PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15804829-0 2004 Reversible hexa- to penta-coordination of the heme Fe atom modulates ligand binding properties of neuroglobin and cytoglobin. Iron 51-53 cytoglobin Homo sapiens 114-124 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. Iron 192-196 cytoglobin Homo sapiens 0-10 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. Iron 192-196 cytoglobin Homo sapiens 12-15 15804830-4 2004 Together with the observation that the distal ligand of the heme iron is the endogenous E7-histidine in both the ferric and ferrous form of neuroglobin and cytoglobin, the flexibility of the heme environment in neuroglobin will play a crucial role in the globins" ability to bind and stabilize exogenous ligands. Iron 65-69 cytoglobin Homo sapiens 156-166 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. Iron 147-151 cytoglobin Homo sapiens 58-68 15804829-7 2004 Reversible hexa- to penta-coordination of the heme Fe atom modulates ligand binding properties of Ngb and Cygb. Iron 51-53 cytoglobin Homo sapiens 106-110 7229753-1 1981 The purpose of this study was to determine the Hgb response to a therapeutic trial of iron in infants with anemia compared to those with low-normal hemoglobin values. Iron 86-90 cytoglobin Homo sapiens 47-50 21706744-4 2004 Ngb and Cygb display the classical three-on-three alpha-helical globin fold and are endowed with a hexa-coordinate heme Fe atom, in both their ferrous and ferric forms, having the heme distal HisE7 residue as the endogenous sixth ligand. Iron 120-122 cytoglobin Homo sapiens 8-12 21706744-5 2004 Reversible intramolecular hexa- to penta-coordination of the heme Fe atom modulates Ngb and Cygb ligand-binding properties. Iron 66-68 cytoglobin Homo sapiens 92-96 15095869-5 2004 In the absence of exogenous ligands (e.g. O2), the cytoglobin distal HisE7 residue is coordinated to the heme Fe atom, thus decreasing the ligand affinity. Iron 110-112 cytoglobin Homo sapiens 51-61 12718557-5 2003 On the basis of the nu(Fe-CO) and nu(C-O) values in the resonance Raman and infrared spectra of the ferrous-CO complexes of Cgb and its mutants, it was found that CO binds to the ferrous iron after the His81 imidazole is dissociated, and three conformers are present in the resultant CO coordination structure. Iron 187-191 cytoglobin Homo sapiens 124-127 7229753-7 1981 Because of the low cost and simplicity of a therapeutic trial, we favor including the low-normal Hgb group for a therapeutic trial of iron in order to avoid missing iron-responsive individuals among groups of infants with a similarly high prevalence of iron deficiency anemia. Iron 165-169 cytoglobin Homo sapiens 97-100 32461519-1 2020 The direct electron transfer between human cytoglobin (Cygb) and the electrode surface, which would allow manipulating the oxidation states of the heme iron in Cygb, was first observed by immobilizing Cygb on a nanoporous gold (NPG) electrode via a carboxy-terminated alkanethiol. Iron 152-156 cytoglobin Homo sapiens 43-53 32913582-4 2020 Compared with mesophilic orthologues, the cold-adapted cytoglobins favor binding of exogenous ligands to the hexa-coordinated bis-histidyl species, a trait related to their higher rate constant for distal-His/heme-Fe dissociation relative to human cytoglobin. Iron 214-216 cytoglobin Homo sapiens 55-65 33576020-8 2021 Replacement the iron centre of the heme group with cobalt nullified the effect of His-CYGB. Iron 16-20 cytoglobin Homo sapiens 82-90 32461519-1 2020 The direct electron transfer between human cytoglobin (Cygb) and the electrode surface, which would allow manipulating the oxidation states of the heme iron in Cygb, was first observed by immobilizing Cygb on a nanoporous gold (NPG) electrode via a carboxy-terminated alkanethiol. Iron 152-156 cytoglobin Homo sapiens 55-59 32461519-1 2020 The direct electron transfer between human cytoglobin (Cygb) and the electrode surface, which would allow manipulating the oxidation states of the heme iron in Cygb, was first observed by immobilizing Cygb on a nanoporous gold (NPG) electrode via a carboxy-terminated alkanethiol. Iron 152-156 cytoglobin Homo sapiens 160-164 32461519-1 2020 The direct electron transfer between human cytoglobin (Cygb) and the electrode surface, which would allow manipulating the oxidation states of the heme iron in Cygb, was first observed by immobilizing Cygb on a nanoporous gold (NPG) electrode via a carboxy-terminated alkanethiol. Iron 152-156 cytoglobin Homo sapiens 160-164 24780244-4 2014 The rate of Cygb(Fe(3+)) reduction increased ~6% per C when temperature varied from 35 C to 40 C. The yield and the rate of Cygb(Fe(3+)) reduction significantly increases with pH (2-3 times per pH unit), paralleling the formation of the Asc ion (A(2-)) and the increased stability of reduced state of heme iron at high pH values. Iron 307-311 cytoglobin Homo sapiens 12-16 26928591-4 2016 Searching for physiologically relevant lipid regulators of Cygb, here we report that anionic phospholipids, particularly phosphatidylinositolphosphates, affect structural organization of the protein and modulate its iron state and peroxidase activity both conjointly and/or independently of cysteine oxidation. Iron 216-220 cytoglobin Homo sapiens 59-63 28671819-2 2017 Unlike the evolutionarily related proteins hemoglobin and myoglobin, cytoglobin shows a six-coordinated heme binding, with the heme iron coordinated by two histidine side chains. Iron 132-136 cytoglobin Homo sapiens 69-79 26928591-2 2016 The iron coordination and spin state of the Cygb heme group are sensitive to oxidation of two cysteine residues (Cys38/Cys83) and/or the binding of free fatty acids. Iron 4-8 cytoglobin Homo sapiens 44-48 24780244-4 2014 The rate of Cygb(Fe(3+)) reduction increased ~6% per C when temperature varied from 35 C to 40 C. The yield and the rate of Cygb(Fe(3+)) reduction significantly increases with pH (2-3 times per pH unit), paralleling the formation of the Asc ion (A(2-)) and the increased stability of reduced state of heme iron at high pH values. Iron 307-311 cytoglobin Homo sapiens 125-129 23416443-8 2013 In fact, the heme reactivity of CYGB depends on the lipid, such as oleate, binding which stabilizes the penta-coordination geometry of the heme-Fe atom. Iron 144-146 cytoglobin Homo sapiens 32-36 23416443-9 2013 Lastly, the reactivity of NGB and CYGB is modulated by the redox state of the intramolecular CysCD7/CysD5 and CysB2/CysE9 residue pairs, respectively, affecting the heme-Fe atom coordination state. Iron 170-172 cytoglobin Homo sapiens 34-38 22097806-4 2011 The results showed that endogenous cytoglobin exerted significant protective effects on hydrogen peroxide or iron-overload induced LX-2 cell damage, confirming that upregulation of cytoglobin was the protective response of activated hepatic stellate cells to oxidative stress. Iron 109-113 cytoglobin Homo sapiens 35-45 22097806-7 2011 Intracellular over-expression of cytoglobin protein could exert significant protective effect on LX-2 cells treated with hydrogen peroxide or iron-overload. Iron 142-146 cytoglobin Homo sapiens 33-43 21254233-2 2011 Unlike myoglobin, Cgb displays a hexa-coordinated (bis-hystidyl) heme iron atom, having the heme distal His81(E7) residue as the endogenous sixth ligand. Iron 70-74 cytoglobin Homo sapiens 18-21