Molecular mechanism of pyruvate‐ferredoxin oxidoreductases based on data obtained with the Clostridium pasteurianum enzyme

FEBS Letters

Gaillard, Jacques¹  Moulis, Jean-Marc²  Davasse, Valérie²  Meyer, Jacques² 

[1] CEA, Département de Recherche Fondamentale sur la Matière Condensée, SESAM/SCPM, 17 rue des Martyrs, 38054 Grenoble Cedex 9, France;CEA, Département de Biologie Moléculaire et Structurale, Laboratoire des Métalloprotéines, 17 rue des Martyrs, 38054 Grenoble Cedex 9, France

关键词: Pyruvate;    Electron paramagnetic resonance;    Electron transfer;    Iron-sulfur;    Ligand exchange;    Clostridium pasteurianum;    PFO;    pyruvate-ferredoxin oxidoreductase;    CoASH;    reduced coenzyme A;    DTT;    dithiothreitol;    TPP;    thiamine pyrophosphate;    PEG;    polyethylene glycol;    SDS-PAGE;    sodium dodecyl sulfate polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(96)00062-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Pyruvate-ferredoxin oxidoreductase oxidises pyruvate in many fermentative microorganisms. The enzyme from Clostridium pasteurianum is an air-sensitive homodimer of 2×120000 daltons, for which pyruvate is the best substrate found among several α-ketoacids. Each subunit contains eight iron atoms in two [4Fe-4S] clusters. Two distinct EPR signals, possibly associated with two ligand environments, arise from one of these clusters. Binding of pyruvate does not generate a radical. The results reported suggest a scheme for the electron flow in pyruvate ferredoxin oxidoreductases according to which the detailed reaction mechanism depends on the number (even or odd) of [4Fe-4S] clusters present in a given enzyme.

【 授权许可】

Unknown