Reduced nicotinamide adenine dinucleotide dependent reduction of fumarate coupled to membrane energization in a cytochrome deficient mutant of Escherichia coli K12.

Escherichia coli SASX76 does not form cytochromes unless supplemented with 5-aminolevulinic acid. It can grow anaerobically on glycerol and DL-glycerol 3-phosphate in the absence of 5-aminolevulinic acid with fumarate but not with nitrate as the terminal electron acceptor. Cytochrome-independent NADH oxidase, glycerol 3-phosphate- and NADH-fumarate oxidoreductase activities are induced by anaerobic growth on a glycerol-fumarate medium. The pathway of electrons from substrate to fumarate involves menaquinone. The NADH-fumarate oxidoreductase and cytochrome-independent NADH oxidase systems are inhibited by piericidin A, 2-heptyl-4-hydroxyquinoline N-oxide, and iron chelating agents. Both systems can energize the membrane particles as indicated by quenching of atebrin fluorescence.