Loading Pathway...
Error: Pathway image not found.
Hide
Pathway Description
Dimethyl Sulfoxide Electron Transfer
Escherichia coli
Metabolic Pathway
The pathway can start in various spots. First step in this case starts with NADH interacting with a menaquinone oxidoreductase resulting in the release of a NADH and a hydrogen Ion, at the same time in the inner membrane a menaquinone interacts with 2 electrons and 2 hydrogen ions thus releasing a menaquinol. This allows for 4 hydrogen ions to be transferred from the cytosol to the periplasmic space. The menaquinol then interacts with a dimethyl sulfoxide reductase resulting in the release of 2 hydrogen ion and 2 electrons. At the same time dimethyl sulfoxide and 2 hydrogen ions interact with the enzyme resulting in the release of a dimethyl sulfide and a water molecule, this reaction happening in the periplasmic space.
The second set of reactions starts with a hydrogen interacting with a menaquinone oxidoreductase resulting in the release of two electrons being released into the inner membrane which then react with with 2 hydrogen ion and a menaquinone to produce a menaquinol. This menaquinol then reacts with a trimethylamine N-oxide reductase following the same steps as mentioned before.
The third set of reactions starts with with formate interacting with a formate dehydrogenase-O resulting in a release of carbon dioxide and a hydrogen ion, this releases 2 electrons that interact with a menaquinone and two hydrogen ions. This releases a menaquinol which then reacts with a trimethylamine N-oxide reductase following the same steps as mentioned before
References
Dimethyl Sulfoxide Electron Transfer References
Abaibou H, Pommier J, Benoit S, Giordano G, Mandrand-Berthelot MA: Expression and characterization of the Escherichia coli fdo locus and a possible physiological role for aerobic formate dehydrogenase. J Bacteriol. 1995 Dec;177(24):7141-9.
Pubmed: 8522521
Berg BL, Stewart V: Structural genes for nitrate-inducible formate dehydrogenase in Escherichia coli K-12. Genetics. 1990 Aug;125(4):691-702.
Pubmed: 2168848
Bilous PT, Weiner JH: Proton translocation coupled to dimethyl sulfoxide reduction in anaerobically grown Escherichia coli HB101. J Bacteriol. 1985 Jul;163(1):369-75.
Pubmed: 2989249
Cotter PA, Gunsalus RP: Oxygen, nitrate, and molybdenum regulation of dmsABC gene expression in Escherichia coli. J Bacteriol. 1989 Jul;171(7):3817-23.
Pubmed: 2544558
Jormakka M, Tornroth S, Byrne B, Iwata S: Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science. 2002 Mar 8;295(5561):1863-8. doi: 10.1126/science.1068186.
Pubmed: 11884747
Simon J, van Spanning RJ, Richardson DJ: The organisation of proton motive and non-proton motive redox loops in prokaryotic respiratory systems. Biochim Biophys Acta. 2008 Dec;1777(12):1480-90. doi: 10.1016/j.bbabio.2008.09.008. Epub 2008 Sep 30.
Pubmed: 18930017
Tran QH, Bongaerts J, Vlad D, Unden G: Requirement for the proton-pumping NADH dehydrogenase I of Escherichia coli in respiration of NADH to fumarate and its bioenergetic implications. Eur J Biochem. 1997 Feb 15;244(1):155-60.
Pubmed: 9063459
Wang H, Gunsalus RP: Coordinate regulation of the Escherichia coli formate dehydrogenase fdnGHI and fdhF genes in response to nitrate, nitrite, and formate: roles for NarL and NarP. J Bacteriol. 2003 Sep;185(17):5076-85.
Pubmed: 12923080
Wissenbach U, Kroger A, Unden G: The specific functions of menaquinone and demethylmenaquinone in anaerobic respiration with fumarate, dimethylsulfoxide, trimethylamine N-oxide and nitrate by Escherichia coli. Arch Microbiol. 1990;154(1):60-6.
Pubmed: 2204318
Highlighted elements will appear in red.
Highlight Compounds
Highlight Proteins
Enter relative concentration values (without units). Elements will be highlighted in a color gradient where red = lowest concentration and green = highest concentration. For the best results, view the pathway in Black and White.
Visualize Compound Data
Visualize Protein Data
Settings