Altering Substrate Specificity at the Heme Edge of Cytochrome c Peroxidase
Author:
Affiliation:
1. Department of Molecular Biology, MB8, The Scripps Research Institute, 10666 North Torrey Pines Road, La Jolla, California 92037
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi952929f
Reference60 articles.
1. Electron paramagnetic resonance and electron nuclear double resonance spectroscopies of the radical site in galactose oxidase and of thioether-substituted phenol model compounds
2. A stopped-flow study of the reaction of cytochromecperoxidase with hydroperoxides
3. Role of the proximal ligand in peroxidase catalysis. Crystallographic, kinetic, and spectral studies of cytochrome c peroxidase proximal ligand mutants.
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