Bacterial NADH-quinone oxidoreductases: iron-sulfur clusters and related problems.
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Natural substances (acetogenins) from the family Annonaceae are powerful inhibitors of mitochondrial NADH dehydrogenase (Complex I)Towards the molecular mechanism of respiratory complex I.Proton pumping by NADH:ubiquinone oxidoreductase. A redox driven conformational change mechanism?NADH/NAD+ interaction with NADH: ubiquinone oxidoreductase (complex I).Were there any "misassignments" among iron-sulfur clusters N4, N5 and N6b in NADH-quinone oxidoreductase (complex I)?Mechanism of H2S Oxidation by the Dissimilatory Perchlorate-Reducing Microorganism Azospira suillum PSCharacterization of the iron-sulfur cluster coordinated by a cysteine cluster motif (CXXCXXXCX27C) in the Nqo3 subunit in the proton-translocating NADH-quinone oxidoreductase (NDH-1) of Thermus thermophilus HB-8.Noncoupled NADH:ubiquinone oxidoreductase of Azotobacter vinelandii is required for diazotrophic growth at high oxygen concentrations.Reversible dissociation of flavin mononucleotide from the mammalian membrane-bound NADH: ubiquinone oxidoreductase (complex I).H+/e- stoichiometry for NADH dehydrogenase I and dimethyl sulfoxide reductase in anaerobically grown Escherichia coli cells.Iron-sulfur cluster N5 is coordinated by an HXXXCXXCXXXXXC motif in the NuoG subunit of Escherichia coli NADH:quinone oxidoreductase (complex I).Uncoupling of substrate-level phosphorylation in Escherichia coli during glucose-limited growth.Allosteric nucleotide-binding site in the mitochondrial NADH:ubiquinone oxidoreductase (respiratory complex I).The proton-translocating NADH-quinone oxidoreductase (NDH-1) of thermophilic bacterium Thermus thermophilus HB-8. Complete DNA sequence of the gene cluster and thermostable properties of the expressed NQO2 subunit.Catalytic activity of NADH-ubiquinone oxidoreductase (complex I) in intact mitochondria. evidence for the slow active/inactive transition.Characterization of cluster N5 as a fast-relaxing [4Fe-4S] cluster in the Nqo3 subunit of the proton-translocating NADH-ubiquinone oxidoreductase from Paracoccus denitrificans.Iron-sulfur cluster N2 of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is located on subunit NuoB.Histidine 129 in the 75-kDa subunit of mitochondrial complex I from Yarrowia lipolytica is not a ligand for [Fe4S4] cluster N5 but is required for catalytic activity.Mitochondrial NADH-ubiquinone oxidoreductase (Complex I). Effect of substrates on the fragmentation of subunits by trypsin.Genetic inactivation of the H(+)-translocating NADH:ubiquinone oxidoreductase of Paracoccus denitrificans is facilitated by insertion of the ndh gene from Escherichia coli.Energy-dependent Complex I-associated ubisemiquinones in submitochondrial particles.On the function of the various quinone species in Escherichia coli.Studies on the proton-translocating NADH:ubiquinone oxidoreductases of mitochondria and Escherichia coli using the inhibitor 1,10-phenanthroline.The Redox-Bohr Group Associated with Iron-Sulfur Cluster N2 of Complex I
P2860
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P2860
Bacterial NADH-quinone oxidoreductases: iron-sulfur clusters and related problems.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh
1993年學術文章
@zh-hant
name
Bacterial NADH-quinone oxidoreductases: iron-sulfur clusters and related problems.
@en
type
label
Bacterial NADH-quinone oxidoreductases: iron-sulfur clusters and related problems.
@en
prefLabel
Bacterial NADH-quinone oxidoreductases: iron-sulfur clusters and related problems.
@en
P2093
P356
P1476
Bacterial NADH-quinone oxidoreductases: iron-sulfur clusters and related problems.
@en
P2093
M W Calhoun
R B Gennis
S W Meinhardt
T Friedrich
Y Fukumori
P2888
P304
P356
10.1007/BF00762460
P577
1993-08-01T00:00:00Z