Abstract
Using the NADH-CoQ reductase of Rhodobacter capsulatus as a model for the mitochondrial Complex I, we have for the first time isolated bacterial mutants resistant to piericidin-A, a classical inhibitor of the mitochondrial enzyme. Their sensitivity to other inhibitors directed towards the quinone binding domain of complex I gives direct genetic evidence for the existence of two inhibitor binding sites.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites
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Electron Transport Complex I
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Enzyme Inhibitors / pharmacology
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Furans / pharmacology
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Multienzyme Complexes / metabolism
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NADH, NADPH Oxidoreductases / antagonists & inhibitors
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NADH, NADPH Oxidoreductases / chemistry*
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NADH, NADPH Oxidoreductases / genetics
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NADH, NADPH Oxidoreductases / metabolism
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Pyridines / pharmacology
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Rhodobacter capsulatus
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Rotenone / pharmacology
Substances
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Enzyme Inhibitors
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Furans
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Multienzyme Complexes
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Pyridines
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Rotenone
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bullatacin
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piericidin A
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NADH oxidase
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NADH, NADPH Oxidoreductases
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Electron Transport Complex I