Roles of distal Asp in heme oxygenase from Corynebacterium diphtheriae, HmuO: A water-driven oxygen activation mechanism.
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The IsdG-family of haem oxygenases degrades haem to a novel chromophoreDistinct reaction pathways followed upon reduction of oxy-heme oxygenase and oxy-myoglobin as characterized by Mössbauer spectroscopy.Coupling of the distal hydrogen bond network to the exogenous ligand in substrate-bound, resting state human heme oxygenase.Electronic properties of the highly ruffled heme bound to the heme degrading enzyme IsdI.Spectroscopic insights into axial ligation and active-site H-bonding in substrate-bound human heme oxygenase-2.Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexesAutomated protein motif generation in the structure-based protein function prediction tool ProMOL.Role of propionates in substrate binding to heme oxygenase from Neisseria meningitidis: a nuclear magnetic resonance studyUnique coupling of mono- and dioxygenase chemistries in a single active site promotes heme degradation.The orbital ground state of the azide-substrate complex of human heme oxygenase is an indicator of distal H-bonding: implications for the enzyme mechanism.1H NMR study of the effect of variable ligand on heme oxygenase electronic and molecular structure.Reaction intermediates in the heme degradation reaction by HutZ from Vibrio cholerae.An unexpected reactivity of the P460 cofactor in hydroxylamine oxidoreductase.Function Coupling Mechanism of PhuS and HemO in Heme Degradation.Heme utilization by pathogenic bacteria: not all pathways lead to biliverdin.A Metagenomic Analysis of Bacterial Microbiota in the Digestive Tract of Triatomines.Biomimic O2 activation hydroxylates a meso-carbon of the porphyrin ring regioselectively under mild conditions.O(2)- and H(2)O(2)-dependent verdoheme degradation by heme oxygenase: reaction mechanisms and potential physiological roles of the dual pathway degradation.Hydrogen sulfide bypasses the rate-limiting oxygen activation of heme oxygenase
P2860
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P2860
Roles of distal Asp in heme oxygenase from Corynebacterium diphtheriae, HmuO: A water-driven oxygen activation mechanism.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年學術文章
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name
Roles of distal Asp in heme ox ...... n oxygen activation mechanism.
@en
Roles of distal Asp in heme ox ...... n oxygen activation mechanism.
@nl
type
label
Roles of distal Asp in heme ox ...... n oxygen activation mechanism.
@en
Roles of distal Asp in heme ox ...... n oxygen activation mechanism.
@nl
prefLabel
Roles of distal Asp in heme ox ...... n oxygen activation mechanism.
@en
Roles of distal Asp in heme ox ...... n oxygen activation mechanism.
@nl
P2093
P2860
P356
P1476
Roles of distal Asp in heme ox ...... en oxygen activation mechanism
@en
P2093
Masaki Unno
Masao Ikeda-Saito
Momoko Furukawa
P2860
P304
P356
10.1074/JBC.M410263200
P407
P577
2004-11-04T00:00:00Z