Resonance Raman characterization of the peroxo and hydroperoxo intermediates in cytochrome P450.
about
Using resonance Raman cross-section data to estimate the spin state populations of Cytochromes P450.Defining the structural consequences of mechanism-based inactivation of mammalian cytochrome P450 2B4 using resonance Raman spectroscopy.Spin equilibrium and O₂-binding kinetics of Mycobacterium tuberculosis CYP51 with mutations in the histidine-threonine dyadCytochromes P450 in nanodiscs.Defining CYP3A4 structural responses to substrate binding. Raman spectroscopic studies of a nanodisc-incorporated mammalian cytochrome P450.Evidence for an elevated aspartate pK(a) in the active site of human aromataseAcid-catalyzed disproportionation of oxoiron(IV) porphyrins to give oxoiron(IV) porphyrin radical cations.Evidence for a ferryl intermediate in a heme-based dioxygenase.Differences and comparisons of the properties and reactivities of iron(III)-hydroperoxo complexes with saturated coordination sphereUnveiling the crucial intermediates in androgen production.Experimental documentation of the structural consequences of hydrogen-bonding interactions to the proximal cysteine of a cytochrome P450.The use of deuterated camphor as a substrate in (1)H ENDOR studies of hydroxylation by cryoreduced oxy P450cam provides new evidence of the involvement of compound IResonance Raman spectroscopic studies of hydroperoxo derivatives of cobalt-substituted myoglobin.Differential hydrogen bonding in human CYP17 dictates hydroxylation versus lyase chemistryCatalytic intermediates of inducible nitric-oxide synthase stabilized by the W188H mutationThe critical iron-oxygen intermediate in human aromataseKinetic solvent isotope effect in human P450 CYP17A1-mediated androgen formation: evidence for a reactive peroxoanion intermediate.Resonance Raman spectroscopy of the oxygenated intermediates of human CYP19A1 implicates a compound i intermediate in the final lyase step.Active intermediates in heme monooxygenase reactions as revealed by cryoreduction/annealing, EPR/ENDOR studies.Spectroscopic features of cytochrome P450 reaction intermediatesSpectroscopic studies of the cytochrome P450 reaction mechanisms.Spectroscopic and Kinetic Evidence for the Crucial Role of Compound 0 in the P450cam -Catalyzed Hydroxylation of Camphor by Hydrogen Peroxide.Cryoradiolysis and cryospectroscopy for studies of heme-oxygen intermediates in cytochromes p450.Phenol-Induced O-O Bond Cleavage in a Low-Spin Heme-Peroxo-Copper Complex: Implications for O2 Reduction in Heme-Copper Oxidases.Critical Aspects of Heme-Peroxo-Cu Complex Structure and Nature of Proton Source Dictate Metal-O(peroxo) Breakage versus Reductive O-O Cleavage Chemistry.A structurally-characterized peroxomanganese(iv) porphyrin from reversible O2 binding within a metal-organic framework.Axial ligand and spin-state influence on the formation and reactivity of hydroperoxo-iron(III) porphyrin complexes.Human Cytochrome CYP17A1: The Structural Basis for Compromised Lyase Activity with 17-HydroxyprogesteroneCryoradiolysis as a Method for Mechanistic Studies in Inorganic Biochemistry
P2860
Q30737738-3D2746AE-6E47-422D-8A6E-9CC836F96CB4Q33646930-1C296972-FCFC-4761-98B9-593EBA52F026Q33859424-7370F095-211F-40AA-B6AB-F4F6F83189B2Q34284199-B0FA2278-201D-4F89-AE7A-CB4DC816BA83Q34551011-D0CB03A0-8F08-4F44-AE3F-950F7E58471EQ34958506-6A746502-47D8-4F06-A6F9-3D6D6832FD18Q34974304-B508B9C2-D3E3-4D00-B32D-6A80ECC84B7AQ35006504-ABFDEA37-4D3F-498E-8462-521BF2FA7FE2Q35046056-6A563F83-A0EA-4616-AEB7-0A0B1C2BFBE5Q36435371-B43526E9-1ADD-4D02-9C09-F967EBCD7778Q36453123-D7A7E830-784B-4BDE-B151-C05CFDD44000Q36600584-C80A5100-8967-4F9B-A622-885CF4845FB6Q37019230-06FD68D3-3B7B-41E6-A4C3-ACC269A21187Q37169659-31F5AC83-3902-4AEE-8C04-ACCDE482CB41Q37277511-343510AA-33AD-458C-A267-9AA7E3AADCC4Q37366162-0E72D69B-6A8F-4F2E-8371-4F5E832A5291Q37401626-D4665295-CCA3-4E16-88E0-B319F1AE7561Q37701442-C24154B4-886C-4A3E-AE81-C655CEDD0BB4Q37790461-C971BC8C-7BA4-4ACE-87DA-22EBA0B1E40BQ37822069-5E772E03-D897-4883-B8D5-D94741F00732Q39409036-F6DF019E-AB47-4A72-9C62-EDFE8D662E25Q40557386-D45AF080-3751-47FC-B1AE-9613AFEC24D1Q42921523-1BAA3F2A-D98B-43FA-99DA-FB42AA84DFA6Q46188634-D45CD2A8-DB23-4C0D-8B64-0BF3FE4893E4Q46342369-B3B914DB-8C83-4CE5-9AA9-C1FEBBDFD2BEQ52314815-C0A4D9D9-39A4-46A5-829B-1B0A47631560Q53172447-AC2E2085-A1A4-412E-B02A-8B8DEF431646Q57142928-FEF58A3B-AA29-4CF3-B033-CF35304998DBQ58035694-3C8D77B2-EEC5-4BE3-A9D5-2A18BAD20154
P2860
Resonance Raman characterization of the peroxo and hydroperoxo intermediates in cytochrome P450.
description
2008 nî lūn-bûn
@nan
2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Resonance Raman characterizati ...... ermediates in cytochrome P450.
@ast
Resonance Raman characterizati ...... ermediates in cytochrome P450.
@en
type
label
Resonance Raman characterizati ...... ermediates in cytochrome P450.
@ast
Resonance Raman characterizati ...... ermediates in cytochrome P450.
@en
prefLabel
Resonance Raman characterizati ...... ermediates in cytochrome P450.
@ast
Resonance Raman characterizati ...... ermediates in cytochrome P450.
@en
P2093
P2860
P356
P1476
Resonance Raman characterizati ...... ermediates in cytochrome P450.
@en
P2093
Ilia G Denisov
James R Kincaid
Piotr J Mak
Stephen G Sligar
P2860
P304
13172-13179
P356
10.1021/JP8017875
P407
P577
2008-12-01T00:00:00Z