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Crystallographic and spectroscopic studies of peroxide-derived myoglobin compound II and occurrence of protonated FeIV OCrystallographic and Single-Crystal Spectral Analysis of the Peroxidase Ferryl IntermediateNature of the Ferryl Heme in Compounds I and IIHeme enzymes. Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidaseMolecular mechanisms for generating transmembrane proton gradientsThermochemistry of proton-coupled electron transfer reagents and its implicationsReactivity of an Fe(IV)-Oxo Complex with Protons and OxidantsSpectroscopic Investigations of Catalase Compound II: Characterization of an Iron(IV) Hydroxide Intermediate in a Non-thiolate-Ligated Heme Enzyme.Setting an upper limit on the myoglobin iron(IV)hydroxide pK(a): insight into axial ligand tuning in heme protein catalysis.Reactive intermediates in cytochrome p450 catalysis.Iron(IV)hydroxide pK(a) and the role of thiolate ligation in C-H bond activation by cytochrome P450Resonance Raman spectroscopy of chloroperoxidase compound II provides direct evidence for the existence of an iron(IV)-hydroxide.Proton-coupled electron transfer reactions at a heme-propionate in an iron-protoporphyrin-IX model compoundEnzyme reactivation by hydrogen peroxide in heme-based tryptophan dioxygenaseFerryl derivatives of human indoleamine 2,3-dioxygenaseCrystal structure of the pristine peroxidase ferryl center and its relevance to proton-coupled electron transfer.Axial ligand tuning of a nonheme iron(IV)-oxo unit for hydrogen atom abstractionX-ray absorption spectroscopic characterization of a cytochrome P450 compound II derivative.Resonance Raman spectroscopic studies of hydroperoxo derivatives of cobalt-substituted myoglobin.Lessons from nature: unraveling biological CH bond activationDirect visualization of a Fe(IV)-OH intermediate in a heme enzyme.Lewis-Acid-assisted Hydrogen Atom Transfer to Manganese(V)-Oxo Corrole through Valence TautomerizationBeyond ferryl-mediated hydroxylation: 40 years of the rebound mechanism and C-H activation.Spectroscopic features of cytochrome P450 reaction intermediatesThe reactivity of the active metal oxo and hydroxo intermediates and their implications in oxidations.Role of the Proximal Cysteine Hydrogen Bonding Interaction in Cytochrome P450 2B4 Studied by Cryoreduction, Electron Paramagnetic Resonance, and Electron-Nuclear Double Resonance Spectroscopy.Characterization of monomeric Mn(II/III/IV)-hydroxo complexes from X- and Q-band dual mode electron paramagnetic resonance (EPR) spectroscopy.Toward a chemical mechanism of proton pumping by the B-type cytochrome c oxidases: application of density functional theory to cytochrome ba3 of Thermus thermophilus.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.Reaction Intermediates and Molecular Mechanism of Peroxynitrite Activation by NO Synthases.A new look at the role of thiolate ligation in cytochrome P450.Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins.
P2860
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P2860
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-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
2006年學術文章
@zh-hant
name
On the status of ferryl protonation.
@ast
On the status of ferryl protonation.
@en
type
label
On the status of ferryl protonation.
@ast
On the status of ferryl protonation.
@en
prefLabel
On the status of ferryl protonation.
@ast
On the status of ferryl protonation.
@en
P1476
On the status of ferryl protonation.
@en
P2093
Michael T Green
Rachel K Behan
P304
P356
10.1016/J.JINORGBIO.2005.12.019
P577
2006-02-28T00:00:00Z