Studies on mechanism of double hydroxylation. I. Evidence for participation of NADH-cytochrome c reductase in the reaction of benzoate 1,2-dioxygenase (benzoate hydroxylase). |
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Authors: | M Yamaguchi T Yamauchi H Fujisawa |
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Institution: | Department of Biochemistry, Asahikawa Medical College, Asahikawa 071-01, Japan |
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Abstract: | Benzoate 1,2-dioxygenase system which catalyzed double hydroxylation of benzoate was obtained from and was shown to consist of two protein components (component A and B). Component A which was purified and was shown to be homogeneous upon sodium dodecyl sulfate disc gel electrophoresis retained high activity of NADH-cytochrome reductase. Both of benzoate 1,2-dioxygenase activity and NADH-cytochrome reductase activity were simultaneously induced by benzoate. Dichlorophenolindophenol which could serve as an electron acceptor of the NADH-cytochrome reductase inhibited the activity of benzoate 1,2-dioxygenase. These results suggest the possibility that NADH-cytochrome reductase activity is required for benzoate 1,2-dioxygenase. |
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Keywords: | DHB 1 2-dihydro-1 2-dihydroxybenzoic acid SDS sodium dodecyl sulfate DCIP 2 6-dichlorophenolindophenol DTT dithiothreitol |
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