Bacterial NADH-quinone oxidoreductases: Iron-sulfur clusters and related problems
| Autor: | Melissa W. Calhoun, Thorsten Friedrich, Hanns Weiss, Yoshihiro Fukumori, Hans Leif, Steven W. Meinhardt, Tomoko Ohnishi, Vladimir D. Sled, Robert B. Gennis |
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| Rok vydání: | 1993 |
| Předmět: |
Iron-Sulfur Proteins
Physiology Iron–sulfur cluster Rhodobacter sphaeroides medicine.disease_cause Electron Transport chemistry.chemical_compound Bacterial Proteins Species Specificity Escherichia coli NAD(P)H Dehydrogenase (Quinone) medicine Rhodospirillaceae Paracoccus denitrificans biology Thermus thermophilus Membrane Proteins Cell Biology biology.organism_classification chemistry Biochemistry bacteria Protons Rhodospirillales Bacteria |
| Zdroj: | Journal of Bioenergetics and Biomembranes. 25:347-356 |
| ISSN: | 1573-6881 0145-479X |
| DOI: | 10.1007/bf00762460 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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