4.6 Review

An analysis of substrate binding interactions in the heme peroxidase enzymes: A structural perspective

Journal

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 500, Issue 1, Pages 13-20

Publisher

ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2010.02.015

Keywords

Heme; Peroxidase; Substrate; Cytochrome c peroxidase; Ascorbate peroxidase; Horseradish peroxidase

Funding

  1. BBSRC
  2. Leverhulme Trust
  3. Biotechnology and Biological Sciences Research Council [BB/C001184/1] Funding Source: researchfish

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The interactions of heme peroxidase enzymes with their substrates have been studied for many years, but only in the last decade or so has structural information begun to appear. This review looks at crystal structures for a number of home peroxidases in complex with a number of (mainly organic) substrates. It examines the nature and location of the binding interaction, and explores functional similarities and differences across the family. (C) 2010 Elsevier Inc. All rights reserved.

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