PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15036292-1 2004 Neuroglobin displays a hexacoordination His-Fe-His in the absence of external ligands such as oxygen. Histidine 40-44 neuroglobin Homo sapiens 0-11 15036292-7 2004 Mutation of specific cysteines, or reduction to break the S-S bond, led to a large decrease in the observed oxygen affinity of human neuroglobin, mainly due to a decrease in the histidine dissociation rate. Histidine 178-187 neuroglobin Homo sapiens 133-144 14530264-1 2003 Neuroglobin and cytoglobin reversibly bind oxygen in competition with the distal histidine, and the observed oxygen affinity therefore depends on the properties of both ligands. Histidine 81-90 neuroglobin Homo sapiens 0-11 29566507-2 2018 Recently, a potential treatment for CO poisoning was introduced, based on binding of CO by neuroglobin (Ngb) with a mutated distal histidine (H64Q). Histidine 131-140 neuroglobin Homo sapiens 91-102 32492011-7 2020 Nevertheless, Ngb contains both proximal and distal conserved heme-biding histidines. Histidine 74-84 neuroglobin Homo sapiens 14-17 29566507-2 2018 Recently, a potential treatment for CO poisoning was introduced, based on binding of CO by neuroglobin (Ngb) with a mutated distal histidine (H64Q). Histidine 131-140 neuroglobin Homo sapiens 104-107 29078150-2 2018 In the human protein (hNgb), Cys46 and Cys55 form an intramolecular disulfide bond under oxidizing conditions, whose cleavage induces a helix-to-strand rearrangement of the CD loop that strengthens the bond between the heme iron and the distal histidine. Histidine 244-253 neuroglobin Homo sapiens 22-26 28246171-6 2017 To resolve this discrepancy, we explored the role of the distal histidine residue in muting the reactivity of human neuroglobin toward H2S. Histidine 64-73 neuroglobin Homo sapiens 116-127 27825818-3 2016 Therefore, ligand binding to the Ngb metal center is limited from the dissociation of the distal His(E7)64-Fe bond. Histidine 97-100 neuroglobin Homo sapiens 33-36 27928027-3 2016 Ngb is a six-coordinate hemoprotein, with the heme iron coordinated by two histidine residues. Histidine 75-84 neuroglobin Homo sapiens 0-3 25554946-14 2015 Conversely, in Ngb, the reduction mechanism does not rely on the delivery of a proton from the histidine side chain, as His64 mutants show the fastest reduction rates. Histidine 95-104 neuroglobin Homo sapiens 15-18 27661977-7 2016 Hexacoordinate hemoglobins such as neuroglobin are limited by tighter histidine coordination that blocks hydroxylamine binding, and pentacoordinate hemoglobins have intrinsically lower hydroxylamine affinities. Histidine 70-79 neuroglobin Homo sapiens 35-46 23249163-1 2013 We report the functional analysis of an artificial hexacoordinate oxygen transport protein, HP7, which operates via a mechanism similar to that of human neuroglobin and cytoglobin: the destabilization of one of two heme-ligating histidine residues. Histidine 229-238 neuroglobin Homo sapiens 153-164 21965683-2 2011 Most of the neuroglobin is present in a hexacoordinate state with proximal and distal histidines in the heme pocket directly bound to the heme iron. Histidine 86-96 neuroglobin Homo sapiens 12-23 23135388-0 2013 Heme orientation modulates histidine dissociation and ligand binding kinetics in the hexacoordinated human neuroglobin. Histidine 27-36 neuroglobin Homo sapiens 107-118 21296891-5 2011 Replacement of the distal histidine by leucine or glutamine leads to a stable five-coordinated geometry; these neuroglobin mutants reduce nitrite to NO ~2000 times faster than the wild type, whereas mutation of either Cys-55 or Cys-46 to alanine stabilizes the six-coordinate structure and slows the reaction. Histidine 26-35 neuroglobin Homo sapiens 111-122 21332165-2 2011 With respect to other globins similar to myoglobin, Ngb displays some peculiarities as the topological reorganization of the internal cavities coupled to the sliding of the heme, or the binding of the endogenous distal histidine to the heme in the absence of an exogenous ligand. Histidine 219-228 neuroglobin Homo sapiens 52-55 19419181-1 2009 We report the selective, controlled binding of a model redox probe, 1,1"-bis(N-imidazolylmethyl)ferrocene (Fc-Im2), and a small redox hemoprotein, histidine-tagged recombinant human neuroglobin (hNb), at the surface of metal electrodes (gold and SER-active silver) modified by a self-assembled monolayer (SAM) of a nitrilotriacetic (NTA)-terminated thiol. Histidine 147-156 neuroglobin Homo sapiens 182-193 20050619-0 2010 Nonadiabatic histidine dissociation of hexacoordinate heme in neuroglobin protein. Histidine 13-22 neuroglobin Homo sapiens 62-73 20050619-1 2010 In the present work, density functional theory and canonical nonadiabatic Monte Carlo transition state theory have been used to investigate the histidine dissociation process from hexacoordinate heme in Ngb protein. Histidine 144-153 neuroglobin Homo sapiens 203-206 16684569-1 2006 The normally hexa coordinate ferrous form of neuroglobin binds CO by replacement of the heme-linked distal histidine residue. Histidine 107-116 neuroglobin Homo sapiens 45-56 18641072-2 2008 In the absence of exogenous ligands, the ferric and the ferrous forms of Ngb are both hexacoordinated to the distal and proximal histidines. Histidine 129-139 neuroglobin Homo sapiens 73-76 18767815-3 2008 In Ngb, the imidazole of a histidine residue (His-64) in the distal position, above the heme plane, provides the sixth coordination bond. Histidine 27-36 neuroglobin Homo sapiens 3-6 18767815-3 2008 In Ngb, the imidazole of a histidine residue (His-64) in the distal position, above the heme plane, provides the sixth coordination bond. Histidine 46-49 neuroglobin Homo sapiens 3-6 18767815-11 2008 Together, the data support the argument that wild-type Ngb is protected from attack by H 2O 2 by the coordinated distal His. Histidine 120-123 neuroglobin Homo sapiens 55-58 17916624-4 2007 The CO adduct of Ngb displays two CO absorption bands in the IR spectrum, referred to as N(3) (distal histidine in the pocket) and N(0) (distal histidine swung out of the pocket), which have absorption spectra that are almost identical with the Mb mutants L29F and H64V, respectively. Histidine 102-111 neuroglobin Homo sapiens 17-20 17916624-4 2007 The CO adduct of Ngb displays two CO absorption bands in the IR spectrum, referred to as N(3) (distal histidine in the pocket) and N(0) (distal histidine swung out of the pocket), which have absorption spectra that are almost identical with the Mb mutants L29F and H64V, respectively. Histidine 144-153 neuroglobin Homo sapiens 17-20 16201751-0 2005 Structural characterization of the proximal and distal histidine environment of cytoglobin and neuroglobin. Histidine 55-64 neuroglobin Homo sapiens 95-106 16201751-1 2005 Cytoglobin (Cgb) and neuroglobin (Ngb) are the first examples of hexacoordinated globins from humans and other vertebrates in which a histidine (His) residue at the sixth position of the heme iron is an endogenous ligand in both the ferric and ferrous forms. Histidine 134-143 neuroglobin Homo sapiens 21-32 16201751-1 2005 Cytoglobin (Cgb) and neuroglobin (Ngb) are the first examples of hexacoordinated globins from humans and other vertebrates in which a histidine (His) residue at the sixth position of the heme iron is an endogenous ligand in both the ferric and ferrous forms. Histidine 134-143 neuroglobin Homo sapiens 34-37 16201751-1 2005 Cytoglobin (Cgb) and neuroglobin (Ngb) are the first examples of hexacoordinated globins from humans and other vertebrates in which a histidine (His) residue at the sixth position of the heme iron is an endogenous ligand in both the ferric and ferrous forms. Histidine 145-148 neuroglobin Homo sapiens 21-32 16201751-1 2005 Cytoglobin (Cgb) and neuroglobin (Ngb) are the first examples of hexacoordinated globins from humans and other vertebrates in which a histidine (His) residue at the sixth position of the heme iron is an endogenous ligand in both the ferric and ferrous forms. Histidine 145-148 neuroglobin Homo sapiens 34-37 15819897-3 2005 Moreover, flash photolysis experiments at high temperatures reveal that Ngb remains functional at 90 degrees C. Human Ngb may have a disulfide bond in the CD loop region; reduction of the disulfide bond increases the affinity of the iron atom for the distal (E7) histidine, and leads to a 3 degrees C increase in the T(m) for ferrous Ngb. Histidine 263-272 neuroglobin Homo sapiens 72-75 15819897-3 2005 Moreover, flash photolysis experiments at high temperatures reveal that Ngb remains functional at 90 degrees C. Human Ngb may have a disulfide bond in the CD loop region; reduction of the disulfide bond increases the affinity of the iron atom for the distal (E7) histidine, and leads to a 3 degrees C increase in the T(m) for ferrous Ngb. Histidine 263-272 neuroglobin Homo sapiens 118-121 15819897-3 2005 Moreover, flash photolysis experiments at high temperatures reveal that Ngb remains functional at 90 degrees C. Human Ngb may have a disulfide bond in the CD loop region; reduction of the disulfide bond increases the affinity of the iron atom for the distal (E7) histidine, and leads to a 3 degrees C increase in the T(m) for ferrous Ngb. Histidine 263-272 neuroglobin Homo sapiens 118-121 15819897-7 2005 Only globins with a high affinity of the distal histidine show the very high thermal stability, indicating that stable hexa-coordination is necessary for the enhanced thermal stability; the CD loop which contains the cysteines appears as a critical region in the neuroglobin thermal stability, because it may influence the affinity of the distal histidine. Histidine 48-57 neuroglobin Homo sapiens 263-274 15804833-4 2004 As with some plant and bacterial globins, neuroglobin and cytoglobin hemes are hexacoordinate in the absence of external ligands, in that the heme iron atom coordinates both a proximal and a distal His residue. Histidine 198-201 neuroglobin Homo sapiens 42-53 15488767-1 2004 Both the ferrous and ferric forms of wild-type neuroglobin are found to be hexacoordinated with axial ligation of the F8-His and E7-His. Histidine 121-124 neuroglobin Homo sapiens 47-58 15488767-1 2004 Both the ferrous and ferric forms of wild-type neuroglobin are found to be hexacoordinated with axial ligation of the F8-His and E7-His. Histidine 132-135 neuroglobin Homo sapiens 47-58 15299006-2 2004 Two new globin proteins have recently been discovered in vertebrates, neuroglobin in neurons and cytoglobin in all tissues, both showing heme hexacoordination by the distal His(E7) in the absence of gaseous ligands. Histidine 173-176 neuroglobin Homo sapiens 70-81 15020597-1 2004 Neuroglobin, recently discovered in the brain and in the retina of vertebrates, belongs to the class of hexacoordinate globins, in which the distal histidine coordinates the iron center in both the Fe(II) and Fe(III) forms. Histidine 148-157 neuroglobin Homo sapiens 0-11