about
Strong Inhibition of O-Atom Transfer Reactivity for Mn(IV)(O)(π-Radical-Cation)(Lewis Acid) versus Mn(V)(O) Porphyrinoid ComplexesPhotooxidation of cytochrome P450-BM3.Heme enzyme structure and function.Molecular probes of the mechanism of cytochrome P450. Oxygen traps a substrate radical intermediateReactive intermediates in cytochrome p450 catalysis.Ferryl protonation in oxoiron(IV) porphyrins and its role in oxygen transferDetection and kinetic characterization of a highly reactive heme-thiolate peroxygenase compound I.Kinetic solvent isotope effect in human P450 CYP17A1-mediated androgen formation: evidence for a reactive peroxoanion intermediate.Idiosyncratic Drug-Induced Liver Injury (IDILI): Potential Mechanisms and Predictive Assays.Cytochrome P450 119 Compounds I Formed by Chemical Oxidation and Photooxidation Are the Same Species.Role of metal-oxo complexes in the cleavage of C-H bonds.N-H Bond Dissociation Enthalpies and Facile H Atom Transfers for Early Intermediates of Fe-N2 and Fe-CN Reductions.Spectroscopic and Kinetic Evidence for the Crucial Role of Compound 0 in the P450cam -Catalyzed Hydroxylation of Camphor by Hydrogen Peroxide.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.Characterization of a selenocysteine-ligated P450 compound I reveals direct link between electron donation and reactivity.Mechanistic insight into peroxo-shunt formation of biomimetic models for compound II, their reactivity toward organic substrates, and the influence of N-methylimidazole axial ligation.Axial ligand and spin-state influence on the formation and reactivity of hydroperoxo-iron(III) porphyrin complexes.
P2860
Q28829610-2C50C679-4DF6-4A5E-AE03-BF12E44205B2Q33718983-F39DA070-0EAD-4E19-B31E-2DD5810DAC02Q34396417-02CCAE70-8AB9-45E5-A522-425BC39B09F8Q34586651-E02461FD-B8E8-4EF6-B1E8-B6E2098670C7Q34696669-4907220F-1EBB-4E5E-8F7B-D0C96F178D15Q35189151-EDF1321A-CF53-42E4-A6DA-454D1CA286D8Q36456678-B6079199-BED0-45E3-B0A7-1AD8E42402A5Q37401626-67E0F393-D384-4233-85C7-D64A993136E7Q37590883-E86C3100-B401-4789-BACB-20E83791ECC5Q37595609-32F8A457-1970-4F6B-A382-C657A0C72B73Q37848679-EE5CACE4-A4DC-4030-84E8-7E3FB9F8386BQ38989706-A4619785-5CBF-4B64-82EC-C29BD47E59B9Q40557386-CE270220-C90D-4AFE-BAC9-5E7D07431351Q44220998-E016013E-9B3F-4A07-B75B-001503B953E9Q44446386-6FB25C30-590F-4A0D-84D8-0E59F00B4D08Q46644746-3024B0D8-6E05-45CF-9B18-B1BE9B25922FQ46944261-4CFAD380-9571-4059-8E10-9D3BDB0A876BQ53172447-E2E79373-9B52-4954-A1A4-EC748A5B0F9A
P2860
description
2010 nî lūn-bûn
@nan
2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Cytochrome P450: the active oxidant and its spectrum.
@ast
Cytochrome P450: the active oxidant and its spectrum.
@en
Cytochrome P450: the active oxidant and its spectrum.
@nl
type
label
Cytochrome P450: the active oxidant and its spectrum.
@ast
Cytochrome P450: the active oxidant and its spectrum.
@en
Cytochrome P450: the active oxidant and its spectrum.
@nl
prefLabel
Cytochrome P450: the active oxidant and its spectrum.
@ast
Cytochrome P450: the active oxidant and its spectrum.
@en
Cytochrome P450: the active oxidant and its spectrum.
@nl
P2093
P356
P1433
P1476
Cytochrome P450: the active oxidant and its spectrum.
@en
P2093
Jarod M Younker
Jonathan Rittle
Michael T Green
P304
P356
10.1021/IC902062D
P407
P577
2010-04-01T00:00:00Z