Fumarate reductase
| Fumarate reductase respiratory complex | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of Quinol-Fumarate Reductase Flavoprotein Subunit A.[1] | |||||||||
| Identifiers | |||||||||
| Symbol | Fum_red_TM | ||||||||
| Pfam | PF01127 | ||||||||
| Pfam clan | CL0335 | ||||||||
| InterPro | IPR004224 | ||||||||
| SCOP | 1qla | ||||||||
| SUPERFAMILY | 1qla | ||||||||
| OPM superfamily | 3 | ||||||||
| OPM protein | 2bs3 | ||||||||
| |||||||||
| Fumarate reductase subunit C | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 quinol-fumarate reductase with menaquinol molecules | |||||||||
| Identifiers | |||||||||
| Symbol | Fumarate_red_C | ||||||||
| Pfam | PF02300 | ||||||||
| Pfam clan | CL0335 | ||||||||
| InterPro | IPR003510 | ||||||||
| SCOP | 1fum | ||||||||
| SUPERFAMILY | 1fum | ||||||||
| |||||||||
| Fumarate reductase subunit D | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 quinol-fumarate reductase with quinol inhibitor 2-[1-(4-chloro-phenyl)-ethyl]-4,6-dinitro-phenol | |||||||||
| Identifiers | |||||||||
| Symbol | Fumarate_red_D | ||||||||
| Pfam | PF02313 | ||||||||
| Pfam clan | CL0335 | ||||||||
| InterPro | IPR003418 | ||||||||
| SCOP | 1fum | ||||||||
| SUPERFAMILY | 1fum | ||||||||
| |||||||||
Fumarate reductase is the enzyme that converts fumarate to succinate, and is important in microbial metabolism as a part of anaerobic respiration.[2]
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).[3]
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.[3] The D subunit may be required to anchor the catalytic components of the fumarate reductase complex to the cytoplasmic membrane.
See also
References
- ↑ Lancaster CR, Sauer US, Gross R, et al. (December 2005). "Experimental support for the "E pathway hypothesis" of coupled transmembrane e- and H+ transfer in dihemic quinol:fumarate reductase". Proc. Natl. Acad. Sci. U.S.A. 102 (52): 18860–5. doi:10.1073/pnas.0509711102. PMC 1323215. PMID 16380425.
- ↑ 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:10.1126/science.284.5422.1961. PMID 10373108.
- ↑ 3.0 3.1 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:10.1038/46483. PMID 10586875.
External links
- Fumarate reductase / succinate dehydrogenase FAD-binding site in PROSITE
- Fumarate Reductase at the US National Library of Medicine Medical Subject Headings (MeSH)
- EC 1.3.99.1
| ||||||||||||||||||||
This article incorporates text from the public domain Pfam and InterPro IPR004224
This article incorporates text from the public domain Pfam and InterPro IPR003510
This article incorporates text from the public domain Pfam and InterPro IPR003418