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Fumarate reductase

Fumarate reductase is the enzyme that converts fumarate to succinate, and is important in microbial metabolism as a part of anaerobic respiration. The catalyzed reaction is:

: succinate + acceptor ↔ fumarate + reduced acceptor

Fumarate reductases can be divided into three classes depending on the electron acceptor:

  • Fumarate reductase (NADH) ()

:The enzyme is monomeric and soluble, and can reduce fumarate independently from the electron transport chain. Fumarate reductase is absent from all mammalian cells.

  • Fumarate reductase (CoM/CoB) ():
  • : This enzyme is present in most methanogenic archea. It is cytoplasmic and uses coenzymes M and B as hydrogen donors.
  • Fumarate reductase (quinol) ()
  • : The membrane-bound enzyme covalently linked to flavin cofactors, which is composed of 3 or 4 subunits, transfers electrons from a quinol to fumarate. This class of enzyme is thus involved in the production of ATP by oxidative phosphorylation.

References

References

  1. Tielens, A.G.. (1998). "The electron transport chain in anearobically functioning eukaryotes". Biochim. Biophys. Acta.
  2. Camarasa. (2007). "Role in anaerobiosis of the isoenzymes for ''Saccharomyces cerevisiae'' fumarate reductase encoded by ''OSM1'' and ''FRDS1''". Yeast.
  3. Heim, S.. (1998-04-01). "Thiol:fumarate reductase (Tfr) from Methanobacterium thermoautotrophicum--identification of the catalytic sites for fumarate reduction and thiol oxidation". European Journal of Biochemistry.
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