Evidence for two ferryl species in chloroperoxidase compound II.
about
Crystallographic and spectroscopic studies of peroxide-derived myoglobin compound II and occurrence of protonated FeIV ONature of the Ferryl Heme in Compounds I and IIDistinct reaction pathways followed upon reduction of oxy-heme oxygenase and oxy-myoglobin as characterized by Mössbauer spectroscopy.Spectroscopic Investigations of Catalase Compound II: Characterization of an Iron(IV) Hydroxide Intermediate in a Non-thiolate-Ligated Heme Enzyme.Reactive intermediates in cytochrome p450 catalysis.Iron(IV)hydroxide pK(a) and the role of thiolate ligation in C-H bond activation by cytochrome P450Enzyme reactivation by hydrogen peroxide in heme-based tryptophan dioxygenaseA catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical.X-ray absorption spectroscopic characterization of a cytochrome P450 compound II derivative.QM/MM study of the active species of the human cytochrome P450 3A4, and the influence thereof of the multiple substrate binding.A long-lived, substrate-hydroxylating peroxodiiron(III/III) intermediate in the amine oxygenase, AurF, from Streptomyces thioluteusMicrobial enzymes for aromatic compound hydroxylation.Bis-Fe(IV): nature's sniper for long-range oxidation.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.Ferryl haem protonation gates peroxidatic reactivity in globins.Characterizing the Intermediates Compound I and II in the Cytochrome P450 Catalytic Cycle with Nonlinear X-ray Spectroscopy: A Simulation Study.A new look at the role of thiolate ligation in cytochrome P450.Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins.1958-2014: after 56 years of research, cytochrome p450 reactivity is finally explained.
P2860
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P2860
Evidence for two ferryl species in chloroperoxidase compound II.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh-hant
name
Evidence for two ferryl species in chloroperoxidase compound II.
@en
Evidence for two ferryl species in chloroperoxidase compound II.
@nl
type
label
Evidence for two ferryl species in chloroperoxidase compound II.
@en
Evidence for two ferryl species in chloroperoxidase compound II.
@nl
prefLabel
Evidence for two ferryl species in chloroperoxidase compound II.
@en
Evidence for two ferryl species in chloroperoxidase compound II.
@nl
P2093
P356
P1476
Evidence for two ferryl species in chloroperoxidase compound II.
@en
P2093
Kari L Stone
Lee M Hoffart
Michael T Green
Rachel K Behan
P304
P356
10.1021/JA057876W
P407
P577
2006-05-01T00:00:00Z