with phenylalanine at position 191 (CcP(MI, F191)), has a pH-independent bimolecular rate constant for the hydrogen peroxide reaction of 65 microM-1.s-1, 40% larger than for CcP or CcP(MI). Hydrogen Peroxide 179-196 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 246-249 2156573-3 1990 A second mutant enzyme, E. coli-produced cytochrome-c peroxidase mutant with phenylalanine at position 191 (CcP(MI, F191)), has a pH-independent bimolecular rate constant for the hydrogen peroxide reaction of 65 microM-1.s-1, 40% larger than for CcP or CcP(MI). Hydrogen Peroxide 179-196 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 246-249 2156573-4 1990 The initial peroxide-oxidation product of CcP(MI, F191) is an oxyferryl porphyrin pi-cation radical intermediate in contrast to the oxyferryl amino-acid radical intermediate formed upon oxidation of CcP or CcP(MI) with hydrogen peroxide. Hydrogen Peroxide 219-236 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 42-45 2156573-8 1990 Both CcP(MI) and CcP(MI, F191) have slightly smaller pH stability regions compared to CcP as assessed by the hydrogen peroxide titer and spectral analysis. Hydrogen Peroxide 109-126 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 5-8 2156573-8 1990 Both CcP(MI) and CcP(MI, F191) have slightly smaller pH stability regions compared to CcP as assessed by the hydrogen peroxide titer and spectral analysis. Hydrogen Peroxide 109-126 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 17-20 2156573-8 1990 Both CcP(MI) and CcP(MI, F191) have slightly smaller pH stability regions compared to CcP as assessed by the hydrogen peroxide titer and spectral analysis. Hydrogen Peroxide 109-126 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 17-20 2557891-0 1989 Detection of an oxyferryl porphyrin pi-cation-radical intermediate in the reaction between hydrogen peroxide and a mutant yeast cytochrome c peroxidase. Hydrogen Peroxide 91-108 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 128-151 16347719-7 1988 However, cytochrome c peroxidase (CCP; EC 1.11.1.5) increased to very high levels in cells which decomposed H(2)O(2). Hydrogen Peroxide 108-116 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 34-37 16347719-14 1988 (ii) Catalase can effectively compete with mitochondrial CCP for hydrogen peroxide only if hydrogen peroxide is generated at the site where catalase is located, namely in the peroxisomes. Hydrogen Peroxide 65-82 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 57-60 16347719-14 1988 (ii) Catalase can effectively compete with mitochondrial CCP for hydrogen peroxide only if hydrogen peroxide is generated at the site where catalase is located, namely in the peroxisomes. Hydrogen Peroxide 91-108 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 57-60 2831888-1 1988 Electron transfer from yeast ferrous cytochrome c to H2O2-oxidized yeast cytochrome c peroxidase has been studied using flash photoreduction methods. Hydrogen Peroxide 53-57 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 73-96 2841676-1 1988 Cytochrome c peroxidase, freshly prepared, contains a penta-coordinated heme iron and is fully reactive with hydroperoxides. Hydrogen Peroxide 109-123 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 0-23 2841676-4 1988 Thus, the reactivity of cytochrome c peroxidase with hydroperoxides is strongly controlled by the coordination state of the heme iron. Hydrogen Peroxide 53-67 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 24-47 230500-0 1979 Electron-nuclear double resonance of the hydrogen peroxide compound of cytochrome c peroxidase: identification of the free radical site with a methionyl cluster. Hydrogen Peroxide 41-58 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 71-94 3024731-6 1987 This indicates that hydrogen peroxide can interact with the 1:1 complex at sites other than the heme of cytochrome c peroxidase, generating additional species capable of oxidizing free ferrocytochrome c. Hydrogen Peroxide 20-37 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 104-127 3006043-1 1986 Yeast cytochrome c peroxidase reacts with hydrogen peroxide to form an intermediate, compound ES, in which the heme iron atom is converted to a ferryl function (Fe4+ = O) and a radical center is generated on a reversibly oxidizable amino acid residue of uncertain identity. Hydrogen Peroxide 42-59 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 6-29 6263919-0 1981 Electron paramagnetic and electron nuclear double resonance of the hydrogen peroxide compound of cytochrome c peroxidase. Hydrogen Peroxide 67-84 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 97-120 6263919-1 1981 We have collected electron paramagnetic resonance (EPR) and electron nuclear double resonance (ENDOR) spectra from the hydrogen peroxide compound of yeast cytochrome c peroxidase, termed ES, employing EPR microwave frequencies of 9.6 and 11.6 GHz. Hydrogen Peroxide 119-136 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 155-178 3036864-8 1987 The aging-induced hexa-coordinated CCP is unreactive with hydrogen peroxide and exhibits an EPR spectrum of purely axial symmetry with extrema at g = 6 and g = 2 and an electronic absorption spectrum with an intensified Soret band at 408 nm (epsilon 408 nm = 120 mM-1 cm-1) and a blue-shifted charge-transfer band at 620 nm. Hydrogen Peroxide 58-75 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 35-38 230500-1 1979 The results of electron-nuclear double resonance and electron paramagnetic resonance (EPR) studies on the hydrogen peroxide compound of yeast cytochrome c peroxidase are inconsistent with previous proposals for the source of the EPR signal in this compound, in particular with its identification with an aromatic amino acid radical such as would arise by oxidation of a tryptophanyl side chain. Hydrogen Peroxide 106-123 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 142-165