Bacterial NADH-quinone oxidoreductases: iron-sulfur clusters and related problems.
Many bacteria contain proton-translocating membrane-bound NADH-quinone oxidoreductases (NDH-1), which demonstrate significant genetic, spectral, and kinetic similarity with their mitochondrial counterparts. This review is devoted to the comparative aspects of the iron-sulfur cluster composition of NDH-1 from the most well-studied bacterial systems to date.: Paracoccus denitrificans, Rhodobacter sphaeroides, Escherichia coli, and Thermus thermophilus. These bacterial systems provide useful models for the study of coupling Site I and contain all the essential parts of the electron-transfer and proton-translocating machinery of their eukaryotic counterparts.
Sled
V D
VD
Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia 19104.
Friedrich
T
T
Leif
H
H
Weiss
H
H
Meinhardt
S W
SW
Fukumori
Y
Y
Calhoun
M W
MW
Gennis
R B
RB
Ohnishi
T
T
D001426:Bacterial Proteins / Q000737:chemistry*; D004579:Electron Transport; D004926:Escherichia coli / Q000201:enzymology; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D016660:NAD(P)H Dehydrogenase (Quinone) / Q000037:antagonists & inhibitors / Q000737:chemistry*; D010231:Paracoccus denitrificans / Q000201:enzymology; D011522:Protons; D012242:Rhodobacter sphaeroides / Q000201:enzymology; D013045:Species Specificity; D016963:Thermus thermophilus / Q000201:enzymology
D001426:Bacterial Proteins; D007506:Iron-Sulfur Proteins; D008565:Membrane Proteins; D011522:Protons; D016660:NAD(P)H Dehydrogenase (Quinone)