1dcc
From Proteopedia
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. 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 Page seeded by OCA on Fri May 2 13:41:11 2008
