Biophysical and biochemical studies of bacterial NADH:quinone oxidoreductase (NDH-1)
| Autor: | Tomoko Ohnishi, V. D. Sled', N. I. Rudnitzky, B. W. Jacobson, Y. Fukumori, S. W. Meinhardt, M. W. Calhoun, R. B. Gennis, H. Leif, T. Friedrich, H. Weiss |
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| Rok vydání: | 1994 |
| Předmět: |
chemistry.chemical_classification
In situ Chemistry Pyridines Electron Spin Resonance Spectroscopy Energy coupling Rhodobacter sphaeroides Biochemistry Electron transfer Lactones Enzyme Oxidoreductase NADH quinone oxidoreductase Rotenone Escherichia coli Photosynthetic bacteria Quinone Reductases Furans Gene |
| Zdroj: | Biochemical Society transactions. 22(1) |
| ISSN: | 0300-5127 |
| Popis: | The mitochondrial NADH-Q oxidoreductase (Complex I) is the most complex among the major mitochondrial energy coupling enzymes. Complex I from bovine heart and Neurosporu crussu contains 41 (1) and >32 (2) distinct subunits, respectively. In contrast, bacterial NDH-1 were shown to contain only 14 subunits both in Parucoccus denilrifcans (3) and in Escherichiu coli based on their gene structure (4). Thus, the bacterial NDH-1 systems provide simpler models for studies of the Site I electron transfer and energy coupling mechanisms. Here we focus on our recent studies of the NDH-1, in situ and in vilro, of photosynthetic bacteria and of E. coli. |
| Databáze: | OpenAIRE |
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