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J Bacteriol. 1969 November; 100(2): 708-714
Copyright © 1969 American Society for Microbiology. All Rights Reserved.

-Hydroxyglutarate Oxidoreductase of Pseudomonas putida

Department of Biochemistry, Purdue University, Lafayette, Indiana 47907

ABSTRACT

Oxidation of D--hydroxyglutarate to -ketoglutarate is catalyzed by D--hydroxyglutarate oxidoreductase, an inducible membrane-bound enzyme of the electron transport particle [ETP; a comminuted cytoplasmic membrane preparation with enzymic properties and chemical composition resembling beef heart mitochondrial ETP (1)] of Pseudomonas putida P2 (P2-ETP). Treatment of P2-ETP with a nonionic detergent yields a preparation with the sedimentation characteristics of a soluble enzyme, but which retains an intact electron transport chain. Oxygen acts solely as a terminal electron acceptor and may be replaced by ferricyanide, 2,6-dichlorophenol indophenol, or mammalian cytochrome c. The oxidoreductase is specific for the D-isomer (K_m = 4.0 x 10^–4M for DL--hydroxyglutarate) and is distinct both from L- and D-malate dehydrogenases. Spectral studies suggest that the carrier sequence is substrate flavine or nonheme iron cyt b [cyt c] oxygen.