Trimethylamine N-oxide reductase

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Overview

Trimethylamine N-oxide reductase (TOR or TMAO reductase, EC 1.7.2.3) is a microbial enzyme that can reduce trimethylamine N-oxide (TMAO) into trimethylamine (TMA), as part of the electron transport chain. The enzyme has been purified from E. coli and the photosynthetic bacteria Roseobacter denitrificans.[1] Both the R. denitrificans and E. coli enzymes can accept electrons from cytochromes.[2]

trimethylamine + 2 (ferricytochrome c)-subunit + H2O → trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+

Trimethylamine oxide is found at high concentrations in the tissues of fish, and the bacterial reduction of this compound to foul-smelling trimethylamine is a major process in the spoilage of fish.[3]

See also

References

  1. Arata H, Shimizu M, Takamiya K (1992). "Purification and properties of trimethylamine N-oxide reductase from aerobic photosynthetic bacterium Roseobacter denitrificans". J. Biochem. 112 (4): 470–5. PMID 1337081.
  2. Gon S, Giudici-Orticoni MT, Méjean 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 (15): 11545–51. PMID 11056172.
  3. Barrett EL, Kwan HS (1985). "Bacterial reduction of trimethylamine oxide". Annu. Rev. Microbiol. 39: 131–49. doi:10.1146/annurev.mi.39.100185.001023. PMID 3904597.

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