Reaction: succinate + a menaquinone = fumarate + a menaquinol
Other name(s): FRD; menaquinol-fumarate oxidoreductase; succinate dehydrogenase (menaquinone)
Systematic name: succinate:menaquinone oxidoreductase
Comments: The reaction is catalysed in the opposite direction. The enzyme is part of the anaerobic electron transfer chain of certain bacteria. It allows fumarate to serve as a terminal electron acceptor. The enzyme from Escherichia coli contains a catalytic domain and an anchor domain, each consisting of two subunits. One of the subunits of the catalytic domain contains a covalently-bound FAD cofactor and the fumarate binding site, and the other contains 3 iron-sulfur clusters. The anchor domain interacts with the menaquinone. The enzyme is closely related to EC 18.104.22.168 [succinate dehydrogenase (ubiquinone)].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
1. Iverson, T.M., Luna-Chavez, C., Cecchini, G. and Rees, D.C. Structure of the Escherichia coli fumarate reductase respiratory complex. Science 284 (1999) 1961-1966. [PMID: 10373108]
2. Cecchini, G., Schroder, I., Gunsalus, R.P. and Maklashina, E. Succinate dehydrogenase and fumarate reductase from Escherichia coli. Biochim. Biophys. Acta 1553 (2002) 140-157. [PMID: 11803023]
3. Iverson, T.M., Luna-Chavez, C., Croal, L.R., Cecchini, G. and Rees, D.C. Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site. J. Biol. Chem. 277 (2002) 16124-16130. [PMID: 11850430]