Abstract
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 heme 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.
| Original language | English |
|---|---|
| Pages (from-to) | 13-20 |
| Number of pages | 8 |
| Journal | Archives of Biochemistry and Biophysics |
| Volume | 500 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 1 Aug 2010 |
Research Groups and Themes
- Inorganic & Materials
Keywords
- Ascorbate peroxidase
- Cytochrome c peroxidase
- Heme
- Horseradish peroxidase
- Peroxidase
- Substrate
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