PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2844764-1 1988 The oxidation of yeast cytochrome c peroxidase by hydrogen peroxide produces a unique enzyme intermediate, cytochrome c peroxidase Compound I, in which the ferric heme iron has been oxidized to an oxyferryl state, Fe(IV), and an amino acid residue has been oxidized to a radical state. Iron 168-172 cytochrome c, somatic Equus caballus 23-35 2844764-1 1988 The oxidation of yeast cytochrome c peroxidase by hydrogen peroxide produces a unique enzyme intermediate, cytochrome c peroxidase Compound I, in which the ferric heme iron has been oxidized to an oxyferryl state, Fe(IV), and an amino acid residue has been oxidized to a radical state. Iron 168-172 cytochrome c, somatic Equus caballus 107-119 3036144-3 1987 The NO-ferrous cytochrome c" would be a mixture of NO complexes with six- and five-coordinate nitrosylheme, suggesting that the heme-iron to histidine bond in the ferrous cytochrome c" is more stable than that from chemoheterotrophic bacteria. Iron 133-137 cytochrome c, somatic Equus caballus 15-27 2825793-4 1987 Three different forms of complexed cytochrome c have been characterized by optical and EPR spectroscopies, in the pH range 6.5-8: an N form, close to the native structure, an A form, analogous to cytochrome c in acidic medium, and a novel B form in which the heme pocket is open but the iron remains low-spin. Iron 287-291 cytochrome c, somatic Equus caballus 35-47 3036144-3 1987 The NO-ferrous cytochrome c" would be a mixture of NO complexes with six- and five-coordinate nitrosylheme, suggesting that the heme-iron to histidine bond in the ferrous cytochrome c" is more stable than that from chemoheterotrophic bacteria. Iron 133-137 cytochrome c, somatic Equus caballus 171-183 3038167-16 1987 Thus, the rate constant for reduction by horse cytochrome c of the peroxidase species in which only the heme iron atom is oxidized was decreased by only 38%, indicating that this oxidized side-chain group is not tightly coupled to the ferryl peroxidase heme iron. Iron 109-113 cytochrome c, somatic Equus caballus 47-59 3038167-16 1987 Thus, the rate constant for reduction by horse cytochrome c of the peroxidase species in which only the heme iron atom is oxidized was decreased by only 38%, indicating that this oxidized side-chain group is not tightly coupled to the ferryl peroxidase heme iron. Iron 258-262 cytochrome c, somatic Equus caballus 47-59 3034243-3 1987 EPR and electronic spectral results for the ferric cytochrome c" suggest that the ground state of heme-iron(III) at neutral pH consists of a quantum mechanical admixture of an intermediate-spin and a high-spin state and that at pH 11.0 is in a high-spin state. Iron 103-107 cytochrome c, somatic Equus caballus 51-63 4375972-6 1974 Polymers of cytochrome c carboxymethylated on the methionine residue normally ligated to iron show simple CO recombination kinetics after photolytic removal (k(on)=1.5x10(6)m(-1).s(-1) at pH6). Iron 89-93 cytochrome c, somatic Equus caballus 12-24 6251057-5 1980 The similarity between the EPR spectra of the NO complexes of horse heart cytochrome c and the heme d1-depleted Pseudomonas cytochrome oxidase before and after interaction with urea suggests structural similarities involving the heme irons. Iron 234-239 cytochrome c, somatic Equus caballus 74-86 6248529-2 1980 The conformation of cytochrome c in solution is believed to change depending on the oxidation-reduction state of the heme iron, since ferri- and ferrocytochrome c exhibit several different physicochemical properties, but so far it is unknown if the conformational difference(s) is (are) confined to a particular part or domain of the molecule. Iron 122-126 cytochrome c, somatic Equus caballus 20-32 6244304-1 1980 The chemical reactivity of fully maleylated horse heart cytochrome c with oxidants, reductants, and iron ligands was studied in the presence and absence of MgCl2. Iron 100-104 cytochrome c, somatic Equus caballus 56-68 6327700-1 1984 Removal of the heme iron from cytochrome c to generate porphyrin cytochrome c relieves the quenching of porphyrin fluorescence and enhances the fluorescence of the single tryptophan residue and the 4 tyrosine residues. Iron 20-24 cytochrome c, somatic Equus caballus 30-42 6327700-1 1984 Removal of the heme iron from cytochrome c to generate porphyrin cytochrome c relieves the quenching of porphyrin fluorescence and enhances the fluorescence of the single tryptophan residue and the 4 tyrosine residues. Iron 20-24 cytochrome c, somatic Equus caballus 65-77 6304037-0 1983 Preferred sites for electron transfer between cytochrome c and iron and cobalt complexes. Iron 63-67 cytochrome c, somatic Equus caballus 46-58 6277949-0 1982 The conformational transition of horse heart porphyrin c. The heme iron of horse heart cytochrome c was selectively removed using anhydrous HF. Iron 67-71 cytochrome c, somatic Equus caballus 87-99 6260144-1 1981 The electron-transfer mechanism of the Fe4S4 high-potential iron-sulfur proteins (HiPIP"s) was explored via a stopped-flow spectrophotometric kinetic study of the reduction of Chromatium vinosum and Rhodopseudomonas gelatinosa HiPIP"s by both native and trinitrophenyllysine-13 horse cytochrome c. Iron 60-64 cytochrome c, somatic Equus caballus 284-296 6258647-3 1981 Under a constant concentration of anion, the redox reaction of various types of cytochrome c with iron hexacyanides was analyzed according to the scheme: (see formula in text) where C(III) and C(II) are ferric and ferrous cytochromes, respectively, Fe(III) and Fe(II) are ferri- and ferrocyanides, respectively, C(III) . Iron 249-251 cytochrome c, somatic Equus caballus 80-92 6252957-3 1980 To further the understanding of biological electron transfer, we have investigated the interaction of two examples of high-potential iron-sulfur proteins (HIPIP"s) with mitochondrial cytochrome c (horse heart) and bacterial cytochrome c2 from Rhodospirillum rubrum, Rhodopseudomonas palustris, Rhodopseudomonas capsulata, and Rhodopseudomonas sphaeroides. Iron 133-137 cytochrome c, somatic Equus caballus 183-195 6251068-3 1980 In the initial, second order step the two fragments combine to form an intermediate complex which exhibits tryptophan 59 fluorescence quenching similar to native cytochrome c, but which has not yet achieved the native ligation state of the heme iron. Iron 245-249 cytochrome c, somatic Equus caballus 162-174 189301-7 1977 We have calculated a volume change of --50 cm3/mol associated with the configurational change accompanying the reformation of the iron-methionine bond in cytochrome c at low pH. Iron 130-134 cytochrome c, somatic Equus caballus 154-166 4375972-7 1974 We therefore suggest that, for native cytochrome c, polymerization has an effect on the lability of the haem crevice, rendering the iron available for binding ligands, without, however, forming the structure of a truly open crevice. Iron 132-136 cytochrome c, somatic Equus caballus 38-50 29554518-9 2018 It has been demonstrated from the ultraviolet-visible spectral studies that the oxidation state of iron in cytochrome c does not change when the protein binds with the investigated surfactants. Iron 99-103 cytochrome c, somatic Equus caballus 107-119 34043488-0 2022 Heme-iron ligand (M80-Fe) in cytochrome c is destabilizing: combined in vitro and in silico approaches to monitor changes in structure, stability and dynamics of the protein on mutation. Iron 5-9 cytochrome c, somatic Equus caballus 29-41 34043488-4 2022 To understand this ligation better, Met80 of horse cyt c has been mutated to Gly that is unable to bind to the heme iron. Iron 116-120 cytochrome c, somatic Equus caballus 51-56 24969400-1 2014 Upon cardiolipin (CL) liposomes binding, horse heart cytochrome c (cytc) changes its tertiary structure disrupting the heme-Fe-Met80 distal bond, reduces drastically the midpoint potential, binds CO and NO with high affinity, displays peroxidase activity, and facilitates peroxynitrite isomerization. Iron 124-126 cytochrome c, somatic Equus caballus 53-65 28938074-6 2017 Similar to the previously reported results on cytochrome c, these fragment ions form near residues known to interact with iron atoms in solution. Iron 122-126 cytochrome c, somatic Equus caballus 46-58 22546244-5 2012 RR data revealed that entrapment of oxidized Cyt c into the Q(230) phase at 1 wt.% content results in near complete reduction of central iron ion of the heme group, while its low-spin state and six-ligand coordination configuration are preserved. Iron 137-141 cytochrome c, somatic Equus caballus 45-50 24662464-1 2014 The electrostatic surface of cytochrome c and its changes with the iron oxidation state are involved in the docking and undocking processes of this protein to its biological partners in the mitochondrial respiratory pathway. Iron 67-71 cytochrome c, somatic Equus caballus 29-41 23863217-3 2013 The VCS spectra revealed for the first time several low-frequency heme modes that are sensitive to cyt c unfolding: gamma(a) (~50 cm(-1)), gamma(b) (~80 cm(-1)), gamma(c) (~100 cm(-1)), and nu(s)(His-Fe-His) at 205 cm(-1). Iron 200-202 cytochrome c, somatic Equus caballus 99-104 23412550-1 2013 We have previously shown that methionine-heme iron coordination is perturbed in domain-swapped dimeric horse cytochrome c. Iron 46-50 cytochrome c, somatic Equus caballus 109-121 23412550-7 2013 The low nu (Fe-CN) frequency suggests weaker binding of the cyanide ion to dimeric cytochrome c compared with other heme proteins possessing a distal heme cavity. Iron 28-30 cytochrome c, somatic Equus caballus 99-111 23412550-9 2013 The results show that diatomic ligands may bind to the heme iron of dimeric cytochrome c and affect its stability. Iron 60-64 cytochrome c, somatic Equus caballus 76-88 21110943-1 2011 Upon interaction with bovine heart cardiolipin (CL), horse heart cytochrome c (cytc) changes its tertiary structure disrupting the heme-Fe-Met80 distal bond, reduces drastically the midpoint potential out of the range required for its physiological role, binds CO and NO with high affinity, and displays peroxidase activity. Iron 136-138 cytochrome c, somatic Equus caballus 65-77 22056558-1 2011 Carboxymethylation of equine heart cytochrome c (cytc) changes its tertiary structure by disrupting the heme-Fe-Met80 distal bond, such that carboxymethylated cytc (CM-cytc) displays myoglobin-like properties. Iron 109-111 cytochrome c, somatic Equus caballus 35-47 17804076-2 2007 Iron deposition into horse spleen ferritin (HoSF) occurs using ferricyanide ion, 2,6-dichlorophenol-indophenol, and several redox proteins: cytochrome c, stellacyanin, and ceruloplasmin. Iron 0-4 cytochrome c, somatic Equus caballus 140-152 17914866-10 2007 Whether His18-Fe-His33 coordination actually facilitates fast secondary structure formation or just slows folding less than His18-Fe-His26 coordination is probed by examining the double histidine mutant H26QH33N of horse heart cytochrome c. Iron 130-132 cytochrome c, somatic Equus caballus 227-239 16800612-7 2006 For ferrous Cyt c, the instantaneous photodissociation of the methionine side chain from the heme iron is the dominant event, and its rebinding proceeds in two phases, with time constants of approximately 5 and approximately 16 ps. Iron 98-102 cytochrome c, somatic Equus caballus 12-17 17142287-1 2007 We report on the structure and dynamics of the Fe ligand cluster of reduced horse heart cytochrome c in solution, in a dried polyvinyl alcohol (PVA) film, and in two trehalose matrices characterized by different contents of residual water. Iron 47-49 cytochrome c, somatic Equus caballus 88-100 16434742-0 2006 The redox couple of the cytochrome c cyanide complex: the contribution of heme iron ligation to the structural stability, chemical reactivity, and physiological behavior of horse cytochrome c. Iron 79-83 cytochrome c, somatic Equus caballus 24-36 16434742-0 2006 The redox couple of the cytochrome c cyanide complex: the contribution of heme iron ligation to the structural stability, chemical reactivity, and physiological behavior of horse cytochrome c. Iron 79-83 cytochrome c, somatic Equus caballus 179-191 15912551-6 2005 Comparison of the natures of the CD spectra in the 400 nm and 695 nm regions of the C357M mutant of cytochrome P450cam with those of horse cytochrome c suggested (R) chirality at the sulfur atom of the iron-bound methionine residue in the mutant. Iron 202-206 cytochrome c, somatic Equus caballus 139-151 15898816-6 2005 Acid titration of ferric cyt c in 9 M urea down to pH 2 is accompanied by protonation of one of the axial ligands, water binding to the heme iron (pK(a) = 5.2), and a sudden protein collapse (pH < 4). Iron 141-145 cytochrome c, somatic Equus caballus 25-30 14769043-2 2004 The two thioether bonds linking protein to heme in cyt c are present in 1, and the native axial ligand His-18 remains coordinated to iron. Iron 133-137 cytochrome c, somatic Equus caballus 51-56 15149817-3 2004 Folding of cyt c leads to a state having the heme iron coordinated to a histidine (His18) and a methionine (Met80) as axial ligands. Iron 50-54 cytochrome c, somatic Equus caballus 11-16 16849170-3 2005 His-26 and His-33 are both solvent exposed, and the results suggest that one of these histidine residues acts as a bridge in the electron transfer to and from the haem iron of cytochrome c. Iron 168-172 cytochrome c, somatic Equus caballus 176-188 12637007-5 2003 The rate constant for cyanide binding to the heme iron of cytochrome c of cytochrome c-polyglutamate complex also decreases by approximately 42.5% with n>or approximately equal 8. Iron 50-54 cytochrome c, somatic Equus caballus 58-70 12637007-5 2003 The rate constant for cyanide binding to the heme iron of cytochrome c of cytochrome c-polyglutamate complex also decreases by approximately 42.5% with n>or approximately equal 8. Iron 50-54 cytochrome c, somatic Equus caballus 74-86 12637007-8 2003 The results indicate that the polyglutamate (n>or approximately equal 8) is able to increase the stability of the methionine sulfur-heme iron bond of cytochrome c in spite of structural differences that weaken the overall stability of the cyt c at neutral and slightly alkaline pH. Iron 140-144 cytochrome c, somatic Equus caballus 153-165 11162121-2 2001 After photodissociating a ligand from the heme iron of unfolded horse cytochrome c, we use transient optical absorption spectroscopy to measure the time scale of the diffusive motions that bring the heme, located at His18, into contact with its native ligand, Met80. Iron 47-51 cytochrome c, somatic Equus caballus 70-82 8627283-2 1996 The results here reported: (i) allow the estimation, for the first time, of the ligand-independent free energy associated with the heme-iron sixth coordination bond in ferric and ferrous native cytochrome c, which turns out to be +8.4 kJ mol-1 and +14.6 kJ mol-1, at 25.0 degrees C, respectively, and (ii) suggest an interplay between redox, structural, ligand binding, and recognition properties of cytochrome c. Iron 136-140 cytochrome c, somatic Equus caballus 194-206 8841125-2 1996 Temperature dependent splitting also occurs for zinc cytochrome c, a derivative in which Fe has been replaced by Zn; at 10 K, the peaks in the Q0,0 band region occur at 17 106 and 16 996 cm-1. Iron 89-91 cytochrome c, somatic Equus caballus 53-65 8679672-5 1996 Comparison of the long-range NOEs of Im-cyt c relative to the crystal structure of native cytochrome c reveals apparent conformational changes of some side-chains especially those close to heme pocket within the N- and C-terminal helices resulting from the binding of imidazole to iron by displacing native Met-80 side-chain. Iron 281-285 cytochrome c, somatic Equus caballus 90-102 8627283-2 1996 The results here reported: (i) allow the estimation, for the first time, of the ligand-independent free energy associated with the heme-iron sixth coordination bond in ferric and ferrous native cytochrome c, which turns out to be +8.4 kJ mol-1 and +14.6 kJ mol-1, at 25.0 degrees C, respectively, and (ii) suggest an interplay between redox, structural, ligand binding, and recognition properties of cytochrome c. Iron 136-140 cytochrome c, somatic Equus caballus 400-412 8609608-5 1996 These results indicate that, at neutral pH, the ligation of His18 of the iron is important for the maintenance of the native structure whereas the Met80 ligation is not essential, and that porphyrin-cytochrome c assumes a molten globule-like state. Iron 73-77 cytochrome c, somatic Equus caballus 199-211 2166170-12 1990 The conservation of this structural feature and its close proximity to the heme iron atom strongly implicate this internal water molecule as having a functional role in the mechanism of action of cytochrome c. Iron 80-84 cytochrome c, somatic Equus caballus 196-208 8907170-8 1996 103, 4912-4921], the anti-Curie behavior observed for the heme methyl proton resonance in met-cyano cytochrome c is attributed to a rotational displacement of the heme about the iron-His bond relative to the protein moiety due to a temperature-dependent conformational alteration of the heme-protein linkage. Iron 178-182 cytochrome c, somatic Equus caballus 100-112 7578019-0 1995 The nature of the thermal equilibrium affecting the iron coordination of ferric cytochrome c. Iron 52-56 cytochrome c, somatic Equus caballus 80-92 7578019-1 1995 In cytochrome c, ligation of the heme iron by the methionine-80 sulfur plays a major role in determining the structure and the thermodynamic stability of the protein. Iron 38-42 cytochrome c, somatic Equus caballus 3-15 7757018-7 1995 The long range of paramagnetic shift effects (up to 20 A from the iron in the case of cytochrome c) provides global structural constraints, which, in conjunction with conventional NMR distance and dihedral angle constraints, will enhance the precision of NMR solution structure determination. Iron 66-70 cytochrome c, somatic Equus caballus 86-98 7880888-4 1994 The lipid-induced perturbations in the structure of cytochrome c involve: i) conformational changes in and around the heme crevice, converting the heme iron to a high-spin state: and ii) a destabilisation/loosening of the overall tertiary and secondary structure. Iron 152-156 cytochrome c, somatic Equus caballus 52-64 1327127-4 1992 From the increase of the rate of electron transfer with decreasing pH, one of the driving forces of the reaction was suggested to be the difference in the redox potentials between the type 1 copper in laccase and the central iron in cytochrome c. Iron 225-229 cytochrome c, somatic Equus caballus 233-245