1akv: Difference between revisions
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D95A SEMIQUINONE FLAVODOXIN MUTANT FROM D. VULGARIS
OverviewOverview
The side chain of aspartate 95 in flavodoxin from Desulfovibrio vulgaris, provides the closest negative charge to N(1) of the bound FMN in the, protein. Site-directed mutagenesis was used to substitute alanine, asparagine, or glutamate for this amino acid to assess the effect of this, charge on the semiquinone/hydroquinone redox potential (E(1)) of the FMN, cofactor. The D95A mutation shifts the E(1) redox potential positively by, 16 mV, while a negative shift of 23 mV occurs in the oxidized/semiquinone, midpoint redox potential (E(2)). The crystal structures of the oxidized, and semiquinone forms of this mutant are similar to the corresponding, states of the wild-type protein. In contrast to the wild-type protein, a, further change in structure occurs in the D95A mutant in the ... [(full description)]
About this StructureAbout this Structure
1AKV is a [Single protein] structure of sequence from [Desulfovibrio vulgaris] with SO4 and FMN as [ligands]. Structure known Active Site: FMN. Full crystallographic information is available from [OCA].
ReferenceReference
Crystallographic investigation of the role of aspartate 95 in the modulation of the redox potentials of Desulfovibrio vulgaris flavodoxin., McCarthy AA, Walsh MA, Verma CS, O'Connell DP, Reinhold M, Yalloway GN, D'Arcy D, Higgins TM, Voordouw G, Mayhew SG, Biochemistry. 2002 Sep 10;41(36):10950-62. PMID:12206666
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