1dcc
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(New page: 200px<br /><applet load="1dcc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dcc, resolution 2.2Å" /> '''2.2 ANGSTROM STRUCTUR...)
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Revision as of 11:02, 20 November 2007
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2.2 ANGSTROM STRUCTURE OF OXYPEROXIDASE: A MODEL FOR THE ENZYME:PEROXIDE COMPLEX
Overview
The Fe+3-OOH complex of peroxidases has a very short half life, and its, structure cannot be determined by conventional methods. The Fe+2-O2, complex provides a useful structural model for this intermediate, as it, differs by only one electron and one proton from the transient Fe+3-OOH, complex. We therefore determined the crystal structure of the Fe+2-O2, complex formed by a yeast cytochrome c peroxidase mutant with Trp 191, replaced by Phe. The refined structure shows that dioxygen can form a, hydrogen bond with the conserved distal His residue, but not with the, conserved distal Arg residue. When the transient Fe+3-OOH complex is, modelled in a similar orientation, the active site of peroxidase appears, to be optimized for catalysing proton transfer between the vicinal oxygen, atoms of the peroxy-anion.
About this Structure
1DCC is a Single protein structure of sequence from Saccharomyces cerevisiae with OXY and HEM as ligands. Active as Cytochrome-c peroxidase, with EC number 1.11.1.5 Full crystallographic information is available from OCA.
Reference
2.2 A structure of oxy-peroxidase as a model for the transient enzyme: peroxide complex., Miller MA, Shaw A, Kraut J, Nat Struct Biol. 1994 Aug;1(8):524-31. PMID:7664080
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