Heme degradation as catalyzed by a recombinant bacterial heme oxygenase (Hmu O) from Corynebacterium diphtheriae.
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Crystal structures of the NO- and CO-bound heme oxygenase from Neisseriae meningitidis. Implications for O2 activationThe crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriaeCrystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: implications for heme oxygenase functionRegulation of intracellular heme levels by HMX1, a homologue of heme oxygenase, in Saccharomyces cerevisiae.The heme complex of Hmu O, a bacterial heme degradation enzyme from Corynebacterium diphtheriae. Structure of the catalytic site.Emerging strategies in microbial haem capture.Solution 1H NMR investigation of the active site molecular and electronic structures of substrate-bound, cyanide-inhibited HmuO, a bacterial heme oxygenase from Corynebacterium diphtheriae.Modulation of the axial water hydrogen-bonding properties by chemical modification of the substrate in resting state, substrate-bound heme oxygenase from Neisseria meningitidis; coupling to the distal H-bond network via ordered water molecules.Degradation of heme in gram-negative bacteria: the product of the hemO gene of Neisseriae is a heme oxygenase.Use of heme compounds as iron sources by pathogenic neisseriae requires the product of the hemO geneIdentification of an Escherichia coli O157:H7 heme oxygenase with tandem functional repeatsSolution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexesDesign of metal cofactors activated by a protein-protein electron transfer system.Heme utilization in Campylobacter jejuni.Structure prediction and activity analysis of human heme oxygenase-1 and its mutant.Structures of the substrate-free and product-bound forms of HmuO, a heme oxygenase from corynebacterium diphtheriae: x-ray crystallography and molecular dynamics investigation.Artificial metalloenzymes constructed from hierarchically-assembled proteins.IsdG and IsdI, heme-degrading enzymes in the cytoplasm of Staphylococcus aureus.Reaction intermediates in the heme degradation reaction by HutZ from Vibrio cholerae.Homologues of neisserial heme oxygenase in gram-negative bacteria: degradation of heme by the product of the pigA gene of Pseudomonas aeruginosaRegiospecificity determinants of human heme oxygenase: differential NADPH- and ascorbate-dependent heme cleavage by the R183E mutant.Roles of distal Asp in heme oxygenase from Corynebacterium diphtheriae, HmuO: A water-driven oxygen activation mechanism.Density functional theory studies on the conversion of hydroxyheme to iron-verdoheme in the presence of dioxygen.Structure of the Escherichia coli O157:H7 heme oxygenase ChuS in complex with heme and enzymatic inactivation by mutation of the heme coordinating residue His-193.
P2860
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P2860
Heme degradation as catalyzed by a recombinant bacterial heme oxygenase (Hmu O) from Corynebacterium diphtheriae.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh-hant
name
Heme degradation as catalyzed ...... m Corynebacterium diphtheriae.
@en
Heme degradation as catalyzed by a recombinant bacterial heme oxygenase
@nl
type
label
Heme degradation as catalyzed ...... m Corynebacterium diphtheriae.
@en
Heme degradation as catalyzed by a recombinant bacterial heme oxygenase
@nl
prefLabel
Heme degradation as catalyzed ...... m Corynebacterium diphtheriae.
@en
Heme degradation as catalyzed by a recombinant bacterial heme oxygenase
@nl
P2093
P2860
P356
P1476
Heme degradation as catalyzed ...... m Corynebacterium diphtheriae.
@en
P2093
P2860
P304
21319-21325
P356
10.1074/JBC.274.30.21319
P407
P577
1999-07-01T00:00:00Z