Trimethylamine-N-oxide reductase (cytochrome c)

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In enzymology, a trimethylamine-N-oxide reductase (cytochrome c) (EC 1.7.2.3) is an enzyme that catalyzes the chemical reaction

trimethylamine + 2 (ferricytochrome c)-subunit + H₂O $\rightleftharpoons$ trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H⁺

The 3 substrates of this enzyme are trimethylamine, (ferricytochrome c)-subunit, and H₂O, whereas its 3 products are trimethylamine N-oxide, (ferrocytochrome c)-subunit, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with a cytochrome as acceptor. The systematic name of this enzyme class is trimethylamine:cytochrome c oxidoreductase. Other names in common use include TMAO reductase, and TOR. This enzyme participates in two-component system - general.

[edit] References

IUBMB entry for 1.7.2.3
BRENDA references for 1.7.2.3 (Recommended.)
PubMed references for 1.7.2.3
PubMed Central references for 1.7.2.3
Google Scholar references for 1.7.2.3
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Knablein J, Dobbek H, Ehlert S, Schneider F (1997). "Isolation, cloning, sequence analysis and X-ray structure of dimethyl sulfoxide/trimethylamine N-oxide reductase from Rhodobacter capsulatus". Biol. Chem. 378: 293–302. PMID 9165084.
Czjzek M, Dos Santos JP, Pommier J, Giordano G, Mejean V, Haser R (1998). "Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanella massilia at 2.5 A resolution". J. Mol. Biol. 284: 435–47. doi:10.1006/jmbi.1998.2156. PMID 9813128.
Gon S, Giudici-Orticoni MT, Mejean V, Iobbi-Nivol C (2001). "Electron transfer and binding of the c-type cytochrome TorC to the trimethylamine N-oxide reductase in Escherichia coli". J. Biol. Chem. 276: 11545–51. doi:10.1074/jbc.M008875200. PMID 11056172.