Structural highlights
Function
[CYC3_DESVH] Participates in sulfate respiration coupled with phosphorylation by transferring electrons from the enzyme dehydrogenase to ferredoxin.
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
The NMR structure of the oxidised wild-type cytochrome c3 from Desulfovibrio vulgaris Hildenborough was determined in solution. Using a newly developed methodology, NMR data from the K45Q mutant was then grafted onto data from the wild-type protein to determine the structure in the region of the mutation. The structural origins of the redox-Bohr effect and haem-haem cooperativities are discussed with respect to the redox-related conformational changes observed in solution.
Solution structures of tetrahaem ferricytochrome c3 from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: the molecular basis of cooperativity.,Messias AC, Aguiar AP, Brennan L, Salgueiro CA, Saraiva LM, Xavier AV, Turner DL Biochim Biophys Acta. 2006 Feb;1757(2):143-53. Epub 2006 Feb 20. PMID:16527248[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Messias AC, Aguiar AP, Brennan L, Salgueiro CA, Saraiva LM, Xavier AV, Turner DL. Solution structures of tetrahaem ferricytochrome c3 from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: the molecular basis of cooperativity. Biochim Biophys Acta. 2006 Feb;1757(2):143-53. Epub 2006 Feb 20. PMID:16527248 doi:10.1016/j.bbabio.2006.01.007
