A novel, enzymatically active conformation of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I).
about
Structural organization of mitochondrial human complex I: role of the ND4 and ND5 mitochondria-encoded subunits and interaction with prohibitinTowards the molecular mechanism of respiratory complex I.Sodium ion cycling mediates energy coupling between complex I and ATP synthase.Proton pumping by NADH:ubiquinone oxidoreductase. A redox driven conformational change mechanism?Specific modification of a Na+ binding site in NADH:quinone oxidoreductase from Klebsiella pneumoniae with dicyclohexylcarbodiimideSynthesis and characterization of new piperazine-type inhibitors for mitochondrial NADH-ubiquinone oxidoreductase (complex I).The structure of eukaryotic and prokaryotic complex I.Mitochondrial threshold effects.Architecture of complex I and its implications for electron transfer and proton pumping.Characterization of the Nqo5 subunit of bacterial complex I in the isolated state.Substrate-induced conformational change in bacterial complex I.The three-dimensional structure of complex I from Yarrowia lipolytica: a highly dynamic enzyme.Direct localization of the 51 and 24 kDa subunits of mitochondrial complex I by three-dimensional difference imaging.Effect of monovalent cations on the kinetics of hypoxic conformational change of mitochondrial complex I.The respiratory complex I (NDH I) from Klebsiella pneumoniae, a sodium pump.Involvement of tyrosines 114 and 139 of subunit NuoB in the proton pathway around cluster N2 in Escherichia coli NADH:ubiquinone oxidoreductase.A role for native lipids in the stabilization and two-dimensional crystallization of the Escherichia coli NADH-ubiquinone oxidoreductase (complex I).The ubiquinone-binding site in NADH:ubiquinone oxidoreductase from Escherichia coli.The C-terminally truncated NuoL subunit (ND5 homologue) of the Na+-dependent complex I from Escherichia coli transports Na+.Functional implications from an unexpected position of the 49-kDa subunit of NADH:ubiquinone oxidoreductase.The location of NuoL and NuoM subunits in the membrane domain of the Escherichia coli complex I: implications for the mechanism of proton pumping.Internal architecture of mitochondrial complex I from Arabidopsis thaliana.EXAFS reveals a structural zinc binding site in the bovine NADH-Q oxidoreductase.Cryo-EM structure of respiratory complex I at workExploring the Ubiquinone Binding Cavity of Respiratory Complex ISuperoxide Radical Formation by Pure Complex I (NADH:Ubiquinone Oxidoreductase) fromYarrowia lipolytica
P2860
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P2860
A novel, enzymatically active conformation of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I).
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh-hant
name
A novel, enzymatically active ...... ne oxidoreductase (complex I).
@en
A novel, enzymatically active ...... ne oxidoreductase (complex I).
@nl
type
label
A novel, enzymatically active ...... ne oxidoreductase (complex I).
@en
A novel, enzymatically active ...... ne oxidoreductase (complex I).
@nl
prefLabel
A novel, enzymatically active ...... ne oxidoreductase (complex I).
@en
A novel, enzymatically active ...... ne oxidoreductase (complex I).
@nl
P2093
P2860
P356
P1476
A novel, enzymatically active ...... ne oxidoreductase (complex I).
@en
P2093
Dierk Scheide
Micaela Hesterberg
Thorsten Friedrich
P2860
P304
17970-17977
P356
10.1074/JBC.M112357200
P407
P577
2002-03-05T00:00:00Z