PathWhiz

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

This pathway was propagated using PathWhiz - Pon, A. et al. Pathways with PathWhiz (2015) Nucleic Acids Res. 43(Web Server issue): W552–W559.

Propagated from PW001892

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

		Carbon dioxide
		Dimethyl sulfoxide
		Dimethylsulfide
		Electron
		Formic acid
		Hydrogen Ion
		Menaquinol 8
		menaquinone-8
		NAD
		NADH
		Water

Visualize Protein Data

		Anaerobic dimethyl sulfoxide reductase chain A
		Anaerobic dimethyl sulfoxide reductase chain B
		Anaerobic dimethyl sulfoxide reductase chain C
		Formate dehydrogenase, cytochrome b556(fdo) subunit
		Formate dehydrogenase-O iron-sulfur subunit
		Formate dehydrogenase-O major subunit
		Hydrogenase-1 large chain
		Hydrogenase-1 small chain
		NADH-quinone oxidoreductase subunit A
		NADH-quinone oxidoreductase subunit B
		NADH-quinone oxidoreductase subunit C/D
		NADH-quinone oxidoreductase subunit E
		NADH-quinone oxidoreductase subunit F
		NADH-quinone oxidoreductase subunit G
		NADH-quinone oxidoreductase subunit H
		NADH-quinone oxidoreductase subunit I
		NADH-quinone oxidoreductase subunit J
		NADH-quinone oxidoreductase subunit K
		NADH-quinone oxidoreductase subunit L
		NADH-quinone oxidoreductase subunit M
		NADH-quinone oxidoreductase subunit N
		Probable Ni/Fe-hydrogenase 1 B-type cytochrome subunit

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