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discounted EARLY registration ends Dec 31, 2014
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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Escherichia coli K-12 substr. MG1655 Pathway: NADH to dimethyl sulfoxide electron transfer

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

Locations of Mapped Genes:

Genetic Regulation Schematic: ?

Superclasses: Generation of Precursor Metabolites and Energy Electron Transfer
Generation of Precursor Metabolites and Energy Respiration Anaerobic Respiration

Summary:
In the respiratory chain formed by NADH dehydrogenase I (NDH-1) and dimethyl sulfoxide (DMSO) reductase the transfer of electrons from NADH to DMSO is coupled to the generation of a proton-motive force across the cytoplasmic membrane.

Two electrons are transferred from the NADH oxidation site to the DMSO reduction site by a menaquinone pool. The number of protons pumped across the membrane by NDH-1 is currently unknown [Yagi03] however the H+/e- ratio for NDH-1 is at least 1.5 [Bogachev96]. DMSO reductase does not catalyse vectorial proton translocation however the reduction of the DMSO and many other amine-N-oxides and methyl-sulfoxides, including trimethylamine N-oxide (TMAO), contributes two protons to the proton-motive force.

DMSO reductase is functionally similar to the TMAO reductases but genetically distinct [Bilous88]. This enzyme functions under anaerobic conditions and in the absence of nitrate (a preferred electron acceptor) [Cotter89]. DMSO is the preferred substrate for this enzyme [Weiner88].

Credits:
Created 12-Aug-2008 by Nolan L , Macquarie University


References

Bilous88: Bilous PT, Weiner JH (1988). "Molecular cloning and expression of the Escherichia coli dimethyl sulfoxide reductase operon." J Bacteriol 170(4);1511-8. PMID: 2832366

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

Cotter89: Cotter PA, Gunsalus RP (1989). "Oxygen, nitrate, and molybdenum regulation of dmsABC gene expression in Escherichia coli." J Bacteriol 171(7);3817-23. PMID: 2544558

Weiner88: Weiner JH, MacIsaac DP, Bishop RE, Bilous PT (1988). "Purification and properties of Escherichia coli dimethyl sulfoxide reductase, an iron-sulfur molybdoenzyme with broad substrate specificity." J Bacteriol 1988;170(4);1505-10. PMID: 3280546

Yagi03: Yagi T, Matsuno-Yagi A (2003). "The proton-translocating NADH-quinone oxidoreductase in the respiratory chain: the secret unlocked." Biochemistry 42(8);2266-74. PMID: 12600193

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

Allison11a: 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

Bairoch93: Bairoch A, Boeckmann B (1993). "The SWISS-PROT protein sequence data bank, recent developments." Nucleic Acids Res. 21:3093-3096. PMID: 8332529

Baranova07: 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

Baranova07a: 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

Belevich07: 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

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

Bilous88a: Bilous PT, Cole ST, Anderson WF, Weiner JH (1988). "Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli." Mol Microbiol 2(6);785-95. PMID: 3062312

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." http://www.brenda-enzymes.org.

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, Gennis RB (1993). "Demonstration of separate genetic loci encoding distinct membrane-bound respiratory NADH dehydrogenases in Escherichia coli." J Bacteriol 1993;175(10);3013-9. PMID: 8387992

Calhoun93a: 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
Page generated by SRI International Pathway Tools version 18.5 on Fri Nov 21, 2014, BIOCYC14B.