PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20421510-1 2010 A structural and functional model of bacterial nitric oxide reductase (NOR) has been designed by introducing two glutamates (Glu) and three histidines (His) in sperm whale myoglobin. Histidine 152-155 myoglobin Physeter catodon 172-181 20481504-0 2010 Straight-chain alkyl isocyanides open the distal histidine gate in crystal structures of myoglobin . Histidine 49-58 myoglobin Physeter catodon 89-98 20088488-0 2010 The main role of inner histidines in the molecular mechanism of myoglobin oxidation catalyzed by copper compounds. Histidine 23-33 myoglobin Physeter catodon 64-73 10681426-1 2000 We determined the structure of the photolytic intermediate of a sperm whale myoglobin (Mb) mutant called Mb-YQR [Leu-(B10)-->Tyr; His(E7)-->Gln; Thr(E10)-->Arg] to 1.4-A resolution by ultra-low temperature (20 K) x-ray diffraction. Histidine 133-136 myoglobin Physeter catodon 76-85 17701542-0 2007 Histidine and not tyrosine is required for the peroxide-induced formation of haem to protein cross-linked myoglobin. Histidine 0-9 myoglobin Physeter catodon 106-115 17701542-9 2007 Moreover, addition of a distal histidine to myoglobin from Aplysia limacina, that naturally lacks this histidine, restores the haem protein"s capacity to generate haem to protein cross-links. Histidine 31-40 myoglobin Physeter catodon 44-53 17701542-9 2007 Moreover, addition of a distal histidine to myoglobin from Aplysia limacina, that naturally lacks this histidine, restores the haem protein"s capacity to generate haem to protein cross-links. Histidine 103-112 myoglobin Physeter catodon 44-53 15849248-4 2005 In wild-type deoxy myoglobin, the passage between the distal pocket and the solvent is strictly correlated to the presence/absence of a water molecule that simultaneously interacts with the distal histidine side chain and the heme iron; conversely, in the photodissociated myoglobin, the connection with the bulk solvent is always open when CO is in the vicinity of the A pyrrole ring. Histidine 197-206 myoglobin Physeter catodon 19-28 11087949-4 2000 As a result, the rate of autoxidation of Tetrahymena oxymyoglobin (MbO(2)) was found to be almost comparable to that of sperm whale MbO(2) over a wide range of pH 4-12 in 0.1 M buffer at 25 degrees C. Moreover, both pH profiles exhibited the remarkable proton-assisted process, which can be performed in sperm whale myoglobin by the distal (E7) histidine as its catalytic residue. Histidine 345-354 myoglobin Physeter catodon 56-65 11087949-5 2000 These kinetic observations are also in full accord with spectral examinations for the presence of a distal histidine in ciliated protozoa myoglobin. Histidine 107-116 myoglobin Physeter catodon 138-147 10813812-2 2000 The trans-substituted histidine to glycine mutant of sperm whale myoglobin (H93G Mb) is used to study energetics of proximal hydrogen bonding, proximal ligand-heme interactions, and coupling to distal ligand binding. Histidine 22-31 myoglobin Physeter catodon 65-74 14719919-0 2004 Hybridization of modified-heme reconstitution and distal histidine mutation to functionalize sperm whale myoglobin. Histidine 57-66 myoglobin Physeter catodon 105-114 12582819-1 2003 The sperm whale myoglobin mutant H64V, where the distal histidine is mutated to valine, is known to be five coordinated in the ferric state at room temperature and physiological pH. Histidine 56-65 myoglobin Physeter catodon 16-25 2037047-4 1991 Alternative mechanisms of ligand stabilization may therefore be operative in Mb"s lacking the distal histidine. Histidine 101-110 myoglobin Physeter catodon 77-79 9915818-0 1999 Effects of the location of distal histidine in the reaction of myoglobin with hydrogen peroxide. Histidine 34-43 myoglobin Physeter catodon 63-72 9407045-0 1997 On the formation and reactivity of compound I of the His-64 myoglobin mutants. Histidine 53-56 myoglobin Physeter catodon 60-69 9407045-5 1997 The results unambiguously indicate that His-64 plays a key role in destabilizing wild type Mb-I. Histidine 40-43 myoglobin Physeter catodon 91-95 9414234-0 1997 The tautomeric state of histidines in myoglobin. Histidine 24-34 myoglobin Physeter catodon 38-47 9414234-3 1997 Of the nine histidines not interacting with the heme in sperm whale myoglobin, it was found that seven (His-12, His-48, His-81, His-82, His-113, His-116, and His-119) are predominantly in the N epsilon2H form with varying degrees of contribution from the Ndelta1 H form. Histidine 12-22 myoglobin Physeter catodon 68-77 9414234-10 1997 With the experimentally determined tautomeric state composition in solution, it will be possible to broaden the scope of other studies focused on the electrostatic contribution of histidines to the thermodynamic properties of myoglobin. Histidine 180-190 myoglobin Physeter catodon 226-235 7479707-0 1995 Phe-46(CD4) orients the distal histidine for hydrogen bonding to bound ligands in sperm whale myoglobin. Histidine 31-40 myoglobin Physeter catodon 94-103 7479707-10 1995 In wild-type myoglobin, the van der Waals contact between C zeta of Phe-46 and C beta of His-64 appears to restrict rotation of the imidazole side chain. Histidine 89-92 myoglobin Physeter catodon 13-22 8230194-0 1993 High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin. Histidine 45-54 myoglobin Physeter catodon 78-87 8230194-1 1993 The highly conserved distal histidine residue (His64) of sperm whale myoglobin modulates the affinity of ligands. Histidine 28-37 myoglobin Physeter catodon 69-78 8419357-0 1993 The roles of His-64, Tyr-103, Tyr-146, and Tyr-151 in the epoxidation of styrene and beta-methylstyrene by recombinant sperm whale myoglobin. Histidine 13-16 myoglobin Physeter catodon 131-140 8642596-1 1996 The distal histidine residue, His64(E7), and the proximal histidine residue, His93(F8), in myoglobin (Mb) are important for the function of the protein. Histidine 11-20 myoglobin Physeter catodon 91-100 8642596-1 1996 The distal histidine residue, His64(E7), and the proximal histidine residue, His93(F8), in myoglobin (Mb) are important for the function of the protein. Histidine 58-67 myoglobin Physeter catodon 91-100 7837273-5 1995 In Ala68 deoxymyoglobin, as in the wild-type protein, a water molecule hydrogen-bonded to the N epsilon atom of the distal histidine restricts ligand binding and appears to be more important in regulating the function of myoglobin than direct steric interactions between the ligand and the C gamma atoms of the native valine side-chain. Histidine 123-132 myoglobin Physeter catodon 14-23 8204590-0 1994 Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His-93-->Gly. Histidine 94-97 myoglobin Physeter catodon 50-59 8504086-0 1993 Solution structure determination of the heme cavity in the E7 His-->Val cyano-met myoglobin point mutant based on the 1H NMR detected dipolar field of the iron: evidence for contraction of the heme pocket. Histidine 62-65 myoglobin Physeter catodon 85-94 1518828-0 1992 Site-directed mutagenesis of histidine residues involved in Cu(II) binding and reduction by sperm whale myoglobin. Histidine 29-38 myoglobin Physeter catodon 104-113 1518828-1 1992 Sperm whale myoglobin (Mb) reduces Cu(II) through a site-specific mechanism involving complexation by one or more surface histidine residues. Histidine 122-131 myoglobin Physeter catodon 12-21 3186740-0 1988 Ligand binding to synthetic mutant myoglobin (His-E7----Gly): role of the distal histidine. Histidine 81-90 myoglobin Physeter catodon 35-44 2545246-0 1989 Resonance Raman evidence that distal histidine protonation removes the steric hindrance to upright binding of carbon monoxide by myoglobin. Histidine 37-46 myoglobin Physeter catodon 129-138 2380176-10 1990 Analysis of the results suggests much easier movement of ligand between the heme pocket and the exterior than in sperm whale myoglobin (His(E7]. Histidine 136-139 myoglobin Physeter catodon 125-134 2752047-2 1989 The proton NMR spectrum of the deoxy myoglobin exhibits an NH signal from the proximal histidine at 78.6 ppm, indicating heme incorporation into the heme pocket to form the Fe-N(His-F8) bond. Histidine 87-96 myoglobin Physeter catodon 37-46 2752047-2 1989 The proton NMR spectrum of the deoxy myoglobin exhibits an NH signal from the proximal histidine at 78.6 ppm, indicating heme incorporation into the heme pocket to form the Fe-N(His-F8) bond. Histidine 178-181 myoglobin Physeter catodon 37-46 3186740-0 1988 Ligand binding to synthetic mutant myoglobin (His-E7----Gly): role of the distal histidine. Histidine 46-49 myoglobin Physeter catodon 35-44 3186740-2 1988 The synthesis and high-level expression of a sperm-whale myoglobin gene in Escherichia coli permits the efficient substitution of the distal histidine through site-directed mutagenesis. Histidine 141-150 myoglobin Physeter catodon 57-66 6746625-5 1984 The essentially identical dipolar shifts and dipolar relaxation times for the distal Gln-E7 side chain NH and the distal His-E7 ring NH in sperm whale myoglobin indicate that those labile protons occupy the same geometrical position relative to the iron and heme plane. Histidine 121-124 myoglobin Physeter catodon 151-160 6498167-3 1984 In diamagnetic derivatives [(carbon monoxy)myoglobin (COMb) and oxymyoglobin (oxyMb)], the titration behavior of His-36 H-2 and H-4 resonances is normalized (pK approximately 6.8). Histidine 113-116 myoglobin Physeter catodon 43-52 6498167-4 1984 The very slight alkaline Bohr effect in sperm whale myoglobin (Mb) is interpreted in terms of the pK change of His-36 from deoxyMb to oxyMb and compensating pK changes in the opposite direction of other unspecified groups. Histidine 111-114 myoglobin Physeter catodon 52-61 3607070-1 1987 We reported previously that the distal(E7) histidine is replaced by glutamine in myoglobin from the shark, Galeorhinus japonicus. Histidine 43-52 myoglobin Physeter catodon 81-90 3607070-3 1987 The myoglobin is composed of 148 residues, is acetylated at the N-terminus, and contains the distal(E7) histidine at position 59. Histidine 104-113 myoglobin Physeter catodon 4-13 3607070-8 1987 On the other hand, the pH dependence of G. japonicus myoglobin, which has the distal glutamine in the place of histidine, was quite different from those of sperm-whale and H. japonicus myoglobins. Histidine 111-120 myoglobin Physeter catodon 53-62 4008494-0 1985 Resonance Raman studies of CO and O2 binding to elephant myoglobin (distal His(E7)----Gln). Histidine 75-78 myoglobin Physeter catodon 57-66 4008494-1 1985 Carbon monoxide and dioxygen were employed as resonance Raman-visible ligands for probing the nature of the heme-binding site in elephant myoglobin, which has glutamine in the distal position (E7) instead of the usual histidine. Histidine 218-227 myoglobin Physeter catodon 138-147 28274434-0 2017 Effect of 4-hydroxy-2-nonenal on myoglobin-mediated lipid oxidation when varying histidine content and hemin affinity. Histidine 81-90 myoglobin Physeter catodon 33-42 7236849-6 1981 The observation that filling the hydrophobic vacancy on the proximal side of the heme near the proximal histidine in Met-cyano myoglobin wih cyclopropane increases the proton lability argues against the role for this hole in facilitating the flexibility of the F helix in the native protein. Histidine 104-113 myoglobin Physeter catodon 127-136 25451928-0 2015 Significantly enhanced heme retention ability of myoglobin engineered to mimic the third covalent linkage by nonaxial histidine to heme (vinyl) in synechocystis hemoglobin. Histidine 118-127 myoglobin Physeter catodon 49-58