1yux
From Proteopedia
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Mixed valant state of nigerythrin
Overview
High-resolution crystal structures of Desulfovibrio vulgaris nigerythrin, (DvNgr), a member of the rubrerythrin (Rbr) family, demonstrate an, approximately 2-A movement of one iron (Fe1) of the diiron site from a, carboxylate to a histidine ligand upon conversion of the mixed-valent, ([Fe2(II),Fe1(III)]) to diferrous states, even at cryogenic temperatures., This Glu<-->His ligand "toggling" of one iron, which also occurs in DvRbr, thus, appears to be a characteristic feature of Rbr-type diiron sites., Unique features of DvNgr revealed by these structures include, redox-induced flipping of a peptide carbonyl that reversibly forms a, hydrogen bond to the histidine ligand to Fe1 of the diiron site, an, intra-subunit proximal orientation of the rubredoxin-(Rub)-like and diiron, domains, and an electron transfer pathway consisting of six covalent and, two hydrogen bonds connecting the Rub-like iron with Fe2 of the diiron, site. This pathway can account for DvNgr's relatively rapid peroxidase, turnover. The characteristic combination of iron sites together with the, redox-dependent iron toggling between protein ligands can account for the, selectivity of Rbrs for hydrogen peroxide over dioxygen.
About this Structure
1YUX is a Single protein structure of sequence from Desulfovibrio vulgaris with FE and FE2 as ligands. Full crystallographic information is available from OCA.
Reference
High-resolution crystal structures of Desulfovibrio vulgaris (Hildenborough) nigerythrin: facile, redox-dependent iron movement, domain interface variability, and peroxidase activity in the rubrerythrins., Iyer RB, Silaghi-Dumitrescu R, Kurtz DM Jr, Lanzilotta WN, J Biol Inorg Chem. 2005 Jun;10(4):407-16. Epub 2005 May 14. PMID:15895271
Page seeded by OCA on Wed Nov 21 07:04:01 2007
