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Abstract
This chapter describes simple purification protocols for isolation of both the catalytic dimer and holoenzyme forms of fumarate reductase and a method for preparation of a membrane fraction enriched in inner membranes and fumarate reductase tubules. When the facultative anaerobe Escherichia coli is grown anaerobically on a glycerol-fumarate medium, a very simple electron-transport chain consisting of the anaerobic glycerol-3-phosphate dehydrogenase, a b -type cytochrome, and fumarate reductase is induced in the cytoplasmic membrane. This chain allows the organism to grow in the absence of oxygen on a nonfermentable carbon source. Fumarate serves as the terminal electron acceptor and is reduced to succinate by fumarate reductase. Fumarate reductase is an intrinsic membrane enzyme with the catalytic site exposed to the cytoplasm, and is composed of four nonidentical subunits. The chapter also outlines the method for the purification of the fumarate reductase holoenzyme.
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