Structural highlights
Function
FLAV_DESVH Low-potential electron donor to a number of redox enzymes.
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 mutant S64C of the short-chain flavodoxin from Desulfovibrio vulgaris has been designed to introduce an accessible and reactive group on the protein surface. Crystals have been obtained of both the monomeric and homodimeric forms of the protein, with the cofactor FMN in either the oxidized or the one electron-reduced (semiquinone) state, and the structures have been determined to high resolution. The redox properties of the different species have been investigated and the variations observed with respect to wild type have been related to the structural changes induced by the mutation and S-S bridge formation.
Redox properties and crystal structures of a Desulfovibrio vulgaris flavodoxin mutant in the monomeric and homodimeric forms.,Fantuzzi A, Artali R, Bombieri G, Marchini N, Meneghetti F, Gilardi G, Sadeghi SJ, Cavazzini D, Rossi GL Biochim Biophys Acta. 2009 Mar;1794(3):496-505. Epub 2008 Dec 11. PMID:19118653[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fantuzzi A, Artali R, Bombieri G, Marchini N, Meneghetti F, Gilardi G, Sadeghi SJ, Cavazzini D, Rossi GL. Redox properties and crystal structures of a Desulfovibrio vulgaris flavodoxin mutant in the monomeric and homodimeric forms. Biochim Biophys Acta. 2009 Mar;1794(3):496-505. Epub 2008 Dec 11. PMID:19118653 doi:10.1016/j.bbapap.2008.11.026
