Structural highlights
Function
[CCPR_YEAST] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Miller MA, Shaw A, Kraut J. 2.2 A structure of oxy-peroxidase as a model for the transient enzyme: peroxide complex. Nat Struct Biol. 1994 Aug;1(8):524-31. PMID:7664080
