1.7.2.3	trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+	-	
1.7.2.3	trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+	-	
1.7.2.3	trimethylamine-N-oxide + electron donor	-	
1.7.2.3	trimethylamine-N-oxide + electron donor	anaerobic respiration	
1.7.2.3	trimethylamine-N-oxide + enzyme-MoIV	anaerobic respiration	
1.7.2.3	trimethylamine-N-oxide + electron donor	cytochrome 554,557 may be the physiological electron donor	
1.7.2.3	trimethylamine-N-oxide + electron donor	cytochrome c-556 may be the physiological electron donor	
1.7.2.3	trimethylamine N-oxide + NADH	enzyme is highly specific for trimethylamine oxide as alternative terminal electron acceptor	
1.7.2.3	additional information	enzyme is probably required for acquisition of molybdenum cofactor and translocation of the trimethylamine reductase TorA, EC 1.6.6.9, monomeric and dimeric enzyme forms bind to Tor A, the dimeric form binds more efficiently	
1.7.2.3	trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+	reaction mechanism