Isolation of succinate dehydrogenase from Desulfobulbus elongatus, a propionate oxidizing, sulfate reducing bacterium

FEBS Letters

LeGall, J.¹  Albagnac, G.²  Patil, D.S.¹  Samain, E.²  DerVartanian, D.V.¹ 

[1] Department of Biochemistry, School of Chemical Sciences, University of Georgia, Athens, GA 30602, USA;Institut National de la Recherche Agronomique, Station de Technologie Alimentaire, BP 39, F59651 Villeneuve d' Ascq, France

关键词: Succinate dehydrogenase;    EPR;    Succinate pathway;    Iron-sulfur center (Desulfobulbus elongatus);    FR;    fumarate reductase;    SDH;    succinate dehydrogenase;    DCPIP;    2;    6-dichlorophenol-indophenol;    PMS;    phenazine methosulfate;    HHOQnO;    2-heptyl-4-hydroxy-quinoline-N-oxide;    MK-S(H2);    menaquinone-5- with saturated isoprenoid side chain;    ClHgPhSO3H;    4-chloromeriphenysulfonate.;   

DOI  :  10.1016/0014-5793(87)80772-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Succinate dehydrogenase was purified from the particulate fraction of Desulfobulbus. The enzyme catalysed both fumarate reduction and succinate oxidation but the rate of fumarate reduction was 8-times less than that of succinate oxidation. Quantitative analysis showed the presence of 1 mol of covalently bound flavin and 1 mol of cytochrome b per mol of succinate dehydrogenase. The enzyme contained three subunits with molecular mass 68.5, 27.5 and 22 kDa. EPR spectroscopy indicated the presence of at least two iron sulfur clusters. 2-Heptyl-4-hydroxy-quinoline-N-oxide inhibited the electron-transfer between succinate dehydrogenase and a high redox potential cytochrome c ₃ from Desulfobulbus elongatus.

【 授权许可】

Unknown