Molecular mechanism of pyruvate‐ferredoxin oxidoreductases based on data obtained with the Clostridium pasteurianum enzyme
- 19 February 1996
- journal article
- Published by Wiley in FEBS Letters
- Vol. 380 (3) , 287-290
- https://doi.org/10.1016/0014-5793(96)00062-2
Abstract
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.Keywords
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