Comparison of H_2O-Forming NADH Oxidase from Leuconostoc mesenteroides subsp. mesenteroides NRIC 1541^T and H_2O_2-Forming NADH Oxidase from Sporolactobacillus inulinus NRIC 1133^T
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概要
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H_2O-forming NADH oxidase from Leuconostoc mesenteroides subsp. mesenteroides NRIC 1541^T and H_2O_2-forming NADH oxidase from Sporolactobacillus inulinus NRIC 1133^T were purified to electrophoretic homogeneity. These enzymes exhibited the absorption spectrum typical of a flavoprotein, and their activities were inhibited by inhibitors of the flavoprotein enzyme such as quinine and quinacrine. In addition, cofactors of the above-mentioned enzymes were identified as FAD. L. mesenteroides subsp. mesenteroides NADH oxidase catalyzed the reduction of oxygen to water with β-NADH as the substrate, while S. inulinus NADH oxidase catalyzed the reduction of oxygen to hydrogen peroxide. In addition, L. mesenteroides subsp. mesenteroides NADH oxidase activity was slightly enhanced by the addition of FAD to the reaction mixture whereas S. inulinus NADH oxidase activity was markedly enhanced. In the absence of free FAD, neither enzyme catalyzed electron transfer from β-NADH to hydrogen peroxide. In the presence FAD, S. inulinus NADH oxidase catalyzed electron transfer from β-NADH to hydrogen peroxide, but L. mesenteroides subsp. mesenteroides NADH oxidase did not. This finding suggests that S. inulinus NADH oxidase has an NADH peroxidase activity.L. mesenteroides subsp. mesenteroides contains NADH oxidase and NADH peroxidase, and an NADH oxidase/NADH peroxidase coupling system is thought to control the intracellular redox balance and protect this bacterium from hydrogen peroxide toxicity. By contrast, a single enzyme in S. inulinus exhibits both NADH oxidase and NADH peroxidase activity. Consequently, despite the fact that they lack the respiratory chain and catalase, these bacteria grow well under aerobic conditions. The N-terminal amino acid sequence of L. mesenteroides subsp. mesenteroides NADH oxidase is very similar to those of other H_2O-forming NADH oxidases. On the other hand, the N-terminal amino acid sequence of S. inulinus NADH oxidase is very similar to those of other H_2O_2-forming NADH oxidases.
- 社団法人日本生物工学会の論文
- 1996-12-25
著者
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UCHIMURA Tai
Department of Applied Biology and Chemistry, Faculty of Applied Bio-Science, Tokyo University of Agr
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Uchimura T
Tokyo University Of Agriculture
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Uchimura Tai
Department Of Agricultural Chemistry Tokyo University Of Agriculture
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Komagata K
Tokyo Univ. Agriculture Tokyo Jpn
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Komagata Kazuo
Department Of Agricultural Chemistry Tokyo University Of Agriculture
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Uchimura Tai
Tokyo University Of Agriculture
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SAKAMOTO MITSUO
Department of Agricultural Chemistry, Tokyo University of Agriculture
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Sakamoto M
Faculty Of Information Sciences Hiroshima City University
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Sakamoto Mitsuo
Department Of Agricultural Chemistry Tokyo University Of Agriculture
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