| Structural highlights
Function
FCCA_SHEON Flavocytochrome that catalyzes the reduction of fumarate to succinate (PubMed:12196158, PubMed:12899636, PubMed:22458729). Is essential for fumarate respiration during anaerobic growth, acting as the terminal reductase (By similarity). Receives electrons from the membrane-bound tetraheme c-type cytochrome CymA (PubMed:12196158, PubMed:12899636, PubMed:19837833, PubMed:22458729). Under ferric iron-reducing conditions, can be part of an electron transport chain to ferric iron, by accepting electrons from CymA and transfering them to the c-type cytochrome MtrA (PubMed:19837833). Also plays an important role in the reduction of selenite to elemental selenium (PubMed:24435070). May act as a transient electron storage protein (PubMed:19837833).[UniProtKB:Q07WU7][1] [2] [3] [4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Fumarate respiration is one of the most widespread types of anaerobic respiration. The soluble fumarate reductase of Shewanella putrefaciens MR-1 is a periplasmic tetraheme flavocytochrome c. The crystal structures of the enzyme were solved to 2.9 A for the uncomplexed form and to 2.8 A and 2.5 A for the fumarate and the succinate-bound protein, respectively. The structures reveal a flexible capping domain linked to the FAD-binding domain. A catalytic mechanism for fumarate reduction based on the structure of the complexed protein is proposed. The mechanism for the reverse reaction is a model for the homologous succinate dehydrogenase (complex II) of the respiratory chain. In flavocytochrome c fumarate reductase, all redox centers are in van der Waals contact with one another, thus providing an efficient conduit of electrons from the hemes via the FAD to fumarate.
Structure and mechanism of the flavocytochrome c fumarate reductase of Shewanella putrefaciens MR-1.,Leys D, Tsapin AS, Nealson KH, Meyer TE, Cusanovich MA, Van Beeumen JJ Nat Struct Biol. 1999 Dec;6(12):1113-7. PMID:10581551[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schwalb C, Chapman SK, Reid GA. The membrane-bound tetrahaem c-type cytochrome CymA interacts directly with the soluble fumarate reductase in Shewanella. Biochem Soc Trans. 2002 Aug;30(4):658-62. PMID:12196158 doi:10.1042/bst0300658
- ↑ Schwalb C, Chapman SK, Reid GA. The tetraheme cytochrome CymA is required for anaerobic respiration with dimethyl sulfoxide and nitrite in Shewanella oneidensis. Biochemistry. 2003 Aug 12;42(31):9491-7. PMID:12899636 doi:10.1021/bi034456f
- ↑ Schuetz B, Schicklberger M, Kuermann J, Spormann AM, Gescher J. Periplasmic electron transfer via the c-type cytochromes MtrA and FccA of Shewanella oneidensis MR-1. Appl Environ Microbiol. 2009 Dec;75(24):7789-96. PMID:19837833 doi:10.1128/AEM.01834-09
- ↑ Marritt SJ, Lowe TG, Bye J, McMillan DG, Shi L, Fredrickson J, Zachara J, Richardson DJ, Cheesman MR, Jeuken LJ, Butt JN. A functional description of CymA, an electron-transfer hub supporting anaerobic respiratory flexibility in Shewanella. Biochem J. 2012 Jun 15;444(3):465-74. PMID:22458729 doi:10.1042/BJ20120197
- ↑ Li DB, Cheng YY, Wu C, Li WW, Li N, Yang ZC, Tong ZH, Yu HQ. Selenite reduction by Shewanella oneidensis MR-1 is mediated by fumarate reductase in periplasm. Sci Rep. 2014 Jan 17;4:3735. PMID:24435070 doi:10.1038/srep03735
- ↑ Leys D, Tsapin AS, Nealson KH, Meyer TE, Cusanovich MA, Van Beeumen JJ. Structure and mechanism of the flavocytochrome c fumarate reductase of Shewanella putrefaciens MR-1. Nat Struct Biol. 1999 Dec;6(12):1113-7. PMID:10581551 doi:http://dx.doi.org/10.1038/70051
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