1yv1: Difference between revisions
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{{STRUCTURE_1yv1| PDB=1yv1 | SCENE= }} | |||
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'''Fully reduced state of nigerythrin (all ferrous)''' | '''Fully reduced state of nigerythrin (all ferrous)''' | ||
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[[Category: Lanzilotta, W N.]] | [[Category: Lanzilotta, W N.]] | ||
[[Category: Silaghi-Dumitrescu, R.]] | [[Category: Silaghi-Dumitrescu, R.]] | ||
[[Category: | [[Category: Diiron center]] | ||
[[Category: | [[Category: Electron transfer]] | ||
[[Category: | [[Category: Hemerythrin]] | ||
[[Category: | [[Category: Peroxidase]] | ||
[[Category: | [[Category: Rubredoxin]] | ||
[[Category: | [[Category: Rubrerythrin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:49:21 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 13:49, 3 May 2008
Fully reduced state of nigerythrin (all ferrous)
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
1YV1 is a Single protein structure of sequence from Desulfovibrio vulgaris. 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 Sat May 3 16:49:21 2008
