Differences in protonation of ubiquinone and menaquinone in fumarate reductase from Escherichia coli.
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A threonine on the active site loop controls transition state formation in Escherichia coli respiratory complex IIGeometric Restraint Drives On- and Off-pathway Catalysis by the Escherichia coli Menaquinol:Fumarate ReductasePerturbation of the Quinone-binding Site of Complex II Alters the Electronic Properties of the Proximal [3Fe-4S] Iron-Sulfur ClusterThiabendazole 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 ReductaseThe bacterial flagellar switch complex is getting more complex.The futalosine pathway played an important role in menaquinone biosynthesis during early prokaryote evolution.Heme biosynthesis is coupled to electron transport chains for energy generation.The quinone-binding and catalytic site of complex II.The quinone binding site in Escherichia coli succinate dehydrogenase is required for electron transfer to the heme b.A conserved lysine residue controls iron-sulfur cluster redox chemistry in Escherichia coli fumarate reductase.Investigating the thermostability of succinate: quinone oxidoreductase enzymes by direct electrochemistry at SWNTs-modified electrodes and FTIR spectroscopyStructural basis for malfunction in complex II.Catalytic mechanisms of complex II enzymes: a structural perspectiveMenaquinone as well as ubiquinone as a bound quinone crucial for catalytic activity and intramolecular electron transfer in Escherichia coli membrane-bound glucose dehydrogenase.Roles of bound quinone in the single subunit NADH-quinone oxidoreductase (Ndi1) from Saccharomyces cerevisiae.Amino acid residues interacting with both the bound quinone and coenzyme, pyrroloquinoline quinone, in Escherichia coli membrane-bound glucose dehydrogenase.The quinone-binding site of Acidithiobacillus ferrooxidans sulfide: quinone oxidoreductase controls both sulfide oxidation and quinone reduction.Diffusion-controlled generation of a proton-motive force across a biomembrane.
P2860
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P2860
Differences in protonation of ubiquinone and menaquinone in fumarate reductase from Escherichia coli.
description
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name
Differences in protonation of ...... ductase from Escherichia coli.
@en
Differences in protonation of ...... ductase from Escherichia coli.
@nl
type
label
Differences in protonation of ...... ductase from Escherichia coli.
@en
Differences in protonation of ...... ductase from Escherichia coli.
@nl
prefLabel
Differences in protonation of ...... ductase from Escherichia coli.
@en
Differences in protonation of ...... ductase from Escherichia coli.
@nl
P2093
P2860
P356
P1476
Differences in protonation of ...... ductase from Escherichia coli.
@en
P2093
Elena Maklashina
Gary Cecchini
Joel H Weiner
Violetta Kotlyar
Yelizaveta Sher
P2860
P304
26655-26664
P356
10.1074/JBC.M602938200
P407
P577
2006-07-08T00:00:00Z