Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site
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Alternative quinone substrates and inhibitors of human electron-transfer flavoprotein-ubiquinone oxidoreductaseA threonine on the active site loop controls transition state formation in Escherichia coli respiratory complex IICrystal Structure of Adenylylsulfate Reductase from Desulfovibrio gigas Suggests a Potential Self-Regulation Mechanism Involving the C Terminus of the -SubunitGeometric Restraint Drives On- and Off-pathway Catalysis by the Escherichia coli Menaquinol:Fumarate ReductaseStructure and Catalytic Mechanism of 3-Ketosteroid- 4-(5 )-dehydrogenase from Rhodococcus jostii RHA1 GenomeThiabendazole inhibits ubiquinone reduction activity of mitochondrial respiratory complex II via a water molecule mediated binding featurePlasticity of the Quinone-binding Site of the Complex II Homolog Quinol:Fumarate ReductaseStructural and computational analysis of the quinone-binding site of complex II (succinate-ubiquinone oxidoreductase): a mechanism of electron transfer and proton conduction during ubiquinone reductionTransmembrane protein alignment and fold recognition based on predicted topologyThe isolation and characterization of cytochrome c nitrite reductase subunits (NrfA and NrfH) from Desulfovibrio desulfuricans ATCC 27774. Re-evaluation of the spectroscopic data and redox properties.A tale of two ferredoxins: sequence similarity and structural differences.The quinone-binding and catalytic site of complex II.Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A.3-nitropropionic acid is a suicide inhibitor of mitochondrial respiration that, upon oxidation by complex II, forms a covalent adduct with a catalytic base arginine in the active site of the enzymeAtpenins, potent and specific inhibitors of mitochondrial complex II (succinate-ubiquinone oxidoreductase).The quinone binding site in Escherichia coli succinate dehydrogenase is required for electron transfer to the heme b.Crystallization of mitochondrial respiratory complex II from chicken heart: a membrane-protein complex diffracting to 2.0 AVariation in proton donor/acceptor pathways in succinate:quinone oxidoreductases.A conserved lysine residue controls iron-sulfur cluster redox chemistry in Escherichia coli fumarate reductase.Wolinella succinogenes quinol:fumarate reductase and its comparison to E. coli succinate:quinone reductase.Escherichia coli succinate dehydrogenase variant lacking the heme b.A limited universe of membrane protein families and folds.Catalytic mechanisms of complex II enzymes: a structural perspectiveRedox state of flavin adenine dinucleotide drives substrate binding and product release in Escherichia coli succinate dehydrogenase.Binding of the Covalent Flavin Assembly Factor to the Flavoprotein Subunit of Complex II.X-ray structure of the membrane-bound cytochrome c quinol dehydrogenase NrfH reveals novel haem coordinationStructural Insights into the Molecular Design of Flutolanil Derivatives Targeted for Fumarate Respiration of Parasite Mitochondria.Production, characterization and determination of the real catalytic properties of the putative 'succinate dehydrogenase' from Wolinella succinogenes.Essentiality of succinate dehydrogenase in Mycobacterium smegmatis and its role in the generation of the membrane potential under hypoxia.Hydrophobicity of transmembrane proteins: spatially profiling the distribution.HdrC2 from Acidithiobacillus ferrooxidans owns two iron-sulfur binding motifs but binds only one variable cluster between [4Fe-4S] and [3Fe-4S].The ubiquinone-binding site of the Saccharomyces cerevisiae succinate-ubiquinone oxidoreductase is a source of superoxide.Evidence for two different electron transfer pathways in the same enzyme, nitrate reductase A from Escherichia coli.Defining the Q-site of Escherichia coli fumarate reductase by site-directed mutagenesis, fluorescence quench titrations and EPR spectroscopy.An integrative computational model for large-scale identification of metalloproteins in microbial genomes: a focus on iron-sulfur cluster proteins.An Unsaturated Quinolone N-Oxide of Pseudomonas aeruginosa Modulates Growth and Virulence of Staphylococcus aureus.Differences in protonation of ubiquinone and menaquinone in fumarate reductase from Escherichia coli.New crystal forms of the integral membrane Escherichia coli quinol:fumarate reductase suggest that ligands control domain movement.Fumarate reductase and succinate oxidase activity of Escherichia coli complex II homologs are perturbed differently by mutation of the flavin binding domain.Crystal structure of an assembly intermediate of respiratory Complex II.
P2860
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P2860
Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site
description
2002 nî lūn-bûn
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2002 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Crystallographic studies of th ...... und to the quinol-binding site
@ast
Crystallographic studies of th ...... und to the quinol-binding site
@en
Crystallographic studies of th ...... und to the quinol-binding site
@nl
type
label
Crystallographic studies of th ...... und to the quinol-binding site
@ast
Crystallographic studies of th ...... und to the quinol-binding site
@en
Crystallographic studies of th ...... und to the quinol-binding site
@nl
prefLabel
Crystallographic studies of th ...... und to the quinol-binding site
@ast
Crystallographic studies of th ...... und to the quinol-binding site
@en
Crystallographic studies of th ...... und to the quinol-binding site
@nl
P2093
P2860
P356
P1476
Crystallographic studies of th ...... und to the quinol-binding site
@en
P2093
César Luna-Chavez
Douglas C Rees
Gary Cecchini
Laura R Croal
Tina M Iverson
P2860
P304
P356
10.1074/JBC.M200815200
P407
P577
2002-05-03T00:00:00Z