PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15648974-0 2004 Kinetics of histidine dissociation from the heme Fe(III) in N-fragment (residues 1-56) of cytochrome c. Histidine 12-21 cytochrome c, somatic Equus caballus 90-102 15952772-6 2005 The implication of His 33 and Glu 104 in the binding site was deduced from the comparison of FTIR data recorded with horse heart and the variant tuna cytochrome c lacking these two amino acids. Histidine 19-22 cytochrome c, somatic Equus caballus 150-162 15952772-7 2005 A two-dimensional NMR analysis of the Zn(2+)-binding site in horse heart cytochrome c confirmed that His 33 and residues close to the C terminus are sensitive to Zn(2+) binding. Histidine 101-104 cytochrome c, somatic Equus caballus 73-85 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. Histidine 0-3 cytochrome c, somatic Equus caballus 176-188 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. Histidine 11-14 cytochrome c, somatic Equus caballus 176-188 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. Histidine 86-95 cytochrome c, somatic Equus caballus 176-188 16320010-0 2006 Insights into the role of the histidines in the structure and stability of cytochrome c. Histidine 30-40 cytochrome c, somatic Equus caballus 75-87 16320010-1 2006 In this paper we investigate the role played by each histidine in the amino acid sequence of yeast iso-1-cytochrome c (with the exception of H18, the residue axially coordinated to the heme iron) in determining the protein structure and stability. Histidine 53-62 cytochrome c, somatic Equus caballus 105-117 15912551-4 2005 The results indicated that the haem of C357M cytochrome P450cam is possibly axially coordinated to a methionine and a histidine, analogously to cytochrome c. Histidine 118-127 cytochrome c, somatic Equus caballus 144-156 10801361-0 2000 Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization. Histidine 47-50 cytochrome c, somatic Equus caballus 25-37 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. Histidine 72-81 cytochrome c, somatic Equus caballus 11-16 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. Histidine 103-106 cytochrome c, somatic Equus caballus 51-56 11802740-0 2002 Rapid intrachain binding of histidine-26 and histidine-33 to heme in unfolded ferrocytochrome C. Time-resolved spectroscopic studies of unfolded horse iron(II) cytochrome c have suggested that the imidazole side chains of His26 and His33 bind transiently to the heme iron on microsecond time scales, after photodissociation of a carbon monoxide ligand from the heme. Histidine 28-37 cytochrome c, somatic Equus caballus 160-172 11802740-3 2002 Transient binding of these histidine side chains to the heme therefore generates one of the fast kinetic phases observed in previous photochemically triggered spectroscopic studies of dynamics in unfolded iron(II) cytochrome c. Histidine 27-36 cytochrome c, somatic Equus caballus 214-226 10889031-9 2000 Further, it appears that a concerted cleavage of both His ligands takes place, suggesting indeed that the different axial ligands present in horse heart cytochrome c (Met/His) and in cytochrome c" from M. methylotrophus (His/His) affect the heme conformational changes. Histidine 54-57 cytochrome c, somatic Equus caballus 153-165 10889031-9 2000 Further, it appears that a concerted cleavage of both His ligands takes place, suggesting indeed that the different axial ligands present in horse heart cytochrome c (Met/His) and in cytochrome c" from M. methylotrophus (His/His) affect the heme conformational changes. Histidine 54-57 cytochrome c, somatic Equus caballus 183-195 12526492-1 2000 The reaction of [Ru(bpy)2L(H2O)]2+ (bpy = 2,2"-bipyridine, L = imidazole, water) with reduced horse heart cytochrome c results in coordination of [RuII(bpy)2L] at the His 33 and His 26 sites. Histidine 167-170 cytochrome c, somatic Equus caballus 106-118 12526492-1 2000 The reaction of [Ru(bpy)2L(H2O)]2+ (bpy = 2,2"-bipyridine, L = imidazole, water) with reduced horse heart cytochrome c results in coordination of [RuII(bpy)2L] at the His 33 and His 26 sites. Histidine 178-181 cytochrome c, somatic Equus caballus 106-118 10801361-2 2000 The variant contains a single misligating His residue at position 26, a location at which His residues are found in several cytochrome c homologues, including horse, tuna, and yeast iso-1. Histidine 42-45 cytochrome c, somatic Equus caballus 124-136 9376358-0 1997 Identification of the predominant non-native histidine ligand in unfolded cytochrome c. Histidine 45-54 cytochrome c, somatic Equus caballus 74-86 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. Histidine 183-186 cytochrome c, somatic Equus caballus 100-112 3030432-5 1987 The function of the heme c moieties in the catalytic cycle of the enzyme is discussed on the basis of their homology with the proximal histidine region of peroxidase (horseradish peroxidase and yeast cytochrome-c peroxidase) and cytochromes (horse cytochrome c and Pseudomonas cytochrome c-551). Histidine 135-144 cytochrome c, somatic Equus caballus 248-260 7867644-6 1995 A comparison between the orientation of the rhombic perturbations and the crystal structures of horse cytochrome c and P. aeruginosa cytochrome c551 reveals that the orientation of the histidine and methionine axial ligands dominates the rhombic perturbation and that the two ligands have approximately equal influence. Histidine 185-194 cytochrome c, somatic Equus caballus 102-114 8204626-2 1994 Under typical denaturing conditions (concentrated guanidine hydrochloride or urea near pH 7), one of the axial ligands, His 18, remains bound to the oxidized heme iron, but the second ligand, Met 80, is replaced by a non-native histidine ligand (His 26 or His 33 in horse cytochrome c). Histidine 120-123 cytochrome c, somatic Equus caballus 272-284 8204626-5 1994 Heme absorbance changes induced by rapid acidification of oxidized cytochrome c in 4.5 M guanidine hydrochloride from pH 7.8 to 4.6 or below exhibit two kinetic phases with rates of 110 and 25 s-1, attributed to the dissociation of non-native histidine ligands from the heme in the unfolded state. Histidine 243-252 cytochrome c, somatic Equus caballus 67-79 1655536-1 1991 Horse heart cytochrome c with either histidine or cysteine replacing the endogenous axial methionine ligand at position 80 has been characterized with magnetic circular dichroism (MCD) spectroscopy in the UV-visible region. Histidine 37-46 cytochrome c, somatic Equus caballus 12-24 2560194-1 1989 Semisynthesis has been employed to replace the axial methionine in horse heart cytochrome c with histidine. Histidine 97-106 cytochrome c, somatic Equus caballus 79-91 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. Histidine 141-150 cytochrome c, somatic Equus caballus 15-27 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. Histidine 141-150 cytochrome c, somatic Equus caballus 171-183 3016549-1 1986 Cytochrome c can be modified by [(NH3)5RuII/III-] specifically at the imidazole moiety of histidine 33, and we have recently discussed the thermodynamics and kinetics of electron transfer within this modified protein. Histidine 90-99 cytochrome c, somatic Equus caballus 0-12 3030432-5 1987 The function of the heme c moieties in the catalytic cycle of the enzyme is discussed on the basis of their homology with the proximal histidine region of peroxidase (horseradish peroxidase and yeast cytochrome-c peroxidase) and cytochromes (horse cytochrome c and Pseudomonas cytochrome c-551). Histidine 135-144 cytochrome c, somatic Equus caballus 277-289 6311172-5 1983 Spectroscopic measurements of pKa values for Lys-55 (horse and tuna cytochromes c) and His-33 and His-39 (C. krusei and S. cerevisiae cytochromes c) are in excellent agreement with expectations based on chemical-modification studies of horse cytochrome c. Histidine 87-90 cytochrome c, somatic Equus caballus 242-254 6329161-1 1984 Preparations of horse heart cytochrome c have been obtained immobilized on Sepharose derivatives via lysine epsilon-amino groups, carboxyl groups of aspartic and glutamic acid residues, methionine and histidine residues as well as imidazole groups additionally introduced by means of modification of free carboxyl groups by histamine. Histidine 201-210 cytochrome c, somatic Equus caballus 28-40 6091699-1 1983 Preparations of horse heart cytochrome c have been obtained immobilized on Sepharose derivatives via lysine epsilon-amino groups, carboxyl groups of aspartic and glutamic acid residues, methionine and histidine residues as well as imidazole groups additionally introduced by means of chemical modification of free carboxyl groups by histamine. Histidine 201-210 cytochrome c, somatic Equus caballus 28-40 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). Histidine 196-199 cytochrome c, somatic Equus caballus 99-104 27588329-9 2016 The complex structure of cyt c meant that this reactant was represented solely by the heme group including the chiral axial ligands L-His and L-Met. Histidine 132-137 cytochrome c, somatic Equus caballus 25-30 229899-4 1979 The spectra of guanidine hydrochloride unfolded cytochrome c-552 were dependent on the pH; the titration curve showed the presence of a cooperative single transition of pK = 4.7, with a one-proton dissociation, suggesting the ionization of a histidine residue. Histidine 242-251 cytochrome c, somatic Equus caballus 48-60 28277678-0 2017 Unravelling the Non-Native Low-Spin State of the Cytochrome c-Cardiolipin Complex: Evidence of the Formation of a His-Ligated Species Only. Histidine 114-117 cytochrome c, somatic Equus caballus 49-61 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). Histidine 203-206 cytochrome c, somatic Equus caballus 99-104