Structural highlights
Evolutionary Conservation
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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.
See Also
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
