A sodium-stimulated membrane-bound fumarate reductase system in Bacteroides amylophilus.
Membrane vesicles derived from whole cells of the strictly anaerobic rumen bacterium Bacteroides amylophilus exhibited fumarate reductase activity with NADH, FADH2, FMNH2, or reduced viologens as electron donors. The fumarate reductase system is most likely localized on the cytoplasmic side of the plasma membrane. Cytochromes and menaquinone were not detectable. The NADH-dependent activity was inactivated by oxygen, an endogenous protease, and by irradiation at 254 nm. The electron transport inhibitor HpHOQnO and Zn2+ were identified as strong inhibitors of the fumarate reductase reaction. Two types of functional SH-groups might be operative in this system as probed by ClHgSO3H. The oxidation of NADH by fumarate was stimulated by low concentrations of Na+. Concentrations of Na+ in the range of 4 to 30 mM had a pronounced influence on growth rate and cell yield of B. amylophilus. In the presence of 1 mM NaCl growth was observed only after a lag-period of 15 h.
D001439:Bacteroides / Q000187:drug effects / Q000201:enzymology* / Q000254:growth & development; D002462:Cell Membrane / Q000201:enzymology; D004579:Electron Transport; D004789:Enzyme Activation; D007700:Kinetics; D010088:Oxidoreductases / Q000378:metabolism*; D044925:Oxidoreductases Acting on CH-CH Group Donors; D012964:Sodium / Q000494:pharmacology
D012964:Sodium; D010088:Oxidoreductases; D044925:Oxidoreductases Acting on CH-CH Group Donors; C020155:fumarate reductase (NADH)