Trimethylamine N-oxide (TMAO) reductase activity in chlorate-resistant or respiration-deficient mutants of<i>Escherichia coli</i>

Cox, John C.; Knight, R. C.

doi:10.1111/j.1574-6968.1981.tb07651.x

Cited by 21 publications

(1 citation statement)

References 8 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…When grown anaerobically with TMAO, these organisms synthesize a TMAO reductase (TOR) which links the reduction of TMAO to the oxidation of NADH or formate (6,11,17) or lactate (15) and which facilitates oxidative phosphorylation (7,13,15). Like nitrate reductase, TOR is absent in pleiotropic chlorate-resistant mutants defective in the molybdenum cofactor (3,7,15). In S. typhimurium, TOR also shares important features with thiosulfate reductase as mutants selected for the inability to produce trimethylamine from TMAO, even when chlorate sensitive, typically lack the ability to produce hydrogen sulfide from thiosulfate as well (4,8).…”

mentioning

confidence: 99%

Purification and properties of trimethylamine oxide reductase from Salmonella typhimurium

Kwan¹,

Barrett²

1983

J Bacteriol

View full text Add to dashboard Cite

The major inducible trimethylamine oxide reductase was purified from Salmonella typhimurium LT2. The molecular weights of the native enzyme were estimated to be 332,000 by gel filtration and 170,000 by nondenaturing disc gel electrophoresis. In sodium dodecyl sulfate-gel electrophoresis, the enzyme formed a single band of molecular weight 84,000. The isoelectric point was 4.28. Maximum activity was at pH 5.65 and 45°C. Reduced flavin mononucleotide, but not reduced flavin adenine dinucleotide, served as an electron donor. The Km for trimethylamine oxide was 0.89 mM and V.., was 1,450 U/mg of protein. The enzyme reduced chlorate with a Km of 2.2 mM and a Vm,, of 350 U/mg of protein.

show abstract