Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/621
Title: Crystal structure of the ascorbate peroxidase-ascorbate complex.
Authors: Sharp, K.H.
Mewies, M.
Moody, Peter C.E.
Raven, E.L.
First Published: 2003
Citation: Nature Structural Biology, 2003, 10 (4), pp.303-307
Abstract: Heme peroxidases catalyze the H2O2-dependent oxidation of a variety of substrates, most of which are organic. Mechanistically, these enzymes are well characterized: they share a common catalytic cycle that involves formation of a two-electron, oxidized Compound I intermediate followed by two single-electron reduction steps by substrate. The substrate specificity is more diverse — most peroxidases oxidize small organic substrates, but there are prominent exceptions — and there is a notable absence of structural information for a representative peroxidase−substrate complex. Thus, the features that control substrate specificity remain undefined. We present the structure of the complex of ascorbate peroxidase−ascorbate. The structure defines the ascorbate-binding interaction for the first time and provides new rationalization of the unusual functional features of the related cytochrome c peroxidase enzyme, which has been a benchmark for peroxidase catalysis for more than 20 years. A new mechanism for electron transfer is proposed that challenges existing views of substrate oxidation in other peroxidases.
DOI Link: 10.1038/nsb913
ISSN: 1072-8368
Links: http://hdl.handle.net/2381/621
Type: Article
Appears in Collections:Published Articles, Dept. of Chemistry
Published Articles, Dept. of Biochemistry

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