Fumarate reductase is an enzyme that catalyzes the conversion of fumarate to succinate . It is an important enzyme for the metabolism of microorganisms, since it is involved in the process of anaerobic respiration [2] .
| Fumarate reductase respiratory complex | |
|---|---|
The structure of the quinol-fumarate reductase dimer [1] | |
| Identifiers | |
| Symbol | Fum_red_tm |
| Pfam | Pf01127 |
| Pfam clan | CL0335 |
| Interpro | IPR004224 |
| SCOP | 1qla |
| SUPERFAMILY | 1qla |
| OPM superfamily | 3 |
| OPM protein | 2bs3 |
| CDD | cd03494 |
| Available protein structures | |
| Pfam | the structure |
| PDB | RCSB PDB ; PDBe ; PDBj |
| PDBsum | 3D model |
- Succinate + acceptor ↔ fumarate + reduced acceptor
Fumarate reductase combines the reduction of fumarate to succinate with the oxidation of quinol to quinone , that is, it is the opposite reaction to that occurring under the action of complex II of the respiratory chain of electron transfer ( succinate dehydrogenase ) [3] . Structurally, this enzyme is similar to succinate dehydrogenase, but kinetically promotes the reverse reaction.
Fumarate reductase consists of four subunits [4] . Subunit A contains a fumarate reduction site and a covalently linked prosthetic group of flavin adenine dinucleotide . Subunit B contains three iron-sulfur centers. The menaquinol-oxidizing subunit C consists of five spiral-piercing membrane segments and binds two heme b molecules [3] . Subunit D is probably necessary for attachment of the complex components to the cytoplasmic membrane .
See also
- Succinate dehydrogenase
Notes
- ↑ Lancaster CR, Sauer US, Gross R. et al. Experimental support for the "E pathway hypothesis" of coupled transmembrane e- and H + transfer in dihemic quinol: fumarate reductase (English) // Proceedings of the National Academy of Sciences of the United States of America : journal. - 2005 .-- December ( vol. 102 , no. 52 ). - P. 18860-18865 . - DOI : 10.1073 / pnas.0509711102 . - PMID 16380425 .
- ↑ Iverson TM, Luna-Chavez C., Cecchini G., Rees DC Structure of the Escherichia coli fumarate reductase respiratory complex (Eng.) // Science: journal. - 1999. - Vol. 284 , no. 5422 . - P. 1961-1966 . - DOI : 10.1126 / science.284.5422.1961 . - PMID 10373108 .
- ↑ 1 2 Michel H., Lancaster CR, Kroger A., Auer M. Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution // English : journal. - 1999. - Vol. 402 , no. 6760 . - P. 377-385 . - DOI : 10.1038 / 46483 . - PMID 10586875 .
- ↑ Iverson TM , Luna-Chavez C. , Cecchini G. , Rees DC Structure of the Escherichia coli fumarate reductase respiratory complex. (English) // Science (New York, NY). - 1999. - Vol. 284, no. 5422 . - P. 1961-1966. - PMID 10373108 .