来自普通脱硫弧菌（希登伯勒菌株）的NADH氧化酶的纯化、表征及性质及其与腺苷酰磷酸硫酸还原酶的偶联
Purification, characterization and properties of an NADH oxidase from Desulfovibrio vulgaris (Hildenborough) and its coupling to adenylyl phosphosulfate reductase.
作者信息
Chen L, Le Gall J, Xavier A V
机构信息
Department of Biochemistry, University of Georgia, Athens 30602.
出版信息
Biochem Biophys Res Commun. 1994 Sep 15;203(2):839-44. doi: 10.1006/bbrc.1994.2259.
An NADH oxidase was purified from Desulfovibrio vulgaris. This FMN-containing enzyme reacts with oxygen forming hydrogen peroxide with a specific activity of 0.21 mumoles.min-1.mg-1. The molecular weight of the protein was determined to be 65 kDa on 12.5% SDS/PAGE. It shows very low NADH: rubredoxin oxidoreductase activity specifically towards the rubredoxin from the same organism. However, adenylyl phosphosulfate reductase can be fully reduced by NADH with the purified enzyme, suggesting that NADH could be an electron donor for respiratory sulfate reduction.
从普通脱硫弧菌中纯化出一种NADH氧化酶。这种含黄素单核苷酸的酶与氧气反应生成过氧化氢，比活性为0.21微摩尔·分钟⁻¹·毫克⁻¹。在12.5%的SDS/聚丙烯酰胺凝胶电泳上测定该蛋白质的分子量为65千道尔顿。它对来自同一生物体的红素氧还蛋白显示出非常低的NADH：红素氧还蛋白氧化还原酶活性。然而，纯化后的酶可使腺苷酰磷酸硫酸还原酶被NADH完全还原，这表明NADH可能是呼吸性硫酸盐还原的电子供体。
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