Escherichia coli K-12 substr. MG1655 Pathway: NADH to trimethylamine N-oxide electron transfer
Inferred from experiment

Pathway diagram: NADH to trimethylamine N-oxide electron transfer

If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Locations of Mapped Genes:

Schematic showing all replicons, marked with selected genes

Genetic Regulation Schematic

Genetic regulation schematic for NADH to trimethylamine N-oxide electron transfer

Superclasses: Generation of Precursor Metabolites and EnergyElectron Transfer
Generation of Precursor Metabolites and EnergyRespirationAnaerobic Respiration

In the anaerobic respiratory chain formed by NADH dehydrogenase I (NDH-1) and trimethylamine N-oxide (TMAO) reductase the transfer of electrons from NADH to TMAO is coupled to the generation of a proton-motive force across the cytoplasmic membrane [Cox80].

By analogy to the related enzyme from mitochondria, NDH-I is thought to function as a proton pump translocating 4H+ per NADH oxidised (2e-) [H+/e- = 2] however a lower ratio of 3H+/2e- has also been proposed [Bogachev96, Wikstrom12]. TMAO reductase does not contribute to proton potential and thus proton pumping by NDH-I is the only mechanism for proton motive force (PMF) generation in anaerobic NADH → TMAO respiration (see review by [Simon08]. Menaquinone (shown here) or demethylmenaquinone serves as the redox mediator during anaerobic respiration with TMAO [Wissenbach90, Wissenbach92].

In addition to the inducible TMAO reductase encoded by torCA (shown here), E. coli K-12 contains a second TMAO reductase encoded by torYZ. torYZ has low constitutive expression and is not induced by TMAO or dimethyl sulfoxide [Gon00]. TorAC is an inducible TMAO reductase and is expressed in both anaerobic and aerobic conditions [Ansaldi07]. The DMSO reductase, DmsABC, is also able to reduce TMAO.

Many early studies on anaerobic TMAO respiration were done using E. coli K-10 [Takagi81, Shimokawa79].

Reviews: [Barrett85, McCrindle05]

Created 12-Aug-2008 by Nolan L, Macquarie University
Revised 05-Nov-2014 by Mackie A, Macquarie University


Ansaldi07: Ansaldi M, Theraulaz L, Baraquet C, Panis G, Mejean V (2007). "Aerobic TMAO respiration in Escherichia coli." Mol Microbiol 66(2);484-94. PMID: 17850256

Barrett85: Barrett EL, Kwan HS (1985). "Bacterial reduction of trimethylamine oxide." Annu Rev Microbiol 1985;39;131-49. PMID: 3904597

Bogachev96: Bogachev AV, Murtazina RA, Skulachev VP (1996). "H+/e- stoichiometry for NADH dehydrogenase I and dimethyl sulfoxide reductase in anaerobically grown Escherichia coli cells." J Bacteriol 178(21);6233-7. PMID: 8892824

Cox80: Cox JC, Madigan MT, Favinger JL, Gest H (1980). "Redox mechanisms in "oxidant-dependent" hexose fermentation by Rhodopseudomonas capsulata." Arch Biochem Biophys 204(1);10-7. PMID: 7000002

Cox81a: Cox JC, Knight R (1981). "Trimethylamine N-oxide (TMAO) reductase activity in chlorate-resistant or respiration-deficient mutants of Escherichia coli." FEMS Microbiology Letters 12 249-252.

Gon00: Gon S, Patte JC, Mejean V, Iobbi-Nivol C (2000). "The torYZ (yecK bisZ) operon encodes a third respiratory trimethylamine N-oxide reductase in Escherichia coli." J Bacteriol 2000;182(20);5779-86. PMID: 11004177

McCrindle05: McCrindle SL, Kappler U, McEwan AG (2005). "Microbial dimethylsulfoxide and trimethylamine-N-oxide respiration." Adv Microb Physiol 50;147-98. PMID: 16221580

Shimokawa79: Shimokawa O, Ishimoto M (1979). "Purification and some properties of inducible tertiary amine N-oxide reductase from Escherichia coli." J Biochem (Tokyo) 1979;86(6);1709-17. PMID: 393699

Simon08: Simon J, van Spanning RJ, Richardson DJ (2008). "The organisation of proton motive and non-proton motive redox loops in prokaryotic respiratory systems." Biochim Biophys Acta 1777(12);1480-90. PMID: 18930017

Takagi81: Takagi M, Tsuchiya T, Ishimoto M (1981). "Proton translocation coupled to trimethylamine N-oxide reduction in anaerobically grown Escherichia coli." J Bacteriol 148(3);762-8. PMID: 7031034

Wikstrom12: Wikstrom M, Hummer G (2012). "Stoichiometry of proton translocation by respiratory complex I and its mechanistic implications." Proc Natl Acad Sci U S A 109(12);4431-6. PMID: 22392981

Wissenbach90: Wissenbach U, Kroger A, Unden G (1990). "The specific functions of menaquinone and demethylmenaquinone in anaerobic respiration with fumarate, dimethylsulfoxide, trimethylamine N-oxide and nitrate by Escherichia coli." Arch Microbiol 154(1);60-6. PMID: 2204318

Wissenbach92: Wissenbach U, Ternes D, Unden G (1992). "An Escherichia coli mutant containing only demethylmenaquinone, but no menaquinone: effects on fumarate, dimethylsulfoxide, trimethylamine N-oxide and nitrate respiration." Arch Microbiol 1992;158(1);68-73. PMID: 1444716

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

Al12: Al Mamun AA, Lombardo MJ, Shee C, Lisewski AM, Gonzalez C, Lin D, Nehring RB, Saint-Ruf C, Gibson JL, Frisch RL, Lichtarge O, Hastings PJ, Rosenberg SM (2012). "Identity and function of a large gene network underlying mutagenic repair of DNA breaks." Science 338(6112);1344-8. PMID: 23224554

Allison11: Allison KR, Brynildsen MP, Collins JJ (2011). "Metabolite-enabled eradication of bacterial persisters by aminoglycosides." Nature 473(7346);216-20. PMID: 21562562

Amarneh03: Amarneh B, Vik SB (2003). "Mutagenesis of subunit N of the Escherichia coli complex I. Identification of the initiation codon and the sensitivity of mutants to decylubiquinone." Biochemistry 42(17);4800-8. PMID: 12718520

Amarneh10: Amarneh B, Vik SB (2010). "Transmembrane topology of subunit N of complex I (NADH:ubiquinone oxidoreductase) from Escherichia coli." J Bioenerg Biomembr 42(6);511-6. PMID: 21120593

Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699

Auriol11: Auriol C, Bestel-Corre G, Claude JB, Soucaille P, Meynial-Salles I (2011). "Stress-induced evolution of Escherichia coli points to original concepts in respiratory cofactor selectivity." Proc Natl Acad Sci U S A 108(4);1278-83. PMID: 21205901

Baranova07: Baranova EA, Morgan DJ, Sazanov LA (2007). "Single particle analysis confirms distal location of subunits NuoL and NuoM in Escherichia coli complex I." J Struct Biol 159(2);238-42. PMID: 17360196

Baranova07a: Baranova EA, Holt PJ, Sazanov LA (2007). "Projection structure of the membrane domain of Escherichia coli respiratory complex I at 8 A resolution." J Mol Biol 366(1);140-54. PMID: 17157874

Belevich07a: Belevich G, Euro L, Wikstrom M, Verkhovskaya M (2007). "Role of the conserved arginine 274 and histidine 224 and 228 residues in the NuoCD subunit of complex I from Escherichia coli." Biochemistry 46(2);526-33. PMID: 17209562

Belevich11: Belevich G, Knuuti J, Verkhovsky MI, Wikstrom M, Verkhovskaya M (2011). "Probing the mechanistic role of the long α-helix in subunit L of respiratory Complex I from Escherichia coli by site-directed mutagenesis." Mol Microbiol 82(5);1086-95. PMID: 22060017

Belevich14: Belevich N, Belevich G, Verkhovskaya M (2014). "Real-time optical studies of respiratory Complex I turnover." Biochim Biophys Acta 1837(12);1973-1980. PMID: 25283488

Berrisford08: Berrisford JM, Thompson CJ, Sazanov LA (2008). "Chemical and NADH-induced, ROS-dependent, cross-linking between subunits of complex I from Escherichia coli and Thermus thermophilus." Biochemistry 47(39);10262-70. PMID: 18771280

Bongaerts95: Bongaerts J, Zoske S, Weidner U, Unden G (1995). "Transcriptional regulation of the proton translocating NADH dehydrogenase genes (nuoA-N) of Escherichia coli by electron acceptors, electron donors and gene regulators." Mol Microbiol 16(3);521-34. PMID: 7565112

Bottcher02: Bottcher B, Scheide D, Hesterberg M, Nagel-Steger L, Friedrich T (2002). "A novel, enzymatically active conformation of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)." J Biol Chem 277(20);17970-7. PMID: 11880370

Braun98: Braun M, Bungert S, Friedrich T (1998). "Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli." Biochemistry 37(7);1861-7. PMID: 9485311

BRENDA14: BRENDA team (2014). Imported from BRENDA version existing on Aug 2014.

Buc99: Buc J, Santini CL, Giordani R, Czjzek M, Wu LF, Giordano G (1999). "Enzymatic and physiological properties of the tungsten-substituted molybdenum TMAO reductase from Escherichia coli." Mol Microbiol 32(1);159-68. PMID: 10216869

Buchanan08: Buchanan G, Maillard J, Nabuurs SB, Richardson DJ, Palmer T, Sargent F (2008). "Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone." FEBS Lett 582(29);3979-84. PMID: 19013157

Bungert99: Bungert S, Krafft B, Schlesinger R, Friedrich T (1999). "One-step purification of the NADH dehydrogenase fragment of the Escherichia coli complex I by means of Strep-tag affinity chromatography." FEBS Lett 1999;460(2);207-11. PMID: 10544236

Calhoun93: Calhoun MW, Oden KL, Gennis RB, de Mattos MJ, Neijssel OM (1993). "Energetic efficiency of Escherichia coli: effects of mutations in components of the aerobic respiratory chain." J Bacteriol 175(10);3020-5. PMID: 8491720

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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