PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19820972-0 2010 Molecular dynamics simulation of a carboxy murine neuroglobin mutated on the proximal side: heme displacement and concomitant rearrangement in loop regions. Heme 92-96 neuroglobin Mus musculus 50-61 29108649-5 2017 We propose that these cavities could store oxygen and allow its relay in the heme proximity, which could correspond to NO location in the nitrite-reductase function of Ngb. Heme 77-81 neuroglobin Mus musculus 168-171 29108649-7 2017 A new gas binding site on the proximal side of the heme has also been characterized, using xenon pressure on a Ngb mutant (V140W) that binds CO with a similar rate and affinity to the wild-type, despite a reshaping of the internal cavity. Heme 51-55 neuroglobin Mus musculus 111-114 28500341-3 2017 In murine Ngb, reversible coordination is achieved by repositioning the heme more deeply into a large internal cavity, the "heme sliding mechanism". Heme 72-76 neuroglobin Mus musculus 10-13 28500341-3 2017 In murine Ngb, reversible coordination is achieved by repositioning the heme more deeply into a large internal cavity, the "heme sliding mechanism". Heme 124-128 neuroglobin Mus musculus 10-13 29108649-3 2017 In murine Ngb, a large internal cavity is involved in the heme sliding mechanism to achieve binding of gaseous ligands through coordination to the heme iron. Heme 58-62 neuroglobin Mus musculus 10-13 29108649-3 2017 In murine Ngb, a large internal cavity is involved in the heme sliding mechanism to achieve binding of gaseous ligands through coordination to the heme iron. Heme 147-151 neuroglobin Mus musculus 10-13 21058400-0 2011 Distal mutation modulates the heme sliding in mouse neuroglobin investigated by molecular dynamics simulation. Heme 30-34 neuroglobin Mus musculus 52-63 21058400-2 2011 Ngb can reversibly bind small ligands such as O2 and CO to the heme iron by replacing the distal histidine which is bound to the iron as the endogenous ligand. Heme 63-67 neuroglobin Mus musculus 0-3 21058400-7 2011 The work elucidates that the key residues K67 at E10 and H64 at E7 are significant in modulating the heme sliding and hence the structural and physiological function of Ngb. Heme 101-105 neuroglobin Mus musculus 169-172 19820972-3 2010 Structurally, neuroglobin enjoys unique features, such as bis-histidyl coordination to heme iron in the absence of exogenous ligand, heme orientational heterogeneity, and a heme sliding mechanism accompanying ligand binding. Heme 87-91 neuroglobin Mus musculus 14-25 19820972-3 2010 Structurally, neuroglobin enjoys unique features, such as bis-histidyl coordination to heme iron in the absence of exogenous ligand, heme orientational heterogeneity, and a heme sliding mechanism accompanying ligand binding. Heme 133-137 neuroglobin Mus musculus 14-25 19820972-3 2010 Structurally, neuroglobin enjoys unique features, such as bis-histidyl coordination to heme iron in the absence of exogenous ligand, heme orientational heterogeneity, and a heme sliding mechanism accompanying ligand binding. Heme 133-137 neuroglobin Mus musculus 14-25 19850349-8 2009 Compared with mouse neuroglobin, the obtained average ligand orientation of human neuroglobin reflects the changeability of heme environment for the Ngb family. Heme 124-128 neuroglobin Mus musculus 20-31 15162488-1 2004 Neuroglobin, a recently discovered globin predominantly expressed in neuronal tissue of vertebrates, binds small, gaseous ligands at the sixth coordination position of the heme iron. Heme 172-176 neuroglobin Mus musculus 0-11 17468165-6 2007 Recent crystallographic data on carboxy Ngb show that binding of an exogenous ligand is associated to structural changes involving heme sliding and a topological reorganization of the internal cavities; in particular, the huge internal tunnel that connects the bulk with the active site, peculiar to Ngb, is heavily reorganized. Heme 131-135 neuroglobin Mus musculus 40-43 16586113-0 2006 The heme environment of mouse neuroglobin: histidine imidazole plane orientations obtained from solution NMR and EPR spectroscopy as compared with X-ray crystallography. Heme 4-8 neuroglobin Mus musculus 30-41 16596390-0 2006 Analyzing heme proteins using EPR techniques: the heme-pocket structure of ferric mouse neuroglobin. Heme 10-14 neuroglobin Mus musculus 88-99 16596390-4 2006 In combination with the hyperfine matrices of the imidazole protons, the 14N EPR parameters reveal structural information on the heme pocket of mNgb that is in agreement with previous X-ray diffraction data on neuroglobins. Heme 129-133 neuroglobin Mus musculus 144-148 15548613-0 2004 The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for control of ligand affinity. Heme 52-56 neuroglobin Mus musculus 30-41 15548613-3 2004 Unlike in Mb, in Ngb the sixth coordination position of the heme iron is occupied by the distal histidine, in the absence of an exogenous ligand. Heme 60-64 neuroglobin Mus musculus 17-20 15548613-9 2004 The heme relocation is accompanied by a significant decrease of structural disorder, especially of the EF loop, which may be the signal whereby Ngb communicates hypoxic conditions. Heme 4-8 neuroglobin Mus musculus 144-147 15548613-10 2004 This unexpected structural change unveils a heme-sliding mechanism of affinity control that may be of significance to understanding Ngb"s role in the pathophysiology of the brain. Heme 44-48 neuroglobin Mus musculus 132-135 15016813-1 2004 We have examined the effects of active site residues on ligand binding to the heme iron of mouse neuroglobin using steady-state and time-resolved visible spectroscopy. Heme 78-82 neuroglobin Mus musculus 97-108 32034988-0 2020 Lack of orientation selectivity of the heme insertion in murine neuroglobin revealed by resonance Raman spectroscopy. Heme 39-43 neuroglobin Mus musculus 64-75 11473111-0 2001 The heme environment of mouse neuroglobin. Heme 4-8 neuroglobin Mus musculus 30-41 11473111-3 2001 To characterize the structure/function relationships of this new heme protein, we have used resonance Raman spectroscopy to determine the structure of the heme environment in Ngb from mice. Heme 65-69 neuroglobin Mus musculus 175-178 11473111-3 2001 To characterize the structure/function relationships of this new heme protein, we have used resonance Raman spectroscopy to determine the structure of the heme environment in Ngb from mice. Heme 155-159 neuroglobin Mus musculus 175-178 11473111-8 2001 These structural properties of the heme pocket of Ngb are discussed with respect to its proposed in vivo oxygen delivery function. Heme 35-39 neuroglobin Mus musculus 50-53 34943874-3 2021 Therefore, the heme-based reactivity of Ngb is modulated by the dissociation of the distal HisE7-heme-Fe bond, which reflects in turn the redox state of the cell. Heme 15-19 neuroglobin Mus musculus 40-43 34943874-3 2021 Therefore, the heme-based reactivity of Ngb is modulated by the dissociation of the distal HisE7-heme-Fe bond, which reflects in turn the redox state of the cell. Heme 97-101 neuroglobin Mus musculus 40-43 12486081-3 2002 Although the functional role of this novel member of the globin family remains unclear, neuroglobin contains a heme-binding domain and may participate in diverse processes such as oxygen transport, oxygen storage, nitric oxide detoxification, or modulation of terminal oxidase activity. Heme 111-115 neuroglobin Mus musculus 88-99 32034988-5 2020 The resonance Raman data, together with the corresponding crystal structures, indicate the presence of two neuroglobin conformers with a reversed (A conformer) or a canonical (B conformer) heme insertion orientation. Heme 189-193 neuroglobin Mus musculus 107-118 30926858-4 2019 We observed the effects of individual and combined mutations of the CD loop and Phe106 that conferred to Ngb higher CO binding velocities, which we correlate with the following structural observations: the mutant F106A shows, upon CO binding, a reduced heme sliding hindrance, with the heme present in a peculiar double conformation, whereas in the CD loop mutant "Gly-loop", the original network of interactions between the loop and the heme was abolished, enhancing binding via facilitated gating out of the distal His64. Heme 253-257 neuroglobin Mus musculus 105-108 30926858-4 2019 We observed the effects of individual and combined mutations of the CD loop and Phe106 that conferred to Ngb higher CO binding velocities, which we correlate with the following structural observations: the mutant F106A shows, upon CO binding, a reduced heme sliding hindrance, with the heme present in a peculiar double conformation, whereas in the CD loop mutant "Gly-loop", the original network of interactions between the loop and the heme was abolished, enhancing binding via facilitated gating out of the distal His64. Heme 286-290 neuroglobin Mus musculus 105-108 30926858-4 2019 We observed the effects of individual and combined mutations of the CD loop and Phe106 that conferred to Ngb higher CO binding velocities, which we correlate with the following structural observations: the mutant F106A shows, upon CO binding, a reduced heme sliding hindrance, with the heme present in a peculiar double conformation, whereas in the CD loop mutant "Gly-loop", the original network of interactions between the loop and the heme was abolished, enhancing binding via facilitated gating out of the distal His64. Heme 286-290 neuroglobin Mus musculus 105-108