Enhanced sensitivity of Streptomyces seoulensis to menadione by superfluous lipoamide dehydrogenase |
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Authors: | Youn H Kang S O |
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Affiliation: | Laboratory of Biophysics, Department of Microbiology, College of Natural Sciences, and Research Center for Molecular Microbiology, Seoul National University, Seoul, South Korea. |
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Abstract: | Lipoamide dehydrogenase from Streptomyces seoulensis could facilitate menadione-mediated cytochrome c reduction, which was mostly inhibited by superoxide dismutase, indicating the obvious involvement of superoxide radical anion. In this reaction, the production of superoxide radical anion occurred via a menadione semiquinone radical anion. When exposed to menadione, lipoamide dehydrogenase-overexpressing cells showed a much lower survival rate with a concomitant decrease of intracellular protein thiol than the wild-type strain. These results suggest that lipoamide dehydrogenase is a facilitating agent in the redox cycling of quinone compounds in vivo as well as in vitro and could inevitably increase the potential toxicity of the compounds. |
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