PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8119983-1 1994 Cytochrome c3 (M(r) 13,000) is a tetrahemic cytochrome in which the four heme iron atoms are coordinated by 2 histidine residues at the axial positions. Iron 78-82 cytochrome c, somatic Homo sapiens 0-12 8119983-3 1994 To investigate this mechanism, four single mutations were introduced in cytochrome c3 by site-directed mutagenesis, leading to the replacement of each histidine, the sixth axial ligand of the heme iron atom, by a methionine residue. Iron 197-201 cytochrome c, somatic Homo sapiens 72-84 8397141-6 1993 The iron-ion reducing ability of apomorphine and laudanosoline was confirmed using cytochrome c. Iron 4-8 cytochrome c, somatic Homo sapiens 83-95 24227666-3 1993 The charge state of iron in the expelled heme from myoglobin and hemoglobin appears to be 3+ but 2f for heme expelled from cytochrome c. Iron 20-24 cytochrome c, somatic Homo sapiens 123-135 8384229-6 1993 We found that cytochrome c(c)covalently coupled to monovalent iron-saturated transferrin (Tf), (c-Tf), is not processed or presented significantly better than unconjugated c, indicating that the majority of cycling TfR does not enter compartments where processing proceeds. Iron 62-66 cytochrome c, somatic Homo sapiens 14-26 1282813-1 1992 The formed complexes of cytochrome c with polyanions retain the bond of Met-80 with heme iron. Iron 89-93 cytochrome c, somatic Homo sapiens 24-36 1332689-0 1992 Investigation of the electron-transfer properties of cytochrome c oxidase covalently cross-linked to Fe- or Zn-containing cytochrome c. Iron 101-103 cytochrome c, somatic Homo sapiens 53-65 1332689-0 1992 Investigation of the electron-transfer properties of cytochrome c oxidase covalently cross-linked to Fe- or Zn-containing cytochrome c. Iron 101-103 cytochrome c, somatic Homo sapiens 122-134 1332689-1 1992 Complexes of cytochrome c oxidase and cytochrome c (Fe- or Zn-containing) have been prepared by 1-ethyl-3-[3-(dimethylamino)propyl]carbodi-imide (EDC) cross-linking. Iron 52-54 cytochrome c, somatic Homo sapiens 13-25 1332689-1 1992 Complexes of cytochrome c oxidase and cytochrome c (Fe- or Zn-containing) have been prepared by 1-ethyl-3-[3-(dimethylamino)propyl]carbodi-imide (EDC) cross-linking. Iron 52-54 cytochrome c, somatic Homo sapiens 38-50 1332689-3 1992 Stopped-flow experiments, monitored either at a single wavelength or through a rapid wavelength-scan facility, showed that covalently bound Fe-containing cytochrome c cannot donate electrons to cytochrome a. Iron 140-142 cytochrome c, somatic Homo sapiens 154-166 1332689-4 1992 Free Fe-containing cytochrome c was, however, able to transfer electrons to cytochrome a in covalent complexes containing either Fe- or Zn-containing cytochrome c. Iron 5-7 cytochrome c, somatic Homo sapiens 19-31 1332689-4 1992 Free Fe-containing cytochrome c was, however, able to transfer electrons to cytochrome a in covalent complexes containing either Fe- or Zn-containing cytochrome c. Iron 5-7 cytochrome c, somatic Homo sapiens 150-162 1332689-4 1992 Free Fe-containing cytochrome c was, however, able to transfer electrons to cytochrome a in covalent complexes containing either Fe- or Zn-containing cytochrome c. Iron 129-131 cytochrome c, somatic Homo sapiens 19-31 1382421-3 1992 Using three in vitro models we observed these two compounds had inhibitory effects on cytochrome C reduction by ferrous iron, by ferrous iron accelerated by an unsaturated fatty acid or by epinephrine. Iron 112-124 cytochrome c, somatic Homo sapiens 86-98 1382421-3 1992 Using three in vitro models we observed these two compounds had inhibitory effects on cytochrome C reduction by ferrous iron, by ferrous iron accelerated by an unsaturated fatty acid or by epinephrine. Iron 129-141 cytochrome c, somatic Homo sapiens 86-98 1314661-5 1992 We confirmed that cytochrome c553 is the endogenous donor to P840+, and at room temperature we observed a recombination reaction between the reduced terminal acceptor and P840+ with a t1/2 = 7 ms. Oxidative degradation of iron-sulfur centers using low concentrations of chaotropic salts introduced a faster recombination reaction of t1/2 = 50 microseconds which was lost at higher concentrations of chaotrope, indicating the participation of another iron-sulfur redox center earlier than the terminal acceptor. Iron 222-226 cytochrome c, somatic Homo sapiens 18-30 1314661-5 1992 We confirmed that cytochrome c553 is the endogenous donor to P840+, and at room temperature we observed a recombination reaction between the reduced terminal acceptor and P840+ with a t1/2 = 7 ms. Oxidative degradation of iron-sulfur centers using low concentrations of chaotropic salts introduced a faster recombination reaction of t1/2 = 50 microseconds which was lost at higher concentrations of chaotrope, indicating the participation of another iron-sulfur redox center earlier than the terminal acceptor. Iron 450-454 cytochrome c, somatic Homo sapiens 18-30 1315745-1 1992 Recombinant cytochrome c peroxidase (CcP) and a W51A mutant of CcP, in contrast to other classical peroxidases, react with phenylhydrazine to give sigma-bonded phenyl-iron complexes. Iron 167-171 cytochrome c, somatic Homo sapiens 12-24 1657909-0 1991 Significance of the "Rieske" iron-sulfur protein for formation and function of the ubiquinol-oxidation pocket of mitochondrial cytochrome c reductase (bc1 complex). Iron 29-33 cytochrome c, somatic Homo sapiens 127-139 1657909-7 1991 The affinity of three preparations of cytochrome c reductase, the complete, the delipidated, and the iron-sulfur depleted enzyme for E-beta-methoxyacrylate-stilbene, was analyzed for different redox states of the catalytic centers of cytochrome c reductase. Iron 101-105 cytochrome c, somatic Homo sapiens 38-50 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. Iron 172-176 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. Iron 217-221 cytochrome c, somatic Homo sapiens 36-48 1646028-1 1991 Molecular dynamics simulations of a tetraheme cytochrome c3 were performed to investigate dynamic aspects of the motion of the axial heme iron ligands. Iron 138-142 cytochrome c, somatic Homo sapiens 46-58 1849482-1 1991 The spectral changes caused by binding soft ligands to the cytochrome c iron and their correlation to ligand affinities support the hypothesis that the iron-methionine sulfur bond of this heme protein is enhanced by delocalization of the metal t2g electrons into the empty 3d orbitals of the ligand atom. Iron 72-76 cytochrome c, somatic Homo sapiens 59-71 1849482-1 1991 The spectral changes caused by binding soft ligands to the cytochrome c iron and their correlation to ligand affinities support the hypothesis that the iron-methionine sulfur bond of this heme protein is enhanced by delocalization of the metal t2g electrons into the empty 3d orbitals of the ligand atom. Iron 152-156 cytochrome c, somatic Homo sapiens 59-71 1937137-4 1991 Using a model system of ferrous iron and ferric cytochrome c, it was determined that substitution of GTP for GDP led to an enhanced reduction of ferric cytochrome c. Iron 32-36 cytochrome c, somatic Homo sapiens 152-164 2159343-6 1990 While in state I the structure of cytochrome c is essentially the same as in solution, state II is characterized by a structural rearrangement of the heme pocket, leading to a weakening of the axial iron-methionine bond and an opening of the heme crevice which is situated in the center of the binding domain for cytochrome oxidase. Iron 199-203 cytochrome c, somatic Homo sapiens 34-46 34954215-2 2022 The peroxidase active form of Cytc occurs due to local conformational changes that support the opening of the heme crevice and the loss of an axial ligand between Met80 and heme Fe. Iron 178-180 cytochrome c, somatic Homo sapiens 30-34 34656823-3 2021 Within the electron transport chain, Fe-S clusters play a critical role in transporting electrons through Complexes I, II and III to cytochrome c, before subsequent transfer to molecular oxygen. Iron 37-41 cytochrome c, somatic Homo sapiens 133-145 34194691-6 2021 These simultaneous XES-XSS studies have provided detailed insight into the mechanism of light-induced spin crossover in iron coordination compounds, the interaction of CT and MC excited states in iron carbene photosensitizers, and the mechanism of Fe-S bond dissociation in cytochrome c. Iron 248-250 cytochrome c, somatic Homo sapiens 274-286 2556275-2 1989 A hypothetical model of the complex formed between the iron-sulfur protein rubredoxin and the tetraheme cytochrome c3 from the sulfate-reducing bacteria Desulfovibrio vulgaris (Hildenborough) has been proposed utilizing computer graphic modeling, computational methods and NMR spectroscopy. Iron 55-59 cytochrome c, somatic Homo sapiens 104-116 2853215-0 1988 Photoexcitation of the methionine-iron bond in iron(III) cytochrome c: bimolecular reaction with NADH. Iron 34-38 cytochrome c, somatic Homo sapiens 57-69 2853215-0 1988 Photoexcitation of the methionine-iron bond in iron(III) cytochrome c: bimolecular reaction with NADH. Iron 47-51 cytochrome c, somatic Homo sapiens 57-69 2853215-1 1988 When iron(III) cytochrome c aqueous solutions containing NADH are irradiated with polychromatic light (wavelength greater than 280 nm), iron(II) cytochrome c and NAD+ in the stoichiometric ratio 2/1 are observed to be the principal reaction products, independently of the presence of oxygen; in addition, a minor process due to direct photodegradation of the nucleotide is observed. Iron 5-9 cytochrome c, somatic Homo sapiens 15-27 2853215-1 1988 When iron(III) cytochrome c aqueous solutions containing NADH are irradiated with polychromatic light (wavelength greater than 280 nm), iron(II) cytochrome c and NAD+ in the stoichiometric ratio 2/1 are observed to be the principal reaction products, independently of the presence of oxygen; in addition, a minor process due to direct photodegradation of the nucleotide is observed. Iron 5-9 cytochrome c, somatic Homo sapiens 145-157 2853215-1 1988 When iron(III) cytochrome c aqueous solutions containing NADH are irradiated with polychromatic light (wavelength greater than 280 nm), iron(II) cytochrome c and NAD+ in the stoichiometric ratio 2/1 are observed to be the principal reaction products, independently of the presence of oxygen; in addition, a minor process due to direct photodegradation of the nucleotide is observed. Iron 136-140 cytochrome c, somatic Homo sapiens 15-27 2853215-1 1988 When iron(III) cytochrome c aqueous solutions containing NADH are irradiated with polychromatic light (wavelength greater than 280 nm), iron(II) cytochrome c and NAD+ in the stoichiometric ratio 2/1 are observed to be the principal reaction products, independently of the presence of oxygen; in addition, a minor process due to direct photodegradation of the nucleotide is observed. Iron 136-140 cytochrome c, somatic Homo sapiens 145-157 2853215-7 1988 radical rapidly reacts with oxygen to give NAD+ and superoxide O2- anion radical which, in turn, reduces the second iron(III) cytochrome c molecule. Iron 116-120 cytochrome c, somatic Homo sapiens 126-138 2848510-0 1988 The binding characteristics of the cytochrome c iron. Iron 48-52 cytochrome c, somatic Homo sapiens 35-47 2848510-2 1988 This explains the outstanding stability of the methionine-iron bond of ferrous cytochrome c, and results from the intrinsic ability of the cytochrome c iron to delocalize its electrons into orbitals of the sixth axial ligand. Iron 58-62 cytochrome c, somatic Homo sapiens 79-91 2848510-2 1988 This explains the outstanding stability of the methionine-iron bond of ferrous cytochrome c, and results from the intrinsic ability of the cytochrome c iron to delocalize its electrons into orbitals of the sixth axial ligand. Iron 58-62 cytochrome c, somatic Homo sapiens 139-151 2848510-2 1988 This explains the outstanding stability of the methionine-iron bond of ferrous cytochrome c, and results from the intrinsic ability of the cytochrome c iron to delocalize its electrons into orbitals of the sixth axial ligand. Iron 152-156 cytochrome c, somatic Homo sapiens 79-91 2848510-2 1988 This explains the outstanding stability of the methionine-iron bond of ferrous cytochrome c, and results from the intrinsic ability of the cytochrome c iron to delocalize its electrons into orbitals of the sixth axial ligand. Iron 152-156 cytochrome c, somatic Homo sapiens 139-151 2842153-3 1988 Porphyrin cytochrome c, the iron-free derivative of cytochrome c, has been used extensively as a fluorescent analog of cytochrome c. Iron 28-32 cytochrome c, somatic Homo sapiens 10-22 2842153-3 1988 Porphyrin cytochrome c, the iron-free derivative of cytochrome c, has been used extensively as a fluorescent analog of cytochrome c. Iron 28-32 cytochrome c, somatic Homo sapiens 52-64 2842153-3 1988 Porphyrin cytochrome c, the iron-free derivative of cytochrome c, has been used extensively as a fluorescent analog of cytochrome c. Iron 28-32 cytochrome c, somatic Homo sapiens 52-64 2842153-8 1988 The N-3 nitrogen of this residue forms one of the axial ligands to the iron in the intact cytochrome c but it is uncoordinated in the iron-free derivative. Iron 71-75 cytochrome c, somatic Homo sapiens 90-102 2844250-4 1988 When the oxidase in the aerobic steady state, with porphyrin cytochrome c (the iron-free derivative of cytochrome c) bound to it, is subjected to pressure, the porphyrin derivative is released. Iron 79-83 cytochrome c, somatic Homo sapiens 61-73 2844250-4 1988 When the oxidase in the aerobic steady state, with porphyrin cytochrome c (the iron-free derivative of cytochrome c) bound to it, is subjected to pressure, the porphyrin derivative is released. Iron 79-83 cytochrome c, somatic Homo sapiens 103-115 2853113-0 1988 Iron release from metmyoglobin, methaemoglobin and cytochrome c by a system generating hydrogen peroxide. Iron 0-4 cytochrome c, somatic Homo sapiens 51-63 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. Iron 160-164 cytochrome c, somatic Homo sapiens 0-12 2821542-7 1987 The conformational rearrangement induced in cytochrome c by cytochrome c oxidase consists of a structural rearrangement of the heme environment and possibly a change of the geometry of the heme iron-methionine-80 sulfur axial bond. Iron 135-139 cytochrome c, somatic Homo sapiens 44-56 2821542-7 1987 The conformational rearrangement induced in cytochrome c by cytochrome c oxidase consists of a structural rearrangement of the heme environment and possibly a change of the geometry of the heme iron-methionine-80 sulfur axial bond. Iron 135-139 cytochrome c, somatic Homo sapiens 60-72 3013197-5 1986 Second, allopurinol was found to act as an electron transfer agent from ferrous iron to ferric cytochrome c. Iron 72-84 cytochrome c, somatic Homo sapiens 95-107 3008856-1 1986 Changes observed in CD- and absorption spectra of cytochrome c solubilized in reversed micelles AOT showed significant structural transformations of protein in the region of the active centre and particularly revealed a replacement of the sixth ligand of heme iron. Iron 260-264 cytochrome c, somatic Homo sapiens 50-62 2999105-8 1985 The isolated iron-sulfur protein catalyzes reduction of cytochrome c by ubiquinol, which is insensitive to antimycin, at a rate of 0.03 mumol of cytochrome c reduced/min/nmol of protein, while the purified cytochrome c1 has no such catalytic activity. Iron 13-17 cytochrome c, somatic Homo sapiens 56-68 2999105-8 1985 The isolated iron-sulfur protein catalyzes reduction of cytochrome c by ubiquinol, which is insensitive to antimycin, at a rate of 0.03 mumol of cytochrome c reduced/min/nmol of protein, while the purified cytochrome c1 has no such catalytic activity. Iron 13-17 cytochrome c, somatic Homo sapiens 145-157 2999105-9 1985 When cytochrome c1 and the iron-sulfur protein form a complex, the rate of cytochrome c reduction increases to 0.12 mumol/min/nmol of the iron-sulfur protein. Iron 27-31 cytochrome c, somatic Homo sapiens 5-17 2999105-10 1985 In this reaction, cytochrome c1 mediates antimycin-insensitive electron transfer from the iron-sulfur protein to cytochrome c, thereby constituting a pathway of electrons: ubiquinol----iron-sulfur protein----cytochrome c1----cytochrome c. Iron 90-94 cytochrome c, somatic Homo sapiens 18-30 2999105-10 1985 In this reaction, cytochrome c1 mediates antimycin-insensitive electron transfer from the iron-sulfur protein to cytochrome c, thereby constituting a pathway of electrons: ubiquinol----iron-sulfur protein----cytochrome c1----cytochrome c. Iron 90-94 cytochrome c, somatic Homo sapiens 113-125 2989537-1 1985 An equal mixture of oxidized and reduced cytochrome c551 experiences a change in the potential of the haem iron when one of the propionates attached to the haem is ionized. Iron 107-111 cytochrome c, somatic Homo sapiens 41-53 2992542-1 1985 We have studied the behaviour of Fe(III) cytochrome c upon irradiation in the 290-360 nm wavelength range either in the presence or in the absence of NADH; in both cases the photoexcitation caused the reduction of the heme iron. Iron 223-227 cytochrome c, somatic Homo sapiens 41-53 6725248-5 1984 The bound ferredoxin can interact with cytochrome c; the iron-sulfur cluster of the cross-linked complex is shown to be reduced under anaerobic conditions by NADPH and to be required for the catalysis of the NADPH-cytochrome c reductase reaction. Iron 57-61 cytochrome c, somatic Homo sapiens 39-51 6725248-5 1984 The bound ferredoxin can interact with cytochrome c; the iron-sulfur cluster of the cross-linked complex is shown to be reduced under anaerobic conditions by NADPH and to be required for the catalysis of the NADPH-cytochrome c reductase reaction. Iron 57-61 cytochrome c, somatic Homo sapiens 214-226 6431395-4 1984 Iron is an essential part of cytochrome C and alpha-glycerolphosphate dehydrogenase, and early stages of iron deficiency may, therefore, cause disturbances in tissue metabolism before development of anaemia. Iron 0-4 cytochrome c, somatic Homo sapiens 29-41 6299195-3 1983 An analysis of the dependence of the proton relaxation rate on the observation frequency indicated that the correlation time, which modulates the interaction between solvent protons and the unpaired electrons on the metal ions, is due to the electron spin relaxation time of the heme irons of cytochrome c oxidase. Iron 284-289 cytochrome c, somatic Homo sapiens 293-305 6127735-4 1982 The function of cytochrome c3 (Mr = 13000) in the mechanism of the periplasmic hydrogenase and the role of the new [3Fe-3S] non-haem iron centres in electron transfer is emphasized. Iron 133-137 cytochrome c, somatic Homo sapiens 16-28 6288087-1 1982 In 5,5"-dithiobis(2-nitrobenzoate) (DTNB)-treated succinate: cytochrome c reductase, the electron transfer from duroquinol to cytochrome c is inhibited due to the fact that the Rieske Fe-S cluster and, consequently, cytochrome, c, are no longer reducible by substrate. Iron 184-188 cytochrome c, somatic Homo sapiens 61-73 6288087-1 1982 In 5,5"-dithiobis(2-nitrobenzoate) (DTNB)-treated succinate: cytochrome c reductase, the electron transfer from duroquinol to cytochrome c is inhibited due to the fact that the Rieske Fe-S cluster and, consequently, cytochrome, c, are no longer reducible by substrate. Iron 184-188 cytochrome c, somatic Homo sapiens 126-138 6289365-0 1982 Resolved fluorescence emission spectra of iron-free cytochrome c. Iron 42-46 cytochrome c, somatic Homo sapiens 52-64 6281261-3 1982 An analogue of cytochrome c in which the iron atom was replaced with cobalt was used to probe the effect of redox potential on the reaction. Iron 41-45 cytochrome c, somatic Homo sapiens 15-27 6284217-1 1982 (1) Using the pulse-radiolysis and stopped-flow techniques, the reactions of iron-free (porphyrin) cytochrome c and native cytochrome c with cytochrome aa3 were investigated. Iron 77-81 cytochrome c, somatic Homo sapiens 99-111 6277946-5 1982 As increasing amounts of iron-sulfur protein are reconstituted to the depleted complex, the amounts of cytochromes b and c1 reduced by succinate in the presence of antimycin increase and closely parallel the amounts of ubiquinol-cytochrome c reductase activity restored to the reconstituted complex, measured before addition of antimycin. Iron 25-29 cytochrome c, somatic Homo sapiens 229-241 6277374-7 1982 In this paper, we discuss the possible methods of analysis of such data and present the results of our model refinement analysis concerning (a) the location of the cytochrome c heme iron atom in the profile structure of a reconstituted membrane containing a photosynthetic reaction center-cytochrome c complex and (b) the location of the heme a and a3 iron atoms in the profile structure of a reconstituted membrane containing cytochrome oxidase. Iron 182-186 cytochrome c, somatic Homo sapiens 164-176 6277374-7 1982 In this paper, we discuss the possible methods of analysis of such data and present the results of our model refinement analysis concerning (a) the location of the cytochrome c heme iron atom in the profile structure of a reconstituted membrane containing a photosynthetic reaction center-cytochrome c complex and (b) the location of the heme a and a3 iron atoms in the profile structure of a reconstituted membrane containing cytochrome oxidase. Iron 182-186 cytochrome c, somatic Homo sapiens 289-301 6277374-7 1982 In this paper, we discuss the possible methods of analysis of such data and present the results of our model refinement analysis concerning (a) the location of the cytochrome c heme iron atom in the profile structure of a reconstituted membrane containing a photosynthetic reaction center-cytochrome c complex and (b) the location of the heme a and a3 iron atoms in the profile structure of a reconstituted membrane containing cytochrome oxidase. Iron 352-356 cytochrome c, somatic Homo sapiens 164-176 16593145-0 1982 Picosecond photochemistry of a cofacial diporphyrin containing iron(III) and zinc(II): Mimicking electron transfer between cytochrome c and the primary electron donor in reaction centers of photosynthetic bacteria. Iron 63-67 cytochrome c, somatic Homo sapiens 123-135 6269606-7 1981 We interpret the long lifetime of the transient state as due to the slow return of Met-80 as sixth ligand to the heme iron upon reduction of the alkaline form of cytochrome c. Iron 118-122 cytochrome c, somatic Homo sapiens 162-174 6251349-3 1980 Unsaturated fatty acids markedly enhanced the reduction of ferric cytochrome c by ferrous iron. Iron 82-94 cytochrome c, somatic Homo sapiens 66-78 35223-8 1979 At pH 1.0 there is a different high-spin form of cytochrome c which has an estimated iron out-of-plane distance of approximately 0.46 A. Iron 85-89 cytochrome c, somatic Homo sapiens 49-61 23724-0 1978 Interaction of beta-lactoglobulin and cytochrome c: complex formation and iron reduction. Iron 74-78 cytochrome c, somatic Homo sapiens 38-50 198807-5 1977 The shift in the Fe K-edge of cytochrome oxidase upon reduction is small (about 2 e V or 3 times 10(-19 J) and is comparable to that previously observed for the reduction of the heme iron of cytochrome c. Iron 183-187 cytochrome c, somatic Homo sapiens 191-203 190037-0 1977 In vivo synthesis of iron-free cytochrome c during lead intoxication. Iron 21-25 cytochrome c, somatic Homo sapiens 31-43 1265-1 1975 Absorption and emission spectra and binding characteristics of iron-free cytochrome c. Iron 63-67 cytochrome c, somatic Homo sapiens 73-85 1265-2 1975 A cytochrome c derivative from which iron is removed has been prepared and characterized. Iron 37-41 cytochrome c, somatic Homo sapiens 2-14 171296-0 1975 Letter: Iron to sulfur bonding in cytochrome C studied by x-ray photoelectron spectroscopy. Iron 8-12 cytochrome c, somatic Homo sapiens 34-46 2584-3 1975 (1) For ferrous alkylated cytochrome c, a Raman line sensitive to the replacement of an axial ligand of the heme iron uas found around 1540 cm=1. Iron 113-117 cytochrome c, somatic Homo sapiens 26-38 170959-4 1975 MNMT-cytochrome c was found to be, structurally and conformationally, a single isomer, reducible with ascorbate, with a small, but definite affinity for both oxidation with molecular oxygen and binding of CO. Conformationally, in both valence states of the metal atom, it represents a molecular form with native-like conformation with small but definite perturbations in the immediate vicinity of the heme group, reflected by the destabilization of the Met-80-S-Fe linkage. Iron 462-464 cytochrome c, somatic Homo sapiens 5-17 234749-11 1975 The results are interpreted in a scheme in which first a transient complex between cytochrome c and the hydrated electron is formed, after which the heme iron is reduced and followed by relaxation of the protein from its oxidized to its reduced conformation. Iron 154-158 cytochrome c, somatic Homo sapiens 83-95 234749-16 1975 A reduction mechanism for cytochrome c is favored in which the reduction equivalent from the hydrated electron is transmitted through a specific pathway from the surface of the molecule to the heme iron. Iron 198-202 cytochrome c, somatic Homo sapiens 26-38 4154211-0 1974 A complex formation of the adrenal iron-sulfur protein (adrenodoxin) with cytochrome c and the decomposition of the iron-sulfur center. Iron 35-39 cytochrome c, somatic Homo sapiens 74-86 11946389-0 1972 Evidence for pentacoordinated iron (II) in carboxymethylated cytochrome c. Iron 30-34 cytochrome c, somatic Homo sapiens 61-73 5260911-1 1969 In cytochrome c the axial positions of the heme iron are occupied by two amino acid residues, one of which is known from X-ray studies to be histidyl. Iron 48-52 cytochrome c, somatic Homo sapiens 3-15 5664904-0 1968 Mossbauer studies of the iron atom in cytochrome c. Iron 25-29 cytochrome c, somatic Homo sapiens 38-50 13172260-0 1954 The function of inorganic iron in the reduction of cytochrome C. Iron 26-30 cytochrome c, somatic Homo sapiens 51-63 17809382-0 1950 Studies on the Metabolism of Administered Cytochrome C by the Aid of Iron-labeled Cytochrome. Iron 69-73 cytochrome c, somatic Homo sapiens 42-54 17783358-0 1948 Cytochrome C Labeled With Radioactive Iron. Iron 38-42 cytochrome c, somatic Homo sapiens 0-12 33597529-0 2021 Short-lived metal-centered excited state initiates iron-methionine photodissociation in ferrous cytochrome c. Iron 51-55 cytochrome c, somatic Homo sapiens 96-108 33597529-2 2021 We report a study of the photodissociation mechanism for the Fe(II)-S bond between the heme iron and methionine sulfur of ferrous cytochrome c. Iron 92-96 cytochrome c, somatic Homo sapiens 130-142 33705282-5 2021 The alkaline isomerization of cyt c in the presence of 8 M urea, measured by Trp59 fluorescence, implied an existence of a high-affinity non-native ligand for the heme iron even in a partially denatured protein conformation. Iron 168-172 cytochrome c, somatic Homo sapiens 30-35 33705282-8 2021 The high affinity of the sixth ligand for the heme iron is likely a reason of the lack of peroxidase activity of cyt c in the alkaline state. Iron 51-55 cytochrome c, somatic Homo sapiens 113-118 32971361-6 2020 However, Fe-S clusters associated with the CPC motif are essential to facilitate the two-electron to one-electron transfer for reducing cytochrome C. Iron 9-13 cytochrome c, somatic Homo sapiens 136-148 32244917-1 2020 It is well known that axial coordination of heme iron in mitochondrial cytochrome c has redox-dependent stability. Iron 49-53 cytochrome c, somatic Homo sapiens 71-83 32020293-8 2020 Therefore, in Cyt with C2 and C3, less intensive reduction of hem iron leaves more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. Iron 66-70 cytochrome c, somatic Homo sapiens 14-17 30807173-10 2019 Raman spectra suggest that both oxidation and spin state of heme iron change when cyt c is adsorbed on SNPs but not on SNPs-APTES. Iron 65-69 cytochrome c, somatic Homo sapiens 82-87 30873034-6 2019 Meanwhile, we found that iron overload induced by 100 muM FAC significantly inhibited mitochondrial fission protein FIS1 and fusion protein MFN2 expressions, inhibited DRP1 and Cytochrome C protein translocation from the cytoplasm to mitochondria. Iron 25-29 cytochrome c, somatic Homo sapiens 177-189 30881663-2 2019 Peroxidase catalysis requires a vacant Fe coordination site, i.e., cyt c must undergo an activation process involving structural changes that rupture the native Met80-Fe contact. Iron 39-41 cytochrome c, somatic Homo sapiens 67-72 30881663-2 2019 Peroxidase catalysis requires a vacant Fe coordination site, i.e., cyt c must undergo an activation process involving structural changes that rupture the native Met80-Fe contact. Iron 167-169 cytochrome c, somatic Homo sapiens 67-72 30282605-2 2018 Cyt c possesses also peroxidase-like activity in the native state despite its six-coordinated heme iron. Iron 99-103 cytochrome c, somatic Homo sapiens 0-5 30268500-0 2018 Alternative pathway linked by hydrogen bonds connects heme-Fe of cytochrome c with subunit II-CuA of cytochrome a. Iron 59-61 cytochrome c, somatic Homo sapiens 65-77 29856995-11 2018 Partial unfolding of CytC in the complex was evidenced by (a) appearance of fluorescence of tyrosine and tryptophan residues and (b) disappearance of the absorption band at 699 nm due to breakdown of heme iron - methionine bond > F S(Met80). Iron 205-209 cytochrome c, somatic Homo sapiens 21-25 29709179-2 2018 Using cytochrome c (cyt c) as a platform, we investigated its structural dynamics during folding processes triggered by local environmental changes (i.e., pH or heme iron center oxidation/spin/ligation states) with time-resolved X-ray solution scattering measurements. Iron 129-133 cytochrome c, somatic Homo sapiens 6-18 29709179-2 2018 Using cytochrome c (cyt c) as a platform, we investigated its structural dynamics during folding processes triggered by local environmental changes (i.e., pH or heme iron center oxidation/spin/ligation states) with time-resolved X-ray solution scattering measurements. Iron 129-133 cytochrome c, somatic Homo sapiens 20-25 29510335-1 2018 The Met80-heme iron bond of cytochrome c (cyt c) is cleaved by the interaction of cyt c with cardiolipin (CL) in membranes. Iron 15-19 cytochrome c, somatic Homo sapiens 28-40 29510335-1 2018 The Met80-heme iron bond of cytochrome c (cyt c) is cleaved by the interaction of cyt c with cardiolipin (CL) in membranes. Iron 15-19 cytochrome c, somatic Homo sapiens 42-47 29510335-1 2018 The Met80-heme iron bond of cytochrome c (cyt c) is cleaved by the interaction of cyt c with cardiolipin (CL) in membranes. Iron 15-19 cytochrome c, somatic Homo sapiens 82-87 27632558-0 2017 Probing the conformational changes and peroxidase-like activity of cytochrome c upon interaction with iron nanoparticles. Iron 102-106 cytochrome c, somatic Homo sapiens 67-79 27632558-1 2017 Herein, the interaction of iron nanoparticle (Fe-NP) with cytochrome c (Cyt c) was investigated, and a range of techniques such as dynamic light scattering (DLS), zeta potential measurements, static and synchronous fluorescence spectroscopy, near and far circular dichroism (CD) spectroscopy, and ultraviolet-visible (UV-vis) spectroscopy were used to analyze the interaction between Cyt c and Fe-NP. Iron 27-31 cytochrome c, somatic Homo sapiens 58-70 27632558-1 2017 Herein, the interaction of iron nanoparticle (Fe-NP) with cytochrome c (Cyt c) was investigated, and a range of techniques such as dynamic light scattering (DLS), zeta potential measurements, static and synchronous fluorescence spectroscopy, near and far circular dichroism (CD) spectroscopy, and ultraviolet-visible (UV-vis) spectroscopy were used to analyze the interaction between Cyt c and Fe-NP. Iron 27-31 cytochrome c, somatic Homo sapiens 72-77 28246923-3 2017 The peroxidase activity of cyt c increases by Met80 dissociation from the heme iron, which may trigger apoptosis. Iron 79-83 cytochrome c, somatic Homo sapiens 27-32 28246923-6 2017 According to differential scanning calorimetric measurements, Met80 coordination to the heme iron had an effect on the stabilization of the monomer (DeltaH = 16 kcal/mol), whereas no large difference was observed between the dimer-to-monomer dissociation temperatures of WT and M80A cyt c (61.0 C). Iron 93-97 cytochrome c, somatic Homo sapiens 283-288 28246923-7 2017 The activation enthalpy values were similar and relatively large for the dissociation of both WT and M80A cyt c dimers (WT, 120 +- 10 kcal/mol; M80A, 110 +- 10 kcal/mol), indicating that the dimers suffered large structural changes upon dissociation to monomers independent of the Met80 coordination to the heme iron. Iron 312-316 cytochrome c, somatic Homo sapiens 106-111 28642436-1 2017 The multifunctional protein cytochrome c (cyt c) plays key roles in electron transport and apoptosis, switching function by modulating bonding between a heme iron and the sulfur in a methionine residue. Iron 158-162 cytochrome c, somatic Homo sapiens 28-40 28642436-1 2017 The multifunctional protein cytochrome c (cyt c) plays key roles in electron transport and apoptosis, switching function by modulating bonding between a heme iron and the sulfur in a methionine residue. Iron 158-162 cytochrome c, somatic Homo sapiens 42-47 28474881-0 2017 Remote Perturbations in Tertiary Contacts Trigger Ligation of Lysine to the Heme Iron in Cytochrome c. Iron 81-85 cytochrome c, somatic Homo sapiens 89-101 28474881-2 2017 In cytochrome c (cyt c), ligation of Met80 to the heme iron is critical for the protein"s electron-transfer (ET) function in oxidative phosphorylation and for suppressing its peroxidase activity in apoptosis. Iron 55-59 cytochrome c, somatic Homo sapiens 3-15 28474881-2 2017 In cytochrome c (cyt c), ligation of Met80 to the heme iron is critical for the protein"s electron-transfer (ET) function in oxidative phosphorylation and for suppressing its peroxidase activity in apoptosis. Iron 55-59 cytochrome c, somatic Homo sapiens 17-22 28418677-4 2017 Moreover, UV-visible absorption and resonance Raman spectra reveal that the conformational ensemble of membrane bound cytochrome c is dominated by a mixture of conformers with pentacoordinated and hexacoordinated high-spin heme irons, which contrast with the dominance of low-spin species at neutral pH. Iron 228-233 cytochrome c, somatic Homo sapiens 118-130 28196881-1 2017 Attachment is catalyzed by holocytochrome c synthase (HCCS), leading to two thioether bonds between heme and a conserved CXXCH motif of cyt c In cyt c, histidine (His19) of CXXCH acts as an axial ligand to heme iron and upon release of holocytochrome c from HCCS, folding leads to formation of a second axial interaction with methionine (Met81). Iron 211-215 cytochrome c, somatic Homo sapiens 136-141 28196881-1 2017 Attachment is catalyzed by holocytochrome c synthase (HCCS), leading to two thioether bonds between heme and a conserved CXXCH motif of cyt c In cyt c, histidine (His19) of CXXCH acts as an axial ligand to heme iron and upon release of holocytochrome c from HCCS, folding leads to formation of a second axial interaction with methionine (Met81). Iron 211-215 cytochrome c, somatic Homo sapiens 145-150 26329855-4 2015 It is noteworthy that the Y48pCMF mutation significantly destabilizes the Fe-Met bond in the ferric form of cytochrome c, thereby lowering the pKa value for the alkaline transition of the heme-protein. Iron 74-76 cytochrome c, somatic Homo sapiens 108-120 26038984-4 2015 Herein we report a high-resolution crystal structure of a Lys73-ligated cyt c conformation that reveals intricate change in the heme environment upon this switch in the heme iron ligation. Iron 136-140 cytochrome c, somatic Homo sapiens 72-77 26373048-6 2015 Cytochrome c is adsorbed to graphene with the group heme lying almost perpendicular to the graphene, and the distance between Fe atom and the graphene is 10.15 A, which is shorter than that between electron donor and receptor in many other biosystems. Iron 126-128 cytochrome c, somatic Homo sapiens 0-12 25798458-3 2015 Oxidation of heme iron was observed from the disappearance of the Q band in the UV-vis spectra of Cyt c upon [Cho][AOT] binding above C3. Iron 18-22 cytochrome c, somatic Homo sapiens 98-103 25467855-5 2015 Iron mediates electron transfer as an essential component of e.g. myeloperoxidase, hemoglobin, cytochrome C and ribonucleotide reductase. Iron 0-4 cytochrome c, somatic Homo sapiens 95-107 25706908-6 2015 The C N stretching mode of the incorporated pCNF detected in the IR spectra reveals a surprising difference, which is related to the oxidation state of the heme iron, thus indicating high sensitivity to changes in the electrostatics of cyt c. Iron 161-165 cytochrome c, somatic Homo sapiens 236-241 25224641-0 2014 Self-oxidation of cytochrome c at methionine80 with molecular oxygen induced by cleavage of the Met-heme iron bond. Iron 105-109 cytochrome c, somatic Homo sapiens 18-30 25224641-1 2014 Met80 of cytochrome c (cyt c) has been shown to dissociate from its heme iron when cyt c interacts with cardiolipin (CL), which triggers the release of cyt c into the cytosol initiating apoptosis. Iron 73-77 cytochrome c, somatic Homo sapiens 9-21 25224641-1 2014 Met80 of cytochrome c (cyt c) has been shown to dissociate from its heme iron when cyt c interacts with cardiolipin (CL), which triggers the release of cyt c into the cytosol initiating apoptosis. Iron 73-77 cytochrome c, somatic Homo sapiens 23-28 25224641-1 2014 Met80 of cytochrome c (cyt c) has been shown to dissociate from its heme iron when cyt c interacts with cardiolipin (CL), which triggers the release of cyt c into the cytosol initiating apoptosis. Iron 73-77 cytochrome c, somatic Homo sapiens 83-88 25224641-1 2014 Met80 of cytochrome c (cyt c) has been shown to dissociate from its heme iron when cyt c interacts with cardiolipin (CL), which triggers the release of cyt c into the cytosol initiating apoptosis. Iron 73-77 cytochrome c, somatic Homo sapiens 83-88 25224641-6 2014 These results indicate that Met80 of cyt c is oxidized site-specifically by formation of the oxy and subsequent compound I-like species when Met80 dissociates from the heme iron, where the Met80 modification may affect its peroxidase activity related to apoptosis. Iron 173-177 cytochrome c, somatic Homo sapiens 37-42 25054239-6 2014 Previously, we proposed a four-step model describing HCCS-mediated cytochrome c assembly, identifying a conserved histidine residue (His154) as an axial ligand to the heme iron. Iron 172-176 cytochrome c, somatic Homo sapiens 67-79 24649965-9 2014 These observations can be explained if the iron-sulfur clusters are involved in stabilizing the electron; the ~50 ms residence time of the electron on FA or FB is sufficiently long to allow cytochrome c6 to reduce P700(+), thereby eliminating the recombination channel. Iron 43-47 cytochrome c, somatic Homo sapiens 190-202 24447894-4 2014 NO2 oxidizes iron(II)cytochrome c with a second-order rate constant of (6.6+-0.5)x10(7) M(-1) s(-1) at pH 7.4; formation of iron(III)cytochrome c is quantitative. Iron 13-17 cytochrome c, somatic Homo sapiens 21-33 24447894-4 2014 NO2 oxidizes iron(II)cytochrome c with a second-order rate constant of (6.6+-0.5)x10(7) M(-1) s(-1) at pH 7.4; formation of iron(III)cytochrome c is quantitative. Iron 13-17 cytochrome c, somatic Homo sapiens 133-145 24447894-5 2014 Based on these rate constants, we propose that the reaction with iron(II)cytochrome c proceeds via a mechanism in which 90% of NO2 oxidizes the iron center directly-most probably via reaction at the solvent-accessible heme edge-whereas 10% oxidizes the amino acid residues to the corresponding radicals, which, in turn, oxidize iron(II). Iron 65-69 cytochrome c, somatic Homo sapiens 73-85 24447894-6 2014 Iron(II)cytochrome c is also oxidized by peroxynitrite in the presence of CO2 to iron(III)cytochrome c, with a yield of ~60% relative to peroxynitrite. Iron 0-4 cytochrome c, somatic Homo sapiens 8-20 24447894-6 2014 Iron(II)cytochrome c is also oxidized by peroxynitrite in the presence of CO2 to iron(III)cytochrome c, with a yield of ~60% relative to peroxynitrite. Iron 0-4 cytochrome c, somatic Homo sapiens 90-102 24447894-6 2014 Iron(II)cytochrome c is also oxidized by peroxynitrite in the presence of CO2 to iron(III)cytochrome c, with a yield of ~60% relative to peroxynitrite. Iron 81-85 cytochrome c, somatic Homo sapiens 8-20 24447894-6 2014 Iron(II)cytochrome c is also oxidized by peroxynitrite in the presence of CO2 to iron(III)cytochrome c, with a yield of ~60% relative to peroxynitrite. Iron 81-85 cytochrome c, somatic Homo sapiens 90-102 24329121-2 2014 Induction of the peroxidase activity of cytochrome c is ascribed to partial unfolding and loss of axial co-ordination between the haem Fe and Met80, and is thought to be triggered by interaction of cytochrome c with cardiolipin (diphosphatidylglycerol) in vivo. Iron 135-137 cytochrome c, somatic Homo sapiens 40-52 24329121-2 2014 Induction of the peroxidase activity of cytochrome c is ascribed to partial unfolding and loss of axial co-ordination between the haem Fe and Met80, and is thought to be triggered by interaction of cytochrome c with cardiolipin (diphosphatidylglycerol) in vivo. Iron 135-137 cytochrome c, somatic Homo sapiens 198-210 25189388-3 2014 Unlike the native protein, cytochrome c within the complex binds ligands rapidly; in particular, NO can coordinate to either the ferric or ferrous iron of the heme. Iron 147-151 cytochrome c, somatic Homo sapiens 27-39 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. Iron 91-95 cytochrome c, somatic Homo sapiens 16-28 23779234-2 2013 The proposed mechanism of this molybdenum cofactor dependent enzyme involves two one-electron intramolecular electron transfer (IET) steps from the molybdenum center to the iron of the b 5-type heme and two one-electron intermolecular electron transfer steps from the heme to cytochrome c. Iron 173-177 cytochrome c, somatic Homo sapiens 276-288 23334161-6 2013 All residue 41 variants decreased the pK (a) of a structural transition of oxidized cytochrome c to the alkaline conformation, and this correlated with a destabilization of the interaction of Met-80 with the heme iron(III) at physiological pH. Iron 229-233 cytochrome c, somatic Homo sapiens 100-112 23433116-4 2013 The formation of carbonyl compounds and the release of iron were obtained in salsolinol- treated cytochrome c. Iron 55-59 cytochrome c, somatic Homo sapiens 97-109 23433116-5 2013 Salsolinol also led to the release of iron from cytochrome c. Iron 38-42 cytochrome c, somatic Homo sapiens 48-60 23433116-6 2013 Reactive oxygen species (ROS) scavengers and iron specific chelator inhibited the salsolinol-mediated cytochrome c modification and carbonyl compound formation. Iron 45-49 cytochrome c, somatic Homo sapiens 102-114 23433116-7 2013 It is suggested that oxidative damage of cytochrome c by salsolinol might induce the increase of iron content in cells, subsequently leading to the deleterious condition which was observed. Iron 97-101 cytochrome c, somatic Homo sapiens 41-53 23581600-1 2013 Iron is an essential component in the structure of certain molecules such as hemoglobin (Hb), myoglobin, cytochrome C and some enzymes. Iron 0-4 cytochrome c, somatic Homo sapiens 105-117 23001667-5 2012 Iron-limited cultures also exhibit decreased cytochrome c-to-total protein ratios and cell-specific sulfate reduction rates (csSRR), implying changes in the electron transport chain that couples carbon and sulfur metabolisms. Iron 0-4 cytochrome c, somatic Homo sapiens 45-57 22803508-2 2012 Once in a complex with cardiolipin, cytochrome c has been shown to undergo a conformational change that leads to the rupture of the bond between the heme iron and the intrinsic sulfur ligand of a methionine residue and to enhance the peroxidatic properties of the protein considered important to its apoptotic activity. Iron 154-158 cytochrome c, somatic Homo sapiens 36-48 22817703-3 2012 On the one hand, TERS measurements on a single mitochondrion are discussed, monitoring the oxidation state of the central iron ion of cytochrome c, leading towards a single protein characterization scheme in a natural environment. Iron 122-126 cytochrome c, somatic Homo sapiens 134-146 22432601-1 2012 Geminate recombination of the methionine ligand to the heme iron in ferrous cytochrome c protein following photodissociation displays rich kinetics. Iron 60-64 cytochrome c, somatic Homo sapiens 76-88 22454108-0 2012 Reductive activation of the heme iron-nitrosyl intermediate in the reaction mechanism of cytochrome c nitrite reductase: a theoretical study. Iron 33-37 cytochrome c, somatic Homo sapiens 89-101 22365930-2 2012 The latter occurs by insertion into cytochrome c of an acyl chain, resulting in the dissociation of the axial Met-80 heme-iron ligand. Iron 122-126 cytochrome c, somatic Homo sapiens 36-48 22310496-0 2012 Spectroscopic characterization of (57)Fe-enriched cytochrome c. Iron 38-40 cytochrome c, somatic Homo sapiens 50-62 22310496-1 2012 Investigation of the heme iron dynamics in cytochrome c with Mossbauer spectroscopy and especially nuclear resonance vibrational spectroscopy requires the replacement of the natural abundant heme iron with the (57)Fe isotope. Iron 26-30 cytochrome c, somatic Homo sapiens 43-55 22310496-1 2012 Investigation of the heme iron dynamics in cytochrome c with Mossbauer spectroscopy and especially nuclear resonance vibrational spectroscopy requires the replacement of the natural abundant heme iron with the (57)Fe isotope. Iron 196-200 cytochrome c, somatic Homo sapiens 43-55 22310496-1 2012 Investigation of the heme iron dynamics in cytochrome c with Mossbauer spectroscopy and especially nuclear resonance vibrational spectroscopy requires the replacement of the natural abundant heme iron with the (57)Fe isotope. Iron 214-216 cytochrome c, somatic Homo sapiens 43-55 21967884-0 2011 Nitration of tyrosines 46 and 48 induces the specific degradation of cytochrome c upon change of the heme iron state to high-spin. Iron 106-110 cytochrome c, somatic Homo sapiens 69-81 21967884-6 2011 Altogether the resulting data suggest that nitration of tyrosines 46 and 48 makes Cc easily degradable upon turning the heme iron state to high-spin. Iron 125-129 cytochrome c, somatic Homo sapiens 82-84 21870858-4 2011 Here we demonstrate that our prior phenomological data can be understood quantitatively in the loss of the methionine ligand of the heme iron, using the cytochrome c from Hydrogenbacter thermophilum as a model system. Iron 137-141 cytochrome c, somatic Homo sapiens 153-165 21128733-3 2011 Under conditions where the sixth coordination position at the cytochrome c heme iron becomes more accessible for exogenous ligands (by carboxymethylation, cardiolipin addition or by partial denaturation with guanidinium hydrochloride) this peroxidase activity is enhanced. Iron 80-84 cytochrome c, somatic Homo sapiens 62-74 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. Iron 148-152 cytochrome c, somatic Homo sapiens 42-47 20599734-4 2010 Upon oxidation of the heme iron in Cyt c, the average S2 value was increased from 0.88+/-0.01 to 0.92+/-0.01, demonstrating that the mobility of the backbone is further restricted in the oxidized form. Iron 27-31 cytochrome c, somatic Homo sapiens 35-40 20398641-4 2010 The peroxidase activity of Cyt c proceeded via the opening of the tertiary structure of Cyt c, as suggested by the loss of the sixth coordination bond of the heme-iron. Iron 163-167 cytochrome c, somatic Homo sapiens 27-32 20398641-4 2010 The peroxidase activity of Cyt c proceeded via the opening of the tertiary structure of Cyt c, as suggested by the loss of the sixth coordination bond of the heme-iron. Iron 163-167 cytochrome c, somatic Homo sapiens 88-93 19683594-7 2009 Spectral data indicate that both cytochrome c protein structure and a +3 heme iron oxidation state are required for the reaction mechanism to proceed optimally. Iron 78-82 cytochrome c, somatic Homo sapiens 33-45 19720549-7 2009 Without Fe...S bond, the backbone and Calpha RMSD increased in holo cyt c"s perhaps resulting in enhanced peroxidase activity. Iron 8-10 cytochrome c, somatic Homo sapiens 68-73 19601561-1 2009 The interaction of cytochrome C and a number of its components such as the apo protein, heme and a coordinated iron with gold nanospheres, has been investigated. Iron 111-115 cytochrome c, somatic Homo sapiens 19-31 19721088-0 2009 Cytochrome c biogenesis: mechanisms for covalent modifications and trafficking of heme and for heme-iron redox control. Iron 100-104 cytochrome c, somatic Homo sapiens 0-12 19629033-6 2009 Thus, this ancient pathway has conserved and orchestrated mechanisms for trafficking, storing and reducing haem, which assure its use for cytochrome c synthesis even in limiting haem (iron) environments and reducing haem in oxidizing environments. Iron 184-188 cytochrome c, somatic Homo sapiens 138-150 19415898-1 2009 During the operation of cytochrome bc(1), a key enzyme of biological energy conversion, the iron-sulfur head domain of one of the subunits of the catalytic core undergoes a large-scale movement from the catalytic quinone oxidation Q(o) site to cytochrome c(1). Iron 92-96 cytochrome c, somatic Homo sapiens 244-256 19296689-4 2009 The 11 mutants of human cyt c expressed in the course of this research have been characterized by UV-vis spectroscopy, circular dichroism, and NMR spectroscopy to verify overall structure integrity as well as axial coordination of the heme iron. Iron 240-244 cytochrome c, somatic Homo sapiens 24-29 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. Iron 176-180 cytochrome c, somatic Homo sapiens 186-191 19196960-1 2009 Native cytochrome c (cyt c) has a compact tertiary structure with a hexacoordinated heme iron and functions in electron transport in mitochondria and apoptosis in the cytoplasm. Iron 89-93 cytochrome c, somatic Homo sapiens 7-19 19196960-1 2009 Native cytochrome c (cyt c) has a compact tertiary structure with a hexacoordinated heme iron and functions in electron transport in mitochondria and apoptosis in the cytoplasm. Iron 89-93 cytochrome c, somatic Homo sapiens 21-26 19173569-0 2009 Vibrational dynamics of iron in cytochrome C. Iron 24-28 cytochrome c, somatic Homo sapiens 32-44 19173569-1 2009 Nuclear resonance vibrational spectroscopy (NRVS) and Raman spectroscopy on (54)Fe- and (57)Fe-enriched cytochrome c (cyt c) identify multiple bands involving vibrations of the heme Fe. Iron 92-94 cytochrome c, somatic Homo sapiens 104-116 19173569-1 2009 Nuclear resonance vibrational spectroscopy (NRVS) and Raman spectroscopy on (54)Fe- and (57)Fe-enriched cytochrome c (cyt c) identify multiple bands involving vibrations of the heme Fe. Iron 92-94 cytochrome c, somatic Homo sapiens 118-123 19173569-4 2009 The stiffness of the low-spin Fe environment in both oxidation states of cyt c significantly exceeds that for the high-spin Fe in deoxymyoglobin, where the 200-300 cm(-1) frequency range dominates the VDOS. Iron 30-32 cytochrome c, somatic Homo sapiens 73-78 19173569-6 2009 The longer Fe-S(Met80) in oxidized cyt c with respect to reduced cyt c leads to a decrease in the stiffness of the iron environment upon oxidation. Iron 11-15 cytochrome c, somatic Homo sapiens 35-40 19173569-6 2009 The longer Fe-S(Met80) in oxidized cyt c with respect to reduced cyt c leads to a decrease in the stiffness of the iron environment upon oxidation. Iron 11-15 cytochrome c, somatic Homo sapiens 65-70 19173569-6 2009 The longer Fe-S(Met80) in oxidized cyt c with respect to reduced cyt c leads to a decrease in the stiffness of the iron environment upon oxidation. Iron 115-119 cytochrome c, somatic Homo sapiens 35-40 19173569-6 2009 The longer Fe-S(Met80) in oxidized cyt c with respect to reduced cyt c leads to a decrease in the stiffness of the iron environment upon oxidation. Iron 115-119 cytochrome c, somatic Homo sapiens 65-70 19173569-8 2009 We consider the possibility that the 372 cm(-1) band in reduced cyt c involves the Fe-S(Met80) bond. Iron 83-87 cytochrome c, somatic Homo sapiens 64-69 18555026-9 2008 In addition, the enzymatic site of cytochrome c was sensitive to the attack of both superoxide and hydroxyl radicals as observed through the reduction of Fe(3+), the degradation of the protoporphyrin IX and the oxidative disruption of the Met80-Fe(3+) bond. Iron 154-156 cytochrome c, somatic Homo sapiens 35-47 18468515-2 2008 We evaluated the superoxide (O2*-) scavenging activities of PFD and the PFD-iron complex by electron spin resonance (ESR) spectroscopy, luminol-dependent chemiluminescence assay, and cytochrome c reduction assay. Iron 76-80 cytochrome c, somatic Homo sapiens 183-195 18439415-5 2008 Experiments replacing the Fe of cytochrome c with redox-inactive metals indicate that cytochrome c does not have to change redox states to activate caspases. Iron 26-28 cytochrome c, somatic Homo sapiens 32-44 18439415-5 2008 Experiments replacing the Fe of cytochrome c with redox-inactive metals indicate that cytochrome c does not have to change redox states to activate caspases. Iron 26-28 cytochrome c, somatic Homo sapiens 86-98 17804076-3 2007 Cytochrome c also loads iron into recombinant human H-chain (rHF), human L-chain (rLF), and A. vinelandii bacterioferritin (AvBF). Iron 24-28 cytochrome c, somatic Homo sapiens 0-12 17761303-7 2007 Further, UV-visible spectroscopic studies show that during the reduction process the coordination environment and redox state of iron in cyt c are changed. Iron 101-105 cytochrome c, somatic Homo sapiens 137-142 17612631-1 2007 The loop segment comprising residues 70-84 in mitochondrial cytochrome c serves to direct the polypeptide backbone to permit the functionally required heme Fe - S (Met-80) co-ordination. Iron 156-162 cytochrome c, somatic Homo sapiens 60-72 16944229-6 2007 Similarly, both the general reaction pattern and detailed kinetics and thermodynamics data point to a regiospecific addition reaction of P(OMe)(3) directed at the heme iron within multiply charged ions from cyt c. Iron 168-172 cytochrome c, somatic Homo sapiens 207-212 17004073-2 2007 With iron(III) cytochrome c, CO (3) (*-) reacts with the protein moiety with rate constants of (5.1 +/- 0.6) x 10(7) M(-1) s(-1) (pH 8.4, I approximately 0.27 M) and (1.0 +/- 0.2) x 10(8) M(-1) s(-1) (pH 10, I = 0.5 M). Iron 5-9 cytochrome c, somatic Homo sapiens 15-27 17004073-6 2007 We propose that CO (3) (*-) oxidizes the iron center directly, and that the lower rate observed at pH 10 is due to the different charge distribution of iron(II) cytochrome c. Iron 41-45 cytochrome c, somatic Homo sapiens 161-173 17004073-6 2007 We propose that CO (3) (*-) oxidizes the iron center directly, and that the lower rate observed at pH 10 is due to the different charge distribution of iron(II) cytochrome c. Iron 152-156 cytochrome c, somatic Homo sapiens 161-173 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. Iron 128-132 cytochrome c, somatic Homo sapiens 38-50 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. Iron 128-132 cytochrome c, somatic Homo sapiens 138-150 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. Iron 228-232 cytochrome c, somatic Homo sapiens 41-53 17037839-3 2006 Irradiation of the NDI in solution with UV light (365 nm), in the presence of cyt c, resulted in the reduction of the heme iron from the Fe3+ to the Fe2+ state. Iron 123-127 cytochrome c, somatic Homo sapiens 78-83 16889691-5 2006 Incubation of cytochrome c with H2O2 resulted in a time-dependent release of iron ions from the cytochrome c molecule. Iron 77-81 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. Iron 77-81 cytochrome c, somatic Homo sapiens 96-108 16889691-6 2006 During the incubation of deoxyribose with cytochrome c and H2O2, the damage to deoxyribose increased in a time-dependent manner, suggesting that the released iron ions may participate in a Fenton-like reaction to produce dOH radicals that may cause the DNA cleavage. Iron 158-162 cytochrome c, somatic Homo sapiens 42-54 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. Iron 18-22 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. Iron 169-173 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. Iron 169-173 cytochrome c, somatic Homo sapiens 213-225 16678819-2 2006 Here, we demonstrate that the transient interaction between soluble cytochrome c(6) and membrane-embedded photosystem I involves subtle changes in the heme iron, as inferred by X-ray absorption spectroscopy (XAS). Iron 156-160 cytochrome c, somatic Homo sapiens 68-80 16605268-9 2006 This catalytic activity correlated with partial unfolding of cyt c monitored by Trp(59) fluorescence and absorbance at 695 nm (Fe-S(Met(80)) band). Iron 127-131 cytochrome c, somatic Homo sapiens 61-66 16677095-4 2006 Presumably as a consequence of the iron-sulfur cluster defect, cytochrome c heme is deficient in mutants, as well as heme-dependent Complex IV. Iron 35-39 cytochrome c, somatic Homo sapiens 63-75 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. Iron 167-171 cytochrome c, somatic Homo sapiens 50-62 15853810-1 2005 NMR and visible spectroscopy coupled to redox measurements were used to determine the equilibrium thermodynamic properties of the four haems in cytochrome c3 under conditions in which the protein was bound to ligands, the small anion phosphate and the protein rubredoxin with the iron in the active site replaced by zinc. Iron 280-284 cytochrome c, somatic Homo sapiens 144-156 15839648-1 2005 The physiological electron-transfer (ET) partners, cytochrome c peroxidase (CcP) and cytochrome c (Cc)1, can be modified to exhibit photoinitiated ET through substitution of Zn (or Mg) for Fe in either partner. Iron 189-191 cytochrome c, somatic Homo sapiens 51-63 15792874-6 2005 UV irradiation (365 nm) of solutions containing DNDI and the redox protein cytochrome c (cyt c) resulted in the reduction of the heme iron from the Fe(III) to the Fe(II) state, a reaction that was inhibited by the incorporation of DNDI into CTAB micelles. Iron 134-138 cytochrome c, somatic Homo sapiens 75-87 15792874-6 2005 UV irradiation (365 nm) of solutions containing DNDI and the redox protein cytochrome c (cyt c) resulted in the reduction of the heme iron from the Fe(III) to the Fe(II) state, a reaction that was inhibited by the incorporation of DNDI into CTAB micelles. Iron 134-138 cytochrome c, somatic Homo sapiens 89-94 15843899-4 2005 Iron deprivation led to the release of cytochrome c from mitochondria into the cytosol only in sensitive cells but it did not affect the cytosolic localization of Apaf-1 in both sensitive and resistant cells. Iron 0-4 cytochrome c, somatic Homo sapiens 39-51 15843899-8 2005 Taken together, we suggest that iron deprivation induces apoptosis via mitochondrial changes concerning proapoptotic Bax translocation to mitochondria, collapse of the mitochondrial membrane potential, release of cytochrome c from mitochondria, and activation of caspase-9 and caspase-3. Iron 32-36 cytochrome c, somatic Homo sapiens 213-225 15588700-0 2004 The heme iron coordination of unfolded ferric and ferrous cytochrome c in neutral and acidic urea solutions. Iron 9-13 cytochrome c, somatic Homo sapiens 58-70 15588700-2 2004 The heme iron coordination of unfolded ferric and ferrous cytochrome c in the presence of 7-9 M urea at different pH values has been probed by several spectroscopic techniques including magnetic and natural circular dichroism (CD), electrochemistry, UV-visible (UV-vis) absorption and resonance Raman (RR). Iron 9-13 cytochrome c, somatic Homo sapiens 58-70 15506748-2 2004 In resting cyt c, two endogenous ligands of the heme iron are histidine-18 (His) and methionine-80 (Met) side chains, and NO binding requires the cleavage of one of the axial bonds. Iron 53-57 cytochrome c, somatic Homo sapiens 11-16 15623339-5 2004 Flash photolysis studies revealed that the actual reductant in the reaction was a photogenerated BPNDI radical anion, which transferred an electron to the cyt c heme iron. Iron 166-170 cytochrome c, somatic Homo sapiens 155-160 15155756-0 2004 Two distinct binding sites for high potential iron-sulfur protein and cytochrome c on the reaction center-bound cytochrome of Rubrivivax gelatinosus. Iron 46-50 cytochrome c, somatic Homo sapiens 70-82 15231239-4 2004 These findings indicate aberrations in iron homeostasis that, we suspect, arise primarily from heme, since heme oxygenase-1, an enzyme that catalyzes the conversion of heme to iron and biliverdin, is increased in AD, and mitochondria, since mitochondria turnover, mitochondrial DNA, and cytochrome C oxidative activity are all increased in AD. Iron 39-43 cytochrome c, somatic Homo sapiens 287-299 16228609-4 2004 On the basis of X-ray crystallographic studies of cytochrome bc (1), it has been proposed that the Rieske iron-sulfur protein undergoes large conformational changes as it transports electrons from ubiquinol to cytochrome c (1). Iron 106-110 cytochrome c, somatic Homo sapiens 210-222 16228609-6 2004 The rate constant for electron transfer from the iron-sulfur center to cytochrome c (1) was found to be 80,000 s(-1), and is controlled by the dynamics of conformational changes in the iron-sulfur protein. Iron 49-53 cytochrome c, somatic Homo sapiens 71-83 14606851-6 2003 This result suggests that the steric environment near the heme iron in cyt c discriminates against coordination of Met(SO)-80. Iron 40-44 cytochrome c, somatic Homo sapiens 71-76 12959597-4 2003 The binding of cyt c to negatively charged SPS particles causes an extensive disruption of the native compact structure of cyt c: the cleavage of Fe-Met80 ligand, about 40% loss of the helical structure, and the disruption of the asymmetry environment of Trp59. Iron 146-148 cytochrome c, somatic Homo sapiens 15-20 12959597-4 2003 The binding of cyt c to negatively charged SPS particles causes an extensive disruption of the native compact structure of cyt c: the cleavage of Fe-Met80 ligand, about 40% loss of the helical structure, and the disruption of the asymmetry environment of Trp59. Iron 146-148 cytochrome c, somatic Homo sapiens 123-128 14499930-6 2003 In contrast, the heme group is not destroyed during glycation of cytochrome c, where the sixth coordination position of the heme iron is not accessible to solvent ligands. Iron 129-133 cytochrome c, somatic Homo sapiens 65-77 12646553-3 2003 Here we demonstrate that cytochrome c is nitrosylated on its heme iron during apoptosis. Iron 66-70 cytochrome c, somatic Homo sapiens 25-37 12646553-9 2003 We conclude that nitrosylation of the heme iron of cytochrome c may be a novel mechanism of apoptosis regulation. Iron 43-47 cytochrome c, somatic Homo sapiens 51-63 12628824-1 2003 Transparent protein film of iron-free cytochrome c (Cyt. Iron 28-32 cytochrome c, somatic Homo sapiens 38-50 12675926-6 2003 Levels of cytochrome c were increased while levels of pro-caspase-9 and pro-caspase-3 were decreased in cytosolic fractions of iron-treated hippocampal slice cultures. Iron 127-131 cytochrome c, somatic Homo sapiens 10-22 12429017-0 2003 Modulation of cytochrome c spin states by lipid acyl chains: a continuous-wave electron paramagnetic resonance (CW-EPR) study of haem iron. Iron 134-138 cytochrome c, somatic Homo sapiens 14-26 14515162-2 2003 It was found that the heme iron in ferric cytochrome c does not react directly with peroxynitrite. Iron 27-31 cytochrome c, somatic Homo sapiens 42-54 12136141-7 2002 The binding constants and the electron-transfer rates between cytochrome b(5) and cytochrome c decrease owing to the mutation, which can be accounted for by molecular modeling: the inter-iron distances increase in order to eliminate the unreasonably close contacts resulting from the large volumes of the mutated side chains. Iron 187-191 cytochrome c, somatic Homo sapiens 82-94 12084923-1 2002 Replacement of iron with cobalt(III) selectively introduces a deep trap in the folding-energy landscape of the heme protein cytochrome c. Iron 15-19 cytochrome c, somatic Homo sapiens 124-136 11996572-1 2002 Axial iron ligation and protein encapsulation of the heme cofactor have been investigated as effectors of the reduction potential (E degrees ") of cytochrome c through direct electrochemistry experiments. Iron 6-10 cytochrome c, somatic Homo sapiens 147-159 11996572-4 2002 These ligands replace Met80 and a water molecule axially coordinated to the heme iron in cytochrome c and MP11, respectively. Iron 81-85 cytochrome c, somatic Homo sapiens 89-101 11939777-5 2002 The two heme groups have nearly parallel heme planes and are stacked at van der Waals distances with an iron-to-iron distance of only 9.9 A, two structural features that are also present in the split-Soret diheme cytochrome c from Desulfovibrio desulfuricans ATCC 27774, which is otherwise unrelated in the peptide chain folding pattern. Iron 104-108 cytochrome c, somatic Homo sapiens 213-225 11939777-5 2002 The two heme groups have nearly parallel heme planes and are stacked at van der Waals distances with an iron-to-iron distance of only 9.9 A, two structural features that are also present in the split-Soret diheme cytochrome c from Desulfovibrio desulfuricans ATCC 27774, which is otherwise unrelated in the peptide chain folding pattern. Iron 112-116 cytochrome c, somatic Homo sapiens 213-225 12007804-5 2002 One cytochrome c was specific for sulfur conditions while three were specific for iron conditions, suggesting that cytochrome c synthesis is modulated depending on the electron donor. Iron 82-86 cytochrome c, somatic Homo sapiens 4-16 12007804-5 2002 One cytochrome c was specific for sulfur conditions while three were specific for iron conditions, suggesting that cytochrome c synthesis is modulated depending on the electron donor. Iron 82-86 cytochrome c, somatic Homo sapiens 115-127 11707449-5 2002 These findings indicate that the movement of the iron-sulfur subunit is composed of two discrete parts: a "micro-movement" at the cytochrome b interface, during which the [2Fe-2S] cluster interacts with ubihydroquinone oxidation site occupants and catalyzes ubihydroquinone oxidation, and a "macro-movement," during which the cluster domain swings away from cytochrome b interface, crosses the ef loop, and reaches a position close to cytochrome c(1) heme, to which it ultimately transfers an electron. Iron 49-53 cytochrome c, somatic Homo sapiens 435-447 11786337-1 2002 Photosystem I reduction by the soluble metalloproteins cytochrome c(6) and plastocyanin, which are alternatively synthesized by some photosynthetic organisms depending on the relative availability of copper and iron, has been investigated in cyanobacteria, green algae and plants. Iron 211-215 cytochrome c, somatic Homo sapiens 55-67 11487579-4 2001 Unfolding by guanidine or urea weakens the Fe-Met bond, and the reduced unfolded cytochrome c easily binds CO and other heme ligands, which would react slowly or not at all with the native protein. Iron 43-45 cytochrome c, somatic Homo sapiens 81-93 11487579-6 2001 This approach is complicated by the breakage of the proximal His-Fe bond that may occur as a consequence of CO photodissociation in the unfolded cytochrome c because of the so-called base elimination mechanism. Iron 65-67 cytochrome c, somatic Homo sapiens 145-157 11444611-1 2001 Electrochemical reduction of the iron bound in the heme group of cytochrome c is shown to occur in the nano-electrospray capillary if the protein is sprayed from neutral water using a steel wire as the electrical contact. Iron 33-37 cytochrome c, somatic Homo sapiens 65-77 11444611-2 2001 Quadrupole ion trap collisional activation is used to study the dissociation reactions of cytochrome c as a function of the oxidation state of the iron. Iron 147-151 cytochrome c, somatic Homo sapiens 90-102 11027687-0 2001 Effect of heme iron valence state on the conformation of cytochrome c and its association with membrane interfaces. Iron 15-19 cytochrome c, somatic Homo sapiens 57-69 11027687-6 2001 Magnetic circular dichroism and CD results show that the interaction of both ferrous and ferric cytochrome c with charged interfaces promotes conformational changes in the alpha-helix content, tertiary structure, and heme iron spin state. Iron 222-226 cytochrome c, somatic Homo sapiens 96-108 11027687-7 2001 Moreover, the association of cytochrome c with different liposomes is sensitive to the heme iron valence state. Iron 92-96 cytochrome c, somatic Homo sapiens 29-41 11071875-1 2000 Microperoxidase 8 (MP8) is a heme octapeptide, obtained by enzymatic hydrolysis of heart cytochrome c, in which a histidine is axially coordinated to the heme iron, and acts as its fifth ligand. Iron 159-163 cytochrome c, somatic Homo sapiens 89-101 10754275-0 2000 Modifications in heme iron of free and vesicle bound cytochrome c by tert-butyl hydroperoxide: a magnetic circular dichroism and electron paramagnetic resonance investigation. Iron 22-26 cytochrome c, somatic Homo sapiens 53-65 10754275-2 2000 Direct low-temperature (11 degrees K) EPR analysis of the cytochrome c heme iron on exposure to tert-BuOOH shows a gradual (180 s) conversion of the low-spin form to a high-spin Fe(III) species of rhombic symmetry (g = 4.3), with disappearance of a prior peroxyl radical signal (g(o) = 2.014). Iron 76-80 cytochrome c, somatic Homo sapiens 58-70 10754275-7 2000 The EPR results show that the primary initial change on exposure of cytochrome c to tert-BuOOH is a change to a high-spin Fe(III) species, and together with MCD measurements show that unsaturated cardiolipin-containing lipid membranes influence the interaction of tert-BuOOH with cytochrome c heme iron, to alter radical production and decrease damage to the cytochrome. Iron 298-302 cytochrome c, somatic Homo sapiens 68-80 10625461-5 1999 Indeed, porphyrin cytochrome c (in which the heme iron ion has been removed) is substantially more ordered than apocytochrome c, having characteristics consistent with a molten globule state. Iron 50-54 cytochrome c, somatic Homo sapiens 18-30 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. Iron 224-228 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. Iron 20-24 cytochrome c, somatic Homo sapiens 66-78 10499291-1 1999 The acetylation of the hemeundecapeptide prepared by proteolysis of cytochrome c yields a species di(N-acetyl)-microperoxidase-11, NAcMP11, that is monomeric in aqueous solution at least for concentrations below 20 microM, in contrast to MP11 itself, which aggregates because of intermolecular coordination of Fe(III) by the N-terminal amino group or the amino group of the side chain of Lys-13. Iron 310-312 cytochrome c, somatic Homo sapiens 68-80 9892658-1 1999 An early folding event of cytochrome c populates a helix-containing intermediate (INC) because of a pH-dependent misligation between the heme iron and nonnative ligands in the unfolded state (U). Iron 142-146 cytochrome c, somatic Homo sapiens 26-38 9878421-4 1999 Nevertheless, addition of heme to two short fragments of cytochrome c enhances helical structure substantially (from approximately 8% to approximately 22%), an effect that depends on iron ligation but not thioether linkage. Iron 183-187 cytochrome c, somatic Homo sapiens 57-69 10380081-0 1999 Protonation of porphyrin in iron-free cytochrome c: spectral properties of monocation free base porphyrin, a charge analogue of ferric heme. Iron 28-32 cytochrome c, somatic Homo sapiens 38-50 9699464-3 1998 The addition of the second polyanion to a solution of ferric cytochrome c at a low ionic strength, pH 7.0, resulted in profound conformational change in the hydrophobic core of protein (opening of the heme crevice with a perturbation of the methionine 80-heme iron bond and the hydrophobic core of the protein). Iron 260-264 cytochrome c, somatic Homo sapiens 61-73 9741591-7 1998 This suggests that the peroxidase activity of cytochrome c involves substrate-induced loss of the methionine ligand at the iron sixth coordination position, which is favored by interaction of cytochrome c with negatively charged interfaces. Iron 123-127 cytochrome c, somatic Homo sapiens 46-58 9741591-7 1998 This suggests that the peroxidase activity of cytochrome c involves substrate-induced loss of the methionine ligand at the iron sixth coordination position, which is favored by interaction of cytochrome c with negatively charged interfaces. Iron 123-127 cytochrome c, somatic Homo sapiens 192-204 9746310-2 1998 In this paper, such a phenomenon was analyzed using the chemical kinetics model of electron transfer from succinate to cytochrome c, including coenzyme Q, the complex III non-heme iron protein FeSIII and cytochromes bl, bh and cl. Iron 180-184 cytochrome c, somatic Homo sapiens 119-131 9526125-8 1998 These results show that oxidation of iron has little effect on the N- and C-terminal regions, but significantly destabilizes the interior regions of cytochrome c. Iron 37-41 cytochrome c, somatic Homo sapiens 149-161 9385449-1 1997 According to spectral data the midtransition temperature of the cleavage of the sulfur-iron bond was 57.4 +/- 0.5 degrees C and 66.8 +/- 0.5 degrees C for cytochrome c and cytochrome c-polyglutamate complex, respectively. Iron 87-91 cytochrome c, somatic Homo sapiens 155-167 9385449-1 1997 According to spectral data the midtransition temperature of the cleavage of the sulfur-iron bond was 57.4 +/- 0.5 degrees C and 66.8 +/- 0.5 degrees C for cytochrome c and cytochrome c-polyglutamate complex, respectively. Iron 87-91 cytochrome c, somatic Homo sapiens 172-184 9440316-1 1997 Under excitation by visible light the iron storage protein ferritin catalyses the reduction of cytochrome c and viologens as well as the oxidation of carboxylic acids, thiol compounds, and sulfite. Iron 38-42 cytochrome c, somatic Homo sapiens 95-107 9311786-5 1997 Concomitantly, a refolding of the cytochrome c domain takes place, resulting in an unexpected change of the c haem iron coordination from His 17/His 69 to Met106/His69. Iron 115-119 cytochrome c, somatic Homo sapiens 34-46 9177190-2 1997 Reduced carboxymethylated cytochrome c (CmCyt c) with carbon monoxide bound to the heme iron is mixed with the oxidized acceptor protein. Iron 88-92 cytochrome c, somatic Homo sapiens 26-38 9131042-2 1997 In these studies, a short pulse of 450 nm light was used to excite the ruthenium complex which was oxidatively quenched by the iron center of cytochrome c. Iron 127-131 cytochrome c, somatic Homo sapiens 142-154 9125127-2 1997 scavenging activity of erythromycin (EM) and of EM-iron complex by means of electron spin resonance spectroscopy, luminol-dependent chemiluminescence assay, and cytochrome c reduction assay. Iron 51-55 cytochrome c, somatic Homo sapiens 161-173 9025273-1 1997 Iron(III) in cytochrome c is replaced with zinc(II) by a modification of a method published by others, and the procedure is described in full detail. Iron 0-4 cytochrome c, somatic Homo sapiens 13-25 9025273-2 1997 Three forms of cytochrome c-those containing iron(III), iron(II), and zinc(II)-are examined by circular dichroism spectroscopy and resonance Raman spectroscopy. Iron 45-49 cytochrome c, somatic Homo sapiens 15-27 9025273-2 1997 Three forms of cytochrome c-those containing iron(III), iron(II), and zinc(II)-are examined by circular dichroism spectroscopy and resonance Raman spectroscopy. Iron 56-60 cytochrome c, somatic Homo sapiens 15-27 8804590-1 1996 We performed hole-burning Stark effect experiments on cytochrome c in which the iron of the herne was either removed or replaced by Zn. Iron 80-84 cytochrome c, somatic Homo sapiens 54-66 11666383-0 1996 Possible Role of the Iron Coordination Sphere in Hemoprotein Electron Transfer Self-Exchange: (1)H NMR Study of the Cytochrome c-PMe(3) Complex. Iron 21-25 cytochrome c, somatic Homo sapiens 116-128 7748900-1 1995 The binding of 1-methylimidazole to the heme iron by displacing Met-80 of cytochrome c has been studied by two-dimensional (2D) exchange spectroscopy. Iron 45-49 cytochrome c, somatic Homo sapiens 74-86