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Issue 22, 2003
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A new framework for understanding substrate binding and functional diversity in haem peroxidases

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Abstract

The haem-containing peroxidase enzymes catalyse the H2O2-dependent oxidation of a wide variety of substrates and have provided a focal point for our more general understanding of structure/function relationships in other, more complex haem enzymes. Mechanistically, the haem peroxidases are well characterised: they share a common catalytic cycle that involves formation of a high-oxidation-state (ferryl) intermediate. In contrast, our understanding of the structural features that control the diverse substrate specificity are less well defined. In this review, we discuss how recent spectroscopic and structural information for ascorbate peroxidase has provided new insight into the modus operandi of this enzyme and how this has helped to clarify certain aspects of the catalytic and, in particular, the substrate binding properties of the closely related cytochrome c peroxidase enzyme, which has been a benchmark for peroxidase catalysis over more than 20 years.

Graphical abstract: A new framework for understanding substrate binding and functional diversity in haem peroxidases

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Publication details

The article was received on 11 Aug 2003, accepted on 23 Sep 2003 and first published on 13 Oct 2003


Article type: Perspective
DOI: 10.1039/B309648N
Citation: Dalton Trans., 2003,0, 4208-4215

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    A new framework for understanding substrate binding and functional diversity in haem peroxidases

    K. H. Sharp, P. C. E. Moody and E. L. Raven, Dalton Trans., 2003, 0, 4208
    DOI: 10.1039/B309648N

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