1.7.2.3 2-chloropyridine N-oxide + electron donor - Escherichia coli 2-chloropyridine + oxidized electron donor + H2O - ? 259482 1.7.2.3 3-hydroxypyridine N-oxide + electron donor - Escherichia coli 3-hydroxypyridine + oxidized electron donor + H2O - ? 259481 1.7.2.3 3-picoline N-oxide + electron donor - Escherichia coli 3-picoline + oxidized electron donor + H2O - ? 259485 1.7.2.3 4-chloropyridine N-oxide + electron donor - Escherichia coli 4-chloropyridine + oxidized electron donor + H2O - ? 259483 1.7.2.3 4-methylmorpholine N-oxide + electron donor - Shewanella massilia 4-methylmorpholine + oxidized electron donor + H2O - ? 259480 1.7.2.3 4-methylmorpholine N-oxide + electron donor good substrate Escherichia coli 4-methylmorpholine + oxidized electron donor + H2O - ? 259480 1.7.2.3 4-methylmorpholine N-oxide + electron donor wild-type enzyme, molybdenum-restored enzyme and tungsten-restored enzyme Escherichia coli 4-methylmorpholine + oxidized electron donor + H2O - ? 259480 1.7.2.3 4-methylmorpholine-N-oxide + (ferrocytochrome c)-subunit + H+ - Escherichia coli 4-methylmorpholine + (ferricytochrome c)-subunit + H2O - ? 287651 1.7.2.3 adenosine N-oxide + electron donor - Escherichia coli adenosine + H2O + oxidized electron donor - ? 259478 1.7.2.3 adenosine N-oxide + electron donor 40% relative activity to trimethylamine N-oxide with the periplasmic enzyme and 35% relative activity to trimethylamine N-oxide with the purified enzyme Shewanella sp. adenosine + H2O + oxidized electron donor - ? 259478 1.7.2.3 alpha-picoline N-oxide + electron donor - Escherichia coli alpha-picoline + H2O + oxidized electron donor - ? 259476 1.7.2.3 alpha-picoline N-oxide + electron donor wild-type enzyme, molybdenum-restored enzyme and tungsten-restored enzyme Escherichia coli alpha-picoline + H2O + oxidized electron donor - ? 259476 1.7.2.3 alpha-picoline N-oxide + electron donor alpha-picoline N-oxide is not an efficient substrate for the enzyme Shewanella massilia alpha-picoline + H2O + oxidized electron donor - ? 259476 1.7.2.3 biotin sulfoxide + (ferrocytochrome c)-subunit - Escherichia coli ? + (ferrocytochrome c)-subunit - ? 287648 1.7.2.3 bromate + (ferrocytochrome c)-subunit - Roseobacter denitrificans ? + (ferricytochrome c)-subunit - ? 287647 1.7.2.3 chlorate + electron donor - Salmonella enterica subsp. enterica serovar Typhimurium ? - ? 259479 1.7.2.3 chlorate + electron donor - Escherichia coli ? - ? 259479 1.7.2.3 chlorate + electron donor - Rhodobacter capsulatus ? - ? 259479 1.7.2.3 dimethylsulfoxide + (ferrocytochrome c)-subunit + 2 H+ - Escherichia coli dimethylsulfide + (ferricytochrome c)-subunit + H2O - ? 287649 1.7.2.3 dimethylsulfoxide + (ferrocytochrome c)-subunit + 2 H+ - Rhodobacter capsulatus dimethylsulfide + (ferricytochrome c)-subunit + H2O - ? 287649 1.7.2.3 dimethylsulfoxide + electron donor - Proteus vulgaris ? + oxidized electron donor + H2O - ? 259488 1.7.2.3 dimethylsulfoxide + electron donor - Shewanella massilia ? + oxidized electron donor + H2O - ? 259488 1.7.2.3 dimethylsulfoxide + electron donor 9% relative activity to trimethylamine N-oxide Rhodospirillum rubrum ? + oxidized electron donor + H2O - ? 259488 1.7.2.3 dimethylsulfoxide + electron donor tungsten-substituted enzyme Escherichia coli ? + oxidized electron donor + H2O - ? 259488 1.7.2.3 diphenylsulfoxide + electron donor - Shewanella massilia diphenylsulfide + oxidized electron donor + H2O - ? 259490 1.7.2.3 diphenylsulfoxide + electron donor tungsten-substituted enzyme Escherichia coli diphenylsulfide + oxidized electron donor + H2O - ? 259490 1.7.2.3 gamma-picoline N-oxide + electron donor - Escherichia coli gamma-picoline + H2O + oxidized electron donor - ? 259477 1.7.2.3 gamma-picoline N-oxide + electron donor wild-type enzyme, molybdenum-restored enzyme and tungsten-restored enzyme Escherichia coli gamma-picoline + H2O + oxidized electron donor - ? 259477 1.7.2.3 gamma-picoline N-oxide + electron donor 11% relative activity to trimethylamine N-oxide with the periplasmic enzyme and 12% relative activity to trimethylamine N-oxide with the purified enzyme Shewanella sp. gamma-picoline + H2O + oxidized electron donor - ? 259477 1.7.2.3 hydroxylamine + (ferrocytochrome c)-subunit - Roseobacter denitrificans ? + (ferricytochrome c)-subunit - ? 287646 1.7.2.3 hydroxylamine N-oxide + electron donor - Escherichia coli hydroxylamine + H2O + oxidized electron donor - ? 259475 1.7.2.3 hydroxylamine N-oxide + electron donor wild-type enzyme, molybdenum-restored enzyme and tungsten-restored enzyme Escherichia coli hydroxylamine + H2O + oxidized electron donor - ? 259475 1.7.2.3 hydroxylamine N-oxide + electron donor 19% relative activity to trimethylamine N-oxide with the periplasmic enzyme and 3% relative activity to trimethylamine N-oxide with the purified enzyme Shewanella sp. hydroxylamine + H2O + oxidized electron donor - ? 259475 1.7.2.3 L-methionine sulfoxide + electron donor - Shewanella massilia L-methionine + oxidized electron donor + H2O - ? 259489 1.7.2.3 L-methionine sulfoxide + electron donor 26% relative activity to trimethylamine N-oxide Rhodospirillum rubrum L-methionine + oxidized electron donor + H2O - ? 259489 1.7.2.3 additional information other electron acceptors: nitrate and fumarate Alteromonas sp. ? - ? 89 1.7.2.3 additional information a single enzyme responsible for both trimethylamine N-oxide and dimethylsulfoxide reductase Rhodobacter capsulatus ? - ? 89 1.7.2.3 additional information a single enzyme responsible for both trimethylamine N-oxide and dimethylsulfoxide reductase Proteus vulgaris ? - ? 89 1.7.2.3 additional information nitrate does not act as electron acceptor Rhodospirillum rubrum ? - ? 89 1.7.2.3 additional information when FMN, FAD, cytochrome c, NADPH, NADH or ascorbate are substituted at equimolar concentration for benzyl viologen, none facilitates the oxidation of dithionite by the trimethylamine N-oxide Salmonella enterica subsp. enterica serovar Typhimurium ? - ? 89 1.7.2.3 additional information no activity with FADH2, NADH, NADPH and the reduced forms of methylene blue and N-methylphenazonium methosulphate Shewanella sp. ? - ? 89 1.7.2.3 additional information the enzyme has very slight activity with nitrate, but no activity with nitrite, sulfite or thiosulfate Salmonella enterica subsp. enterica serovar Typhimurium ? - ? 89 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 Shewanella massilia ? - ? 89 1.7.2.3 additional information regulator TorR and sensor TorS, encoded by genes torR and torS in the same operon as torA, are required for the trimethylamine oxide respiration pathway Shewanella oneidensis ? - ? 89 1.7.2.3 additional information the enzyme binds to the trimethylamine oxide reductase TorA apoenzyme, EC 1.6.6.9, recognizing a signal peptide, and allows TorA to bind the essential molybdenum cofactor for transport from the periplasm across the cytoplasmic membrane, TorD is not involved in the transport itself, TorD has a regulatory and controlling function on TorA assembly Escherichia coli ? - ? 89 1.7.2.3 additional information TorD chaperone is a chaperone of trimethylamine oxide reductase, EC 1.6.6.9, addition of the chaperone activates the TorA apoenzyme up to 4fold, allowing its maturation, in absence or presence of the TorA molybdenum cofactor, TorD modifies the TorA apoenzyme conformation in absence of the cofactor, probably making the apoenzyme competent for cofactor binding, binding study Escherichia coli ? - ? 89 1.7.2.3 additional information TorD is an essentially required chaperone for cofactor binding and enzyme maturation of the trimethylamine oxide reductase TorA, EC 1.6.6.9, in absence of TorD at 42°C, the TorA is poorly maturated and almost completely degraded, at elevated temperatures above 37°C TorD prevents the missfolding of TorA apoenzyme before molybdenum cofactor binding, temperature-dependent effect Escherichia coli ? - ? 89 1.7.2.3 additional information the enzyme performs trimethylamine oxide reduction during aerobiosis, in the absence of oxygen, Escherichia coli can use alternative exogenous electron acceptors, including trimethylamine oxide, to generate energy, regulation, overview Escherichia coli ? - ? 89 1.7.2.3 additional information the enzyme performs trimethylamine oxide reduction Escherichia coli ? - ? 89 1.7.2.3 additional information the TMAO reductase active site can exist in multiple forms, molecular modelling, overview Escherichia coli ? - ? 89 1.7.2.3 N,N-dimethyldodecylamine N-oxide + electron donor - Escherichia coli N,N-dimethyldodecylamine + H2O + oxidized electron donor - ? 259474 1.7.2.3 N,N-dimethyldodecylamine N-oxide + electron donor 63% relative activity to trimethylamine N-oxide with the periplasmic enzyme and 41% relative activity to trimethylamine N-oxide with the purified enzyme Shewanella sp. N,N-dimethyldodecylamine + H2O + oxidized electron donor - ? 259474 1.7.2.3 N,N-dimethyldodecylamine N-oxide + electron donor N,N-dimethyldodecylamine N-oxide is not an efficient substrate for the enzyme Shewanella massilia N,N-dimethyldodecylamine + H2O + oxidized electron donor - ? 259474 1.7.2.3 N,N-dimethylhexylamine N-oxide + electron donor - Escherichia coli N,N-dimethylhexylamine + oxidized electron donor + H2O - ? 259486 1.7.2.3 N-cyclohexyldimethylamine N-oxide + electron donor - Escherichia coli N-cyclohexyldimethylamine + oxidized electron donor + H2O - ? 259487 1.7.2.3 nicotinic acid N-oxide + (ferrocytochrome c)-subunit + H+ - Roseobacter denitrificans nicotinic acid + (ferricytochrome c)-subunit + H2O - ? 287644 1.7.2.3 nitrite + dibutylsulfoxide - Shewanella massilia ? - ? 453901 1.7.2.3 nitrite + DL-methionine sulfoxide - Shewanella massilia ? - ? 453900 1.7.2.3 picoline N-oxide + (ferrocytochrome c)-subunit + H+ - Roseobacter denitrificans picoline + (ferricytochrome c)-subunit + H2O - ? 287645 1.7.2.3 pyridine N-oxide + electron donor - Escherichia coli pyridine + oxidized electron donor + H2O - ? 259484 1.7.2.3 pyridine N-oxide + electron donor wild-type enzyme, molybdenum-restored enzyme and tungsten-restored enzyme Escherichia coli pyridine + oxidized electron donor + H2O - ? 259484 1.7.2.3 tetramethylene sulfoxide + (ferrocytochrome c)-subunit + H+ - Escherichia coli ? + (ferricytochrome c)-subunit - ? 287650 1.7.2.3 tetramethylene sulfoxide + electron donor tungsten-substituted enzyme Escherichia coli tetrahydrothiophene + oxidized electron donor + H2O - ? 259491 1.7.2.3 trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+ - Rhodobacter capsulatus trimethylamine + (ferricytochrome c)-subunit + H2O - ? 287643 1.7.2.3 trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+ - Shewanella massilia trimethylamine + (ferricytochrome c)-subunit + H2O - ? 287643 1.7.2.3 trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+ reaction mechanism Escherichia coli trimethylamine + (ferricytochrome c)-subunit + H2O - ? 287643 1.7.2.3 trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+ enzyme forms a functional association with cytochrome c-556 Rhodobacter capsulatus trimethylamine + (ferricytochrome c)-subunit + H2O - ? 287643 1.7.2.3 trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+ cytochrome c2, cytochrome c552 and methylviologen can serve as electron donors Roseobacter denitrificans trimethylamine + (ferricytochrome c)-subunit + H2O - ? 287643 1.7.2.3 trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+ cytochrome c, cytochrome b-c1 and cytochrome c551 can act as electron donors Erythrobacter sp. trimethylamine + (ferricytochrome c)-subunit + H2O - ? 287643 1.7.2.3 trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+ trimethylamine N-oxide reductase and dimethyl sulfoxide reductase are identical enzymes Rhodobacter capsulatus trimethylamine + (ferricytochrome c)-subunit + H2O - ? 287643 1.7.2.3 trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+ reduction of trimethylamine N-oxide is catalyzed by at least 2 enzymes: trimethylamine N-oxide reductase and dimethyl sulfoxide reductase Escherichia coli trimethylamine + (ferricytochrome c)-subunit + H2O - ? 287643 1.7.2.3 trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+ cytochrome c, cytochrome b-c1 and cytochrome c551 can act as electron donors Erythrobacter sp. Och 114 trimethylamine + (ferricytochrome c)-subunit + H2O - ? 287643 1.7.2.3 trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+ - Shewanella massilia MR1 trimethylamine + (ferricytochrome c)-subunit + H2O - ? 287643 1.7.2.3 trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+ - Escherichia coli trimethylamine + 2 (ferricytochrome c)-subunit + H2O - ? 461707 1.7.2.3 trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+ - uncultured bacterium trimethylamine + 2 (ferricytochrome c)-subunit + H2O - ? 461707 1.7.2.3 trimethylamine N-oxide + benzyl viologen + H+ - Escherichia coli trimethylamine + oxidized benzyl viologen + H2O - ? 463071 1.7.2.3 trimethylamine N-oxide + electron donor - Shewanella massilia trimethylamine + oxidized electron donor + H2O - ? 259473 1.7.2.3 trimethylamine N-oxide + electron donor methyl viologen as electron donor Salmonella enterica subsp. enterica serovar Typhimurium trimethylamine + oxidized electron donor + H2O - ? 259473 1.7.2.3 trimethylamine N-oxide + electron donor methyl viologen as electron donor Escherichia coli trimethylamine + oxidized electron donor + H2O - ? 259473 1.7.2.3 trimethylamine N-oxide + electron donor methyl viologen as electron donor Proteus vulgaris trimethylamine + oxidized electron donor + H2O - ? 259473 1.7.2.3 trimethylamine N-oxide + electron donor methyl viologen as electron donor Alteromonas sp. trimethylamine + oxidized electron donor + H2O - ? 259473 1.7.2.3 trimethylamine N-oxide + electron donor methyl viologen as electron donor Shewanella sp. trimethylamine + oxidized electron donor + H2O - ? 259473 1.7.2.3 trimethylamine N-oxide + electron donor reduced methylene blue, reduced N-methylphenazonium methosulfate as electron donors Shewanella sp. trimethylamine + oxidized electron donor + H2O - ? 259473 1.7.2.3 trimethylamine N-oxide + electron donor benzyl viologen as electron donor Salmonella enterica subsp. enterica serovar Typhimurium trimethylamine + oxidized electron donor + H2O - ? 259473 1.7.2.3 trimethylamine N-oxide + electron donor benzyl viologen as electron donor Escherichia coli trimethylamine + oxidized electron donor + H2O - ? 259473 1.7.2.3 trimethylamine N-oxide + electron donor benzyl viologen as electron donor Rhodospirillum rubrum trimethylamine + oxidized electron donor + H2O - ? 259473 1.7.2.3 trimethylamine N-oxide + electron donor benzyl viologen as electron donor Shewanella sp. trimethylamine + oxidized electron donor + H2O - ? 259473 1.7.2.3 trimethylamine N-oxide + electron donor formate as electron donor Escherichia coli trimethylamine + oxidized electron donor + H2O - ? 259473 1.7.2.3 trimethylamine N-oxide + electron donor formate as electron donor Alteromonas sp. trimethylamine + oxidized electron donor + H2O - ? 259473 1.7.2.3 trimethylamine N-oxide + electron donor quinone as electron donor Escherichia coli trimethylamine + oxidized electron donor + H2O - ? 259473 1.7.2.3 trimethylamine N-oxide + electron donor wild-type enzyme, molybdenum-restored enzyme and tungsten-restored enzyme Escherichia coli trimethylamine + oxidized electron donor + H2O - ? 259473 1.7.2.3 trimethylamine N-oxide + electron donor vitamin K5 or FMN as electron donors Salmonella enterica subsp. enterica serovar Typhimurium trimethylamine + oxidized electron donor + H2O - ? 259473 1.7.2.3 trimethylamine N-oxide + electron donor the activity with 3.4 mM FMN is 17% of that obtained with 0.33 mM benzyl viologen Salmonella enterica subsp. enterica serovar Typhimurium trimethylamine + oxidized electron donor + H2O - ? 259473 1.7.2.3 trimethylamine N-oxide + electron donor NADH as electron donor Salmonella enterica subsp. enterica serovar Typhimurium trimethylamine + oxidized electron donor + H2O - ? 259473 1.7.2.3 trimethylamine N-oxide + electron donor NADH as electron donor Escherichia coli trimethylamine + oxidized electron donor + H2O - ? 259473 1.7.2.3 trimethylamine N-oxide + NADH enzyme is highly specific for trimethylamine oxide as alternative terminal electron acceptor Shewanella oneidensis NAD+ + trimethylamine + H2O - ? 371197 1.7.2.3 trimethylamine N-oxide + NADH enzyme is highly specific for trimethylamine oxide as electron acceptor Shewanella oneidensis NAD+ + trimethylamine + H2O trimethylamine is volatile ? 371197 1.7.2.3 trimethylamine N-oxide + oxidized benzyl viologen + 2 H+ - Vibrio fluvialis trimethylamine + reduced benzyl viologen + H2O - ? 463072 1.7.2.3 trimethylamine N-oxide + oxidized benzyl viologen + 2 H+ - Vibrio fluvialis QY27 trimethylamine + reduced benzyl viologen + H2O - ? 463072 1.7.2.3 trimethylamine N-oxide + oxidized benzyl viologen + 2 H+ - Vibrio fluvialis ATCC33809 trimethylamine + reduced benzyl viologen + H2O - ? 463072 1.7.2.3 trimethylamine N-oxide + oxidized benzyl viologen + H+ - Escherichia coli trimethylamine + reduced benzyl viologen + H2O - r 451733 1.7.2.3 trimethylamine N-oxide + oxidized methyl viologen + H+ - Escherichia coli trimethylamine + reduced methyl viologen + H2O - r 451734 1.7.2.3 trimethylamine-N-oxide + electron donor - Shewanella massilia trimethylamine + oxidized electron donor + H2O - ? 370183 1.7.2.3 trimethylamine-N-oxide + electron donor anaerobic respiration Escherichia coli trimethylamine + oxidized electron donor + H2O - ? 370183 1.7.2.3 trimethylamine-N-oxide + electron donor anaerobic respiration Aliivibrio fischeri ES114 trimethylamine + oxidized electron donor + H2O - ? 370183 1.7.2.3 trimethylamine-N-oxide + electron donor trimethylamine N-oxide acts as a terminal electron acceptor for an anaerobic respiratory chain which requires, in addition to a primary dehydrogenase, cytochromes and quinones Escherichia coli trimethylamine + oxidized electron donor + H2O - ? 370183 1.7.2.3 trimethylamine-N-oxide + electron donor trimethylamine N-oxide acts as a terminal electron acceptor for an anaerobic respiratory chain which requires, in addition to a primary dehydrogenase, cytochromes and quinones Alteromonas sp. trimethylamine + oxidized electron donor + H2O - ? 370183 1.7.2.3 trimethylamine-N-oxide + electron donor cytochrome 554,557 may be the physiological electron donor Escherichia coli trimethylamine + oxidized electron donor + H2O - ? 370183 1.7.2.3 trimethylamine-N-oxide + electron donor cytochrome c-556 may be the physiological electron donor Rhodobacter capsulatus trimethylamine + oxidized electron donor + H2O - ? 370183 1.7.2.3 trimethylamine-N-oxide + enzyme-MoIV anaerobic respiration Escherichia coli trimethylamine + enzyme-MoVI + H2O - ? 395007