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. 1969 Nov;100(2):708–714. doi: 10.1128/jb.100.2.708-714.1969

α-Hydroxyglutarate Oxidoreductase of Pseudomonas putida

Marvin S Reitz 1, Victor W Rodwell 1
PMCID: PMC250148  PMID: 5354943

Abstract

Oxidation of d-α-hydroxyglutarate to α-ketoglutarate is catalyzed by d-α-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 (Km = 4.0 × 10−4m for dl-α-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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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