Thioredoxin reduction dependent on α‐ketoacid oxidation by α‐ketoacid dehydrogenase complexes

FEBS Letters

Bunik, Victoria¹  Follmann, Hartmut² 

[1] A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russian Federation;Fachbereich Biologie-Chemie der Universität, D-34109 Kassel, Germany

关键词: Thioredoxin;    Thioredoxin reductase;    α-Ketoacid dehydrogenase complex;    Insulin;    Lipoate;    Mitochondrion;    CoA;    coenzyme A;    lip;    lipoate;    KGD;    α-ketoglutarate dehydrogenase;   

DOI  :  10.1016/0014-5793(93)80801-Z

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The pyruvate and α-ketoglutarate dehydrogenase complexes isolated from pig heart mitochondria promote the reduction of thioredoxin in the presence of their α-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 α-ketoacid oxidation provides a potential role for the specific thioredoxins previously identified by us in mitochondria.

【 授权许可】

Unknown