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| Fumarate reductase respiratory complex | ||
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| Identifiers | ||
| Symbol | Fum_red_TM | |
| Pfam | PF02967 | |
| InterPro | IPR004224 | |
| SCOP | 1qla | |
| OPM family | 3 | |
| OPM protein | 2bs3 | |
| Available PDB structures: | ||
Fumarate reductase is the enzyme that converts fumarate to succinate, it is important in microbial metabolism as a means for anaerobic respiration.[1]
Succinate + acceptor <=> fumarate + reduced acceptor
In other words, fumarate reductase couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, in a reaction opposite to that catalysed by the related complex II of the respiratory chain (succinate dehydrogenase)[2].
Fumarate reductase complex includes three subunits. Subunit A contains the site of fumarate reduction and a covalently bound flavin adenine dinucleotide prosthetic group. Subunit B contains three iron-sulphur centres. The menaquinol-oxidizing subunit C consists of five membrane-spanning, primarily helical segments and binds two haem b molecules[2].
See also
References
- ^ Iverson TM, Luna-Chavez C, Cecchini G, Rees DC (1999). "Structure of the Escherichia coli fumarate reductase respiratory complex". Science 284 (5422): 1961–6. doi:. PMID 10373108.
- ^ a b Michel H, Lancaster CR, Kroger A, Auer M (1999). "Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution". Nature 402 (6760): 377–385. doi:. PMID 10586875.
External links
- Fumarate reductase / succinate dehydrogenase FAD-binding site in PROSITE
- MeSH Fumarate+Reductase
- EC 1.3.99.1
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This article includes text from the public domain Pfam and InterPro IPR004224
