| Literature DB >> 1650556 |
L Grinblat1, C M Sreider, A O Stoppani.
Abstract
Redox-cycling of porcine heart lipoamide dehydrogenase in the presence of NADH and oxygen produced O2-. (NADH-oxidase activity) as demonstrated by (a) reduction of cytochrome c; (b) reduction of the Fe(III)-ADP complex; (c) lucigenin luminescence and (d) the inhibitory effect of superoxide dismutase. NAD+ and p-chloromercuribenzoate inhibited O2-. generation whereas arsenite enhanced it. Comparison of heart and yeast enzyme preparations revealed a close correlation between lipoamide reductase and NADH-oxidase activities. It is concluded that O2-. production is a molecular property of lipoamide dehydrogenase.Entities:
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Year: 1991 PMID： 1650556
Source DB: PubMed Journal: Biochem Int ISSN： 0158-5231