Resonance Raman spectroscopy of chloroperoxidase compound II provides direct evidence for the existence of an iron(IV)-hydroxide.
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Crystallographic and spectroscopic studies of peroxide-derived myoglobin compound II and occurrence of protonated FeIV OMechanisms of peroxynitrite interactions with heme proteinsReactivity of an Fe(IV)-Oxo Complex with Protons and OxidantsDistinct 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.Low-frequency dynamics of Caldariomyces fumago chloroperoxidase probed by femtosecond coherence spectroscopy.Insight into the mechanism of an iron dioxygenase by resolution of steps following the FeIV=HO speciesSetting 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 P450Structure of the key species in the enzymatic oxidation of methane to methanolAxial ligand tuning of a nonheme iron(IV)-oxo unit for hydrogen atom abstractionExperimental documentation of the structural consequences of hydrogen-bonding interactions to the proximal cysteine of a cytochrome P450.X-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 activationThe protonation states of oxo-bridged Mn(IV) dimers resolved by experimental and computational Mn K pre-edge X-ray absorption spectroscopy.Spectroscopic and theoretical investigation of a complex with an [O═Fe(IV)-O-Fe(IV)═O] core related to methane monooxygenase intermediate Q.Spectroscopic studies of the cytochrome P450 reaction mechanisms.Role of the Proximal Cysteine Hydrogen Bonding Interaction in Cytochrome P450 2B4 Studied by Cryoreduction, Electron Paramagnetic Resonance, and Electron-Nuclear Double Resonance Spectroscopy.Water-soluble Fe(II)-H2O complex with a weak O-H bond transfers a hydrogen atom via an observable monomeric Fe(III)-OH.Synthesis and structural characterization of a series of Mn(III)OR complexes, including a water-soluble Mn(III)OH that promotes aerobic hydrogen-atom transfer.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.Direct Observation of Oxygen Rebound with an Iron-Hydroxide Complex.Cross-linking of dicyclotyrosine by the cytochrome P450 enzyme CYP121 from Mycobacterium tuberculosis proceeds through a catalytic shunt pathway.Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins.
P2860
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P2860
Resonance Raman spectroscopy of chloroperoxidase compound II provides direct evidence for the existence of an iron(IV)-hydroxide.
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2006 nî lūn-bûn
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2006 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
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2006 թվականի օգոստոսին հրատարակված գիտական հոդված
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2006年の論文
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2006年論文
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2006年論文
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2006年論文
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2006年論文
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2006年論文
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2006年论文
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name
Resonance Raman spectroscopy o ...... ence of an iron(IV)-hydroxide.
@ast
Resonance Raman spectroscopy o ...... ence of an iron(IV)-hydroxide.
@en
type
label
Resonance Raman spectroscopy o ...... ence of an iron(IV)-hydroxide.
@ast
Resonance Raman spectroscopy o ...... ence of an iron(IV)-hydroxide.
@en
prefLabel
Resonance Raman spectroscopy o ...... ence of an iron(IV)-hydroxide.
@ast
Resonance Raman spectroscopy o ...... ence of an iron(IV)-hydroxide.
@en
P2093
P2860
P356
P1476
Resonance Raman spectroscopy o ...... ence of an iron(IV)-hydroxide.
@en
P2093
Kari L Stone
Michael T Green
Rachel K Behan
P2860
P304
12307-12310
P356
10.1073/PNAS.0603159103
P407
P577
2006-08-08T00:00:00Z