Distinct reaction pathways followed upon reduction of oxy-heme oxygenase and oxy-myoglobin as characterized by Mössbauer spectroscopy.
about
An oxyferrous heme/protein-based radical intermediate is catalytically competent in the catalase reaction of Mycobacterium tuberculosis catalase-peroxidase (KatG)Crystallographic and Spectroscopic Insights into Heme Degradation by Mycobacterium tuberculosis MhuDHeme enzyme structure and function.Resonance Raman characterization of the peroxo and hydroperoxo intermediates in cytochrome P450.Enzyme reactivation by hydrogen peroxide in heme-based tryptophan dioxygenaseDynamic ruffling distortion of the heme substrate in non-canonical heme oxygenase enzymes.Resonance Raman spectroscopic studies of hydroperoxo derivatives of cobalt-substituted myoglobin.Active intermediates in heme monooxygenase reactions as revealed by cryoreduction/annealing, EPR/ENDOR studies.Why copper is preferred over iron for oxygen activation and reduction in haem-copper oxidases.Tight binding of heme to Staphylococcus aureus IsdG and IsdI precludes design of a competitive inhibitor.Heme utilization by pathogenic bacteria: not all pathways lead to biliverdin.Unprecedented Fe(IV) Species in a Diheme Protein MauG: A Quantum Chemical Investigation on the Unusual Mössbauer Spectroscopic Properties.Electron paramagnetic resonance and electron-nuclear double resonance studies of the reactions of cryogenerated hydroperoxoferric-hemoprotein intermediates.Cryoradiolysis and cryospectroscopy for studies of heme-oxygen intermediates in cytochromes p450.Characterization of the microsomal cytochrome P450 2B4 O2 activation intermediates by cryoreduction and electron paramagnetic resonance.Manganese and Cobalt in the Nonheme-Metal-Binding Site of a Biosynthetic Model of Heme-Copper Oxidase Superfamily Confer Oxidase Activity through Redox-Inactive Mechanism.Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins.Cryoradiolysis as a Method for Mechanistic Studies in Inorganic Biochemistry
P2860
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P2860
Distinct reaction pathways followed upon reduction of oxy-heme oxygenase and oxy-myoglobin as characterized by Mössbauer spectroscopy.
description
2007 nî lūn-bûn
@nan
2007 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Distinct reaction pathways fol ...... zed by Mössbauer spectroscopy.
@ast
Distinct reaction pathways fol ...... zed by Mössbauer spectroscopy.
@en
type
label
Distinct reaction pathways fol ...... zed by Mössbauer spectroscopy.
@ast
Distinct reaction pathways fol ...... zed by Mössbauer spectroscopy.
@en
prefLabel
Distinct reaction pathways fol ...... zed by Mössbauer spectroscopy.
@ast
Distinct reaction pathways fol ...... zed by Mössbauer spectroscopy.
@en
P2093
P2860
P356
P1476
Distinct reaction pathways fol ...... ized by Mössbauer spectroscopy
@en
P2093
Boi Hanh Huynh
Brian M Hoffman
Masao Ikeda-Saito
Roman M Davydov
P2860
P304
P356
10.1021/JA067209I
P407
P577
2007-02-01T00:00:00Z