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2.2 Å structure of oxy-peroxidase as a model for the transient enzyme: peroxide complex

Nature Structural Biology volume 1, pages 524–531 (1994)Cite this article

Abstract

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.

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  1. Department of Chemistry, University of California, San Diego La Jolla, CA, 92093-0317

    Mark A. Miller, Andrew Shaw & Joseph Kraut

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Miller, M., Shaw, A. & Kraut, J. 2.2 Å structure of oxy-peroxidase as a model for the transient enzyme: peroxide complex. Nat Struct Mol Biol 1, 524–531 (1994). https://doi.org/10.1038/nsb0894-524

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