Bacterial reduction of trimethylamine oxide.

Trimethylamine oxide, which is found in relatively high concentrations in the tissues of marine animals, serves as an electron acceptor in the anaerobic metabolism of a number of bacteria associated primarily with three environments: the marine environment (e.g. Alteromonas and Vibrio), the brackish pond (nonsulfur photosynthetic bacteria), and animal intestines (Enterobacteriaceae). Its reduction to trimethylamine by such bacteria can constitute a major spoilage reaction during the storage of marine fish. In the Enterobacteriaceae, anaerobic respiration with TMAO has been shown to support oxidative phosphorylation. Electron transport to TMAO in these bacteria involves flavin nucleotides, menaquinones, both b- and c-type cytochromes, and a molybdoenzyme reductase. Formate, hydrogen, lactate, and glycerol all serve as electron donors for TMAO respiration. Electrophoretically distinct constitutive and TMAO-induced reductases are synthesized by both E. coli and S. typhimurium. Electron transport to TMAO is repressed both by air and by nitrate. A number of genes involved in TMAO respiration have been mapped, but the structural gene for the inducible TMAO reductase has not yet been firmly established. Oxidative phosphorylation is also supported by TMAO reduction in Alteromonas. In this organism, which is nonfermentative, TMAO respiration resembles aerobic respiration in that intermediates of the TCA cycle are excellent electron donors. Alteromonas exhibits a requirement for NaCl for growth on TMAO and certain electron donors. As in the Enterobacteriaceae, air and nitrate both interfere with TMAO reduction. The role of TMAO reduction in the anaerobic metabolism of nonsulfur purple bacteria has not yet been resolved; it is not clear if TMAO serves simply as an accessory oxidant for fermentation or if TMAO reduction is associated with energy-yielding membrane-bound electron transport. Some of the confusion regarding this bacterial group stems from the fact that much of the work to date has involved parallel studies of TMAO and dimethyl sulfoxide reduction, and it is not yet known whether the two compounds are reduced by the same enzyme. Although our understanding of bacterial TMAO reduction lags far behind our knowledge of bacterial nitrate reduction, it is unlikely that this will always be the case.(ABSTRACT TRUNCATED AT 400 WORDS)