Bunik V, Follmann H
A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russian Federation.
FEBS Lett. 1993 Dec 27;336(2):197-200. doi: 10.1016/0014-5793(93)80801-z.
The pyruvate and alpha-ketoglutarate dehydrogenase complexes isolated from pig heart mitochondria promote the reduction of thioredoxin in the presence of their alpha-ketoacid substrates, coenzyme A, and free lipoate. Substrate-specific generation of reduced thioredoxin was established by two independent methods, viz. reduction of insulin and thioredoxin reductase-catalyzed NADPH formation. Dihydrolipoate accumulating in the absence of NAD+ is the likely intermediate. A redox function in alpha-ketoacid oxidation provides a potential role for the specific thioredoxins previously identified by us in mitochondria.
从猪心线粒体中分离出的丙酮酸和α-酮戊二酸脱氢酶复合物，在其α-酮酸底物、辅酶A和游离硫辛酸存在的情况下，能促进硫氧还蛋白的还原。通过两种独立的方法确定了还原型硫氧还蛋白的底物特异性生成，即胰岛素的还原和硫氧还蛋白还原酶催化的NADPH形成。在没有NAD⁺的情况下积累的二氢硫辛酸可能是中间产物。α-酮酸氧化中的氧化还原功能为我们之前在线粒体中鉴定出的特定硫氧还蛋白提供了潜在作用。
