Ligand binding and hexacoordination in synechocystis hemoglobin.
about
Covalent heme attachment inSynechocystishemoglobin is required to prevent ferrous heme dissociationThe crystal structure of Synechocystis hemoglobin with a covalent heme linkageA hydrogen-bonding network formed by the B10-E7-E11 residues of a truncated hemoglobin from Tetrahymena pyriformis is critical for stability of bound oxygen and nitric oxide detoxificationA ubiquitously expressed human hexacoordinate hemoglobinNO dioxygenase activity in hemoglobins is ubiquitous in vitro, but limited by reduction in vivoStructure and reactivity of hexacoordinate hemoglobinsSignificantly enhanced heme retention ability of myoglobin engineered to mimic the third covalent linkage by nonaxial histidine to heme (vinyl) in synechocystis hemoglobinTruncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants.Distal histidine stabilizes bound O2 and acts as a gate for ligand entry in both subunits of adult human hemoglobin.Ligand binding and protein dynamics in neuroglobinDirect measurement of equilibrium constants for high-affinity hemoglobins.Peroxidase activity and involvement in the oxidative stress response of roseobacter denitrificans truncated hemoglobin.Chemical reactivity of Synechococcus sp. PCC 7002 and Synechocystis sp. PCC 6803 hemoglobins: covalent heme attachment and bishistidine coordination.Proximal influences in two-on-two globins: effect of the Ala69Ser replacement on Synechocystis sp. PCC 6803 hemoglobinNitrite reduction by molybdoenzymes: a new class of nitric oxide-forming nitrite reductases.Rice ( Oryza) hemoglobins.Residues in the Distal Heme Pocket of Arabidopsis Non-Symbiotic Hemoglobins: Implication for Nitrite Reductase Activity.Kinetic modulation in carbonmonoxy derivatives of truncated hemoglobins: the role of distal heme pocket residues and extended apolar tunnel.Binding of oxygen and carbon monoxide to a heme-regulated phosphodiesterase from Escherichia coli. Kinetics and infrared spectra of the full-length wild-type enzyme, isolated PAS domain, and Met-95 mutants.Hydroxylamine-induced oxidation of ferrous carbonylated truncated hemoglobins from Mycobacterium tuberculosis and Campylobacter jejuni is limited by carbon monoxide dissociation.The oxidation process of Antarctic fish hemoglobins.Structural dynamics in the active site of murine neuroglobin and its effects on ligand binding.Resonance Raman and ligand binding studies of the oxygen-sensing signal transducer protein HemAT from Bacillus subtilis.NO-degradation by alfalfa class 1 hemoglobin (Mhb1): a possible link to PR-1a gene expression in Mhb1-overproducing tobacco plants.
P2860
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P2860
Ligand binding and hexacoordination in synechocystis hemoglobin.
description
2001 nî lūn-bûn
@nan
2001 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Ligand binding and hexacoordination in synechocystis hemoglobin.
@ast
Ligand binding and hexacoordination in synechocystis hemoglobin.
@en
type
label
Ligand binding and hexacoordination in synechocystis hemoglobin.
@ast
Ligand binding and hexacoordination in synechocystis hemoglobin.
@en
prefLabel
Ligand binding and hexacoordination in synechocystis hemoglobin.
@ast
Ligand binding and hexacoordination in synechocystis hemoglobin.
@en
P2093
P2860
P356
P1476
Ligand binding and hexacoordination in synechocystis hemoglobin.
@en
P2093
Hargrove MS
Hvitved AN
Trent JT 3rd
P2860
P304
34714-34721
P356
10.1074/JBC.M105175200
P407
P577
2001-07-03T00:00:00Z