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 | ||||||||||
| SCOP2 | 1qla / SCOPe / SUPFAM | ||||||||||
| OPM superfamily | 3 | ||||||||||
| OPM protein | 2bs3 | ||||||||||
| CDD | cd03494 | ||||||||||
| |||||||||||
| Fumarate reductase subunit C | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 quinol-fumarate reductase with menaquinol molecules | |||||||||
| Identifiers | |||||||||
| Symbol | Fumarate_red_C | ||||||||
| Pfam | PF02300 | ||||||||
| Pfam clan | CL0335 | ||||||||
| InterPro | IPR003510 | ||||||||
| SCOP2 | 1fum / SCOPe / SUPFAM | ||||||||
| CDD | cd00546 | ||||||||
| |||||||||
| 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 | ||||||||
| SCOP2 | 1fum / SCOPe / SUPFAM | ||||||||
| CDD | cd00547 | ||||||||
| |||||||||
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 four subunits.[4] 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ 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:10.1038/46483. PMID 10586875.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Iverson, T. M.; Luna-Chavez, C; Cecchini, G; Rees, D. C. (1999). "Structure of the Escherichia coli fumarate reductase respiratory complex". Science. 284 (5422): 1961–6. PMID 10373108.
External links
- Fumarate reductase / succinate dehydrogenase FAD-binding site in PROSITE
- Fumarate+Reductase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- EC 1.3.99.1