Spectroscopy and kinetics of wild-type and mutant tyrosine hydroxylase: mechanistic insight into O2 activation
about
Evidence for a high-spin Fe(IV) species in the catalytic cycle of a bacterial phenylalanine hydroxylaseMeasurement of intrinsic rate constants in the tyrosine hydroxylase reactionFormation of the iron-oxo hydroxylating species in the catalytic cycle of aromatic amino acid hydroxylases.Mechanisms of tryptophan and tyrosine hydroxylase.Activation of phenylalanine hydroxylase by phenylalanine does not require binding in the active siteActive-site structure of a β-hydroxylase in antibiotic biosynthesisX-ray absorption spectroscopy structural investigation of early intermediates in the mechanism of DNA repair by human ABH2.Theoretical study of the mechanism of oxoiron(IV) formation from H2O2 and a nonheme iron(II) complex: O-O cleavage involving proton-coupled electron transferPulsed EPR study of amino acid and tetrahydropterin binding in a tyrosine hydroxylase nitric oxide complex: evidence for substrate rearrangements in the formation of the oxygen-reactive complex.First- and second-sphere contributions to Fe(II) site activation by cosubstrate binding in non-heme Fe enzymes.Allosteric regulation of phenylalanine hydroxylase.Complex molecular regulation of tyrosine hydroxylase.Spectroscopic analyses of 2-oxoglutarate-dependent oxygenases: TauD as a case study.Dioxygen activation by nonheme iron enzymes with the 2-His-1-carboxylate facial triad that generate high-valent oxoiron oxidants.Characterization of unstable products of flavin- and pterin-dependent enzymes by continuous-flow mass spectrometry.Measurement of the intramolecular isotope effect on aliphatic hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase.Kinetic mechanism of phenylalanine hydroxylase: intrinsic binding and rate constants from single-turnover experiments.Single turnover kinetics of tryptophan hydroxylase: evidence for a new intermediate in the reaction of the aromatic amino acid hydroxylases.Mutagenesis of a specificity-determining residue in tyrosine hydroxylase establishes that the enzyme is a robust phenylalanine hydroxylase but a fragile tyrosine hydroxylaseMagnetic circular dichroism studies of iron(ii) binding to human calprotectin.Near-stoichiometric conversion of H(2)O(2) to Fe(IV)=O at a nonheme iron(II) center. Insights into the O-O bond cleavage step.Spectroscopic studies of the mononuclear non-heme Fe(II) enzyme FIH: second-sphere contributions to reactivity.C-H Activation from Iron(II)-Nitroxido Complexes.Demonstration of the heterolytic O-O bond cleavage of putative nonheme iron(II)-OOH(R) complexes for Fenton and enzymatic reactions.NRVS Studies of the Peroxide Shunt Intermediate in a Rieske Dioxygenase and Its Relation to the Native FeII O2 Reaction.
P2860
Q24594412-3AE446AF-A3F8-492C-9850-181821F55F0DQ28578356-31E64B76-7CF1-4239-AC63-D8E0116A51AEQ34166879-C4441F3C-915D-48DE-A4F4-A8265304B130Q34329841-595A46E6-AF33-4BC3-94CA-9EA1AE7D7D38Q34731673-C3F7F86B-A526-40C4-8E48-9659E13E72FCQ34985898-D751986B-E52F-46D7-918F-7F134193CCACQ35070629-36A2DB8C-ACE1-4608-81E5-994F8AC7D730Q35104404-E70CB79B-2CBA-4AE6-8C76-95BABDBF4F38Q37518382-5F859313-8E4A-47FA-9A77-931D45ECE42EQ37686836-1C6116F1-EF82-4B63-9C3C-38D9FAE1455EQ37946639-94485D39-5A4C-46D1-8D14-5E8D7289490BQ38215359-1F011908-1CB6-45CA-931E-1DC711FE2523Q38998319-0066C65F-E4BC-4828-AB44-4D9EA20FBD3CQ39078942-AFB7C406-D24A-4797-BC47-DD13655E7659Q39234649-E575B86A-8F98-4C68-AC9C-47EDE71994A3Q40148585-664FD5B3-3ED5-4A69-BDF6-C72519A15579Q41817640-7EEA7DAF-20DE-487D-A565-3D73BC6C8501Q41928729-5E0983D3-4FB1-4C85-9615-3F61B73E3588Q42024350-2D6CB715-B569-45C0-9EE2-361FC6AB3D7DQ42314747-5988D207-4AC8-426E-ADC1-E6F8B7D71189Q42913355-C3364078-3027-48D1-AD4A-9A329563112EQ43090007-2BBFC954-86A7-405D-B9DE-A9F069EF7FE6Q46327417-7621CC82-6D5C-4DAB-B426-24C741D1488CQ46881367-A51C8A9C-C219-4005-8D55-DB27D19628D8Q55001908-E7BECC18-FD84-4938-A955-080DF882BA30
P2860
Spectroscopy and kinetics of wild-type and mutant tyrosine hydroxylase: mechanistic insight into O2 activation
description
2009 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հունիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2009
@ast
im Juni 2009 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2009/06/10)
@sk
vědecký článek publikovaný v roce 2009
@cs
wetenschappelijk artikel (gepubliceerd op 2009/06/10)
@nl
наукова стаття, опублікована в червні 2009
@uk
مقالة علمية (نشرت في 10-6-2009)
@ar
name
Spectroscopy and kinetics of w ...... tic insight into O2 activation
@ast
Spectroscopy and kinetics of w ...... tic insight into O2 activation
@en
Spectroscopy and kinetics of w ...... tic insight into O2 activation
@nl
type
label
Spectroscopy and kinetics of w ...... tic insight into O2 activation
@ast
Spectroscopy and kinetics of w ...... tic insight into O2 activation
@en
Spectroscopy and kinetics of w ...... tic insight into O2 activation
@nl
prefLabel
Spectroscopy and kinetics of w ...... tic insight into O2 activation
@ast
Spectroscopy and kinetics of w ...... tic insight into O2 activation
@en
Spectroscopy and kinetics of w ...... tic insight into O2 activation
@nl
P2093
P2860
P356
P1476
Spectroscopy and kinetics of w ...... tic insight into O2 activation
@en
P2093
Bekir E. Eser
Britt Hedman
Edward I. Solomon
Keith O. Hodgson
Marina S. Chow
Paul F. Fitzpatrick
Samuel A. Wilson
P2860
P304
P356
10.1021/JA810080C
P407
P577
2009-06-10T00:00:00Z