Sensitivity of tyrosyl radical g-values to changes in protein structure: a high-field EPR study of mutants of ribonucleotide reductase.

Sensitivity of tyrosyl radical g-values to changes in protein structure: a high-field EPR study of mutants of ribonucleotide reductase.

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http://www.wikidata.org/entity/Q30328406
An oxyferrous heme/protein-based radical intermediate is catalytically competent in the catalase reaction of Mycobacterium tuberculosis catalase-peroxidase (KatG)Displacement of the tyrosyl radical cofactor in ribonucleotide reductase obtained by single-crystal high-field EPR and 1.4-A x-ray dataProtein Radicals in Fungal Versatile Peroxidase: CATALYTIC TRYPTOPHAN RADICAL IN BOTH COMPOUND I AND COMPOUND II AND STUDIES ON W164Y, W164H, AND W164S VARIANTSCrystallographic, Kinetic, and Spectroscopic Study of the First Ligninolytic Peroxidase Presenting a Catalytic TyrosineHF-EPR, Raman, UV/VIS light spectroscopic, and DFT studies of the ribonucleotide reductase R2 tyrosyl radical from Epstein-Barr virusIdentifying the elusive sites of tyrosyl radicals in cytochrome c peroxidase: implications for oxidation of substrates bound at a site remote from the heme.Spectroscopic studies of the iron and manganese reconstituted tyrosyl radical in Bacillus cereus ribonucleotide reductase R2 protein.Spectroscopic and theoretical approaches for studying radical reactions in class I ribonucleotide reductase.Single and double nitroxide labeled bis(terpyridine)-copper(II): influence of orientation selectivity and multispin effects on PELDOR and RIDME.Determination of the structural environment of the tyrosyl radical in prostaglandin H2 synthase-1: a high frequency ENDOR/EPR study.Structural comparisons of arachidonic acid-induced radicals formed by prostaglandin H synthase-1 and -2.High field EPR study of the pheophytin anion radical in wild type and D1-E130 mutants of photosystem II in Chlamydomonas reinhardtii.Tyrosine radical formation in the reaction of wild type and mutant cytochrome P450cam with peroxy acids: a multifrequency EPR study of intermediates on the millisecond time scale.The use of multi-frequency EPR techniques to identify the radicals produced in irradiated beta-blockers.A tryptophan neutral radical in the oxidized state of versatile peroxidase from Pleurotus eryngii: a combined multifrequency EPR and density functional theory study.Orientation of the tyrosyl radical in Salmonella typhimurium class Ib ribonucleotide reductase determined by high field EPR of R2F single crystals.EPR parameters of amino acid radicals in P. eryngii versatile peroxidase and its W164Y variant computed at the QM/MM level
P2860

Sensitivity of tyrosyl radical g-values to changes in protein structure: a high-field EPR study of mutants of ribonucleotide reductase.

Item
http://www.wikidata.org/entity/Q30328406
description
2001 nî lūn-bûn
@nan
2001 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Sensitivity of tyrosyl radical ...... s of ribonucleotide reductase.
@ast
Sensitivity of tyrosyl radical ...... s of ribonucleotide reductase.
@en
type
label
Sensitivity of tyrosyl radical ...... s of ribonucleotide reductase.
@ast
Sensitivity of tyrosyl radical ...... s of ribonucleotide reductase.
@en
prefLabel
Sensitivity of tyrosyl radical ...... s of ribonucleotide reductase.
@ast
Sensitivity of tyrosyl radical ...... s of ribonucleotide reductase.
@en
P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P577
P698
P356
P1433
P1476
Sensitivity of tyrosyl radical ...... s of ribonucleotide reductase.
@en
P2093
P304
P31
P356
P407
P433
P478
P577
P698