| Literature DB >> 8226716 |
V D Sled1, T Friedrich, H Leif, H Weiss, S W Meinhardt, Y Fukumori, M W Calhoun, R B Gennis, T Ohnishi.
Abstract
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.Entities:
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Year: 1993 PMID: 8226716 DOI: 10.1007/bf00762460
Source DB: PubMed Journal: J Bioenerg Biomembr ISSN: 0145-479X Impact factor: 2.945