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Molecular mechanism of pyruvate‐ferredoxin oxidoreductases based on data obtained with the Clostridium pasteurianum enzyme
Author(s) -
Moulis Jean-Marc,
Davasse Valérie,
Meyer Jacques,
Gaillard Jacques
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00062-2
Subject(s) - ferredoxin , enzyme , chemistry , clostridium , mechanism (biology) , biochemistry , pyruvate decarboxylation , pyruvate dehydrogenase complex , biology , bacteria , physics , genetics , quantum mechanics
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.