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Carboxyl Group of Glu113 Is Required for Stabilization of the Diferrous and Bis-Fe IV States of MauGProbing the conformational mobility of the active site of a heme peroxidaseA structural and dynamic investigation of the inhibition of catalase by nitric oxideHeme enzymes. Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidaseReactivity of an Fe(IV)-Oxo Complex with Protons and OxidantsSetting an upper limit on the myoglobin iron(IV)hydroxide pK(a): insight into axial ligand tuning in heme protein catalysis.In crystallo optical spectroscopy (icOS) as a complementary tool on the macromolecular crystallography beamlines of the ESRF.Ferryl protonation in oxoiron(IV) porphyrins and its role in oxygen transferRoles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis-FeIV state of MauG.Geometric and electronic structures of the His-Fe(IV)=O and His-Fe(IV)-Tyr hemes of MauG.MauG: a di-heme enzyme required for methylamine dehydrogenase maturation.Converting the bis-FeIV state of the diheme enzyme MauG to Compound I decreases the reorganization energy for electron transferMechanism of protein oxidative damage that is coupled to long-range electron transfer to high-valent haems.Production of dioxygen in the dark: dismutases of oxyanions.Direct visualization of a Fe(IV)-OH intermediate in a heme enzyme.MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis.Structure-Based Mechanism for Oxidative Decarboxylation Reactions Mediated by Amino Acids and Heme Propionates in Coproheme Decarboxylase (HemQ).Combining X-ray and neutron crystallography with spectroscopyA Suicide Mutation Affecting Proton Transfers to High-Valent Hemes Causes Inactivation of MauG during Catalysis.The pKa value of the proximal water molecule trans to a high-valent MnV[double bond, length as m-dash]O porphyrin: towards the control of reactivity by pH.Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins.Reactivity Patterns of (Protonated) Compound II and Compound I of Cytochrome P450: Which is the Better Oxidant?Properties of the high-spin heme of MauG are altered by binding of preMADH at the protein surface 40 Å away.Decarboxylation involving a ferryl, propionate, and a tyrosyl group in a radical relay yields heme <em>b</em>.Intramolecular Oxidative O-Demethylation of an Oxoferryl Porphyrin Complexed with a Per-O-methylated β-Cyclodextrin Dimer.The rise of neutron cryo-crystallography
P2860
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P2860
description
2011 nî lūn-bûn
@nan
2011 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2011年の論文
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2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Nature of the Ferryl Heme in Compounds I and II
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Nature of the Ferryl Heme in Compounds I and II
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Nature of the Ferryl Heme in Compounds I and II
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Nature of the Ferryl Heme in Compounds I and II
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type
label
Nature of the Ferryl Heme in Compounds I and II
@ast
Nature of the Ferryl Heme in Compounds I and II
@en
Nature of the Ferryl Heme in Compounds I and II
@en-gb
Nature of the Ferryl Heme in Compounds I and II
@nl
prefLabel
Nature of the Ferryl Heme in Compounds I and II
@ast
Nature of the Ferryl Heme in Compounds I and II
@en
Nature of the Ferryl Heme in Compounds I and II
@en-gb
Nature of the Ferryl Heme in Compounds I and II
@nl
P2860
P50
P356
P1476
Nature of the Ferryl Heme in Compounds I and II
@en
P2093
Andrea Gumiero
P2860
P304
P356
10.1074/JBC.M110.183483
P407
P577
2011-01-14T00:00:00Z