Siroheme- and [Fe4-S4]-dependent NirA from Mycobacterium tuberculosis is a sulfite reductase with a covalent Cys-Tyr bond in the active site
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The alternative route to heme in the methanogenic archaeon Methanosarcina barkeriSulfite reduction in mycobacteriaCross-Link Formation of the Cysteine 228−Tyrosine 272 Catalytic Cofactor of Galactose Oxidase Does Not Require Dioxygen † ‡The Crystal Structure of Desulfovibrio vulgaris Dissimilatory Sulfite Reductase Bound to DsrC Provides Novel Insights into the Mechanism of Sulfate RespirationThe C-terminal of CysM from Mycobacterium tuberculosis protects the aminoacrylate intermediate and is involved in sulfur donor selectivityStructural Insights into Dissimilatory Sulfite Reductases: Structure of Desulforubidin from Desulfomicrobium NorvegicumStructure-function relationship of assimilatory nitrite reductases from the leaf and root of tobacco based on high-resolution structuresCovalent modifications of the catalytic tyrosine in octahaem cytochrome c nitrite reductase and their effect on the enzyme activityThe reductive reaction mechanism of tobacco nitrite reductase derived from a combination of crystal structures and ultraviolet-visible microspectroscopyX-ray crystal structure of a mutant assimilatory nitrite reductase that shows sulfite reductase-like activityStructural and mutational studies of an electron transfer complex of maize sulfite reductase and ferredoxinAtomic resolution modeling of the ferredoxin:[FeFe] hydrogenase complex from Chlamydomonas reinhardtiiThiol dioxygenases: unique families of cupin proteins.Identifying proteins that can form tyrosine-cysteine crosslinks.The electronic structure of the Cys-Tyr(*) free radical in galactose oxidase determined by EPR spectroscopyThe twists and turns of enzyme function.Identification and functional analysis of a nitrate assimilation operon nasACKBDEF from Amycolatopsis mediterranei U32.Spectroscopic and computational investigation of iron(III) cysteine dioxygenase: implications for the nature of the putative superoxo-Fe(III) intermediate.Comparative analyses of nonpathogenic, opportunistic, and totally pathogenic mycobacteria reveal genomic and biochemical variabilities and highlight the survival attributes of Mycobacterium tuberculosis.Drug targets in mycobacterial sulfur metabolism.New targets and inhibitors of mycobacterial sulfur metabolism.Perturbation of cytochrome c maturation reveals adaptability of the respiratory chain in Mycobacterium tuberculosis.Kinetics and mechanism of oxidation of super-reduced cobalamin and cobinamide species by thiosulfate, sulfite and dithioniteSpectroscopic and computational characterization of the NO adduct of substrate-bound Fe(II) cysteine dioxygenase: insights into the mechanism of O2 activation.Understanding and applying tyrosine biochemical diversity.Synthesis of amino acid cofactor in cysteine dioxygenase is regulated by substrate and represents a novel post-translational regulation of activity.Structure and function of atypically coordinated enzymatic mononuclear non-heme-Fe(II) centers.Probing the function of the Tyr-Cys cross-link in metalloenzymes by the genetic incorporation of 3-methylthiotyrosine.A novel variant of ferredoxin-dependent sulfite reductase having preferred substrate specificity for nitrite in the unicellular red alga Cyanidioschyzon merolae.Cleavage of a carbon-fluorine bond by an engineered cysteine dioxygenaseFunctional tuning and expanding of myoglobin by rational protein design
P2860
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P2860
Siroheme- and [Fe4-S4]-dependent NirA from Mycobacterium tuberculosis is a sulfite reductase with a covalent Cys-Tyr bond in the active site
description
2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2005
@ast
im Juli 2005 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2005/07/22)
@sk
vědecký článek publikovaný v roce 2005
@cs
wetenschappelijk artikel (gepubliceerd op 2005/07/22)
@nl
наукова стаття, опублікована в липні 2005
@uk
name
Siroheme- and [Fe4-S4]-depende ...... ys-Tyr bond in the active site
@ast
Siroheme- and [Fe4-S4]-depende ...... ys-Tyr bond in the active site
@en
Siroheme- and [Fe4-S4]-depende ...... ys-Tyr bond in the active site
@nl
type
label
Siroheme- and [Fe4-S4]-depende ...... ys-Tyr bond in the active site
@ast
Siroheme- and [Fe4-S4]-depende ...... ys-Tyr bond in the active site
@en
Siroheme- and [Fe4-S4]-depende ...... ys-Tyr bond in the active site
@nl
prefLabel
Siroheme- and [Fe4-S4]-depende ...... ys-Tyr bond in the active site
@ast
Siroheme- and [Fe4-S4]-depende ...... ys-Tyr bond in the active site
@en
Siroheme- and [Fe4-S4]-depende ...... ys-Tyr bond in the active site
@nl
P2860
P50
P356
P1476
Siroheme- and [Fe4-S4]-depende ...... ys-Tyr bond in the active site
@en
P2093
Robert Schnell
Ulf Hellman
P2860
P304
27319–27328
P356
10.1074/JBC.M502560200
P407
P577
2005-07-22T00:00:00Z