The peroxide complex of yeast cytochrome c peroxidase contains two distinct radical species, neither of which resides at methionine 172 or tryptophan 51.-Reference-Cited by-同舟云学术

The peroxide complex of yeast cytochrome c peroxidase contains two distinct radical species, neither of which resides at methionine 172 or tryptophan 51.

Published:1987-06 Issue:16 Volume:262 Page:7719-7724
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Goodin D B,Mauk A G,Smith M

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference39 articles.

1. Studies of the radical species in compound ES of cytochrome c peroxidase altered by site-directed mutagenesis.

2. Electron paramagnetic and electron nuclear double resonance of the hydrogen peroxide compound of cytochrome c peroxidase.

3. Powder and single-crystal electron paramagnetic resonance studies of yeast cytochrome c peroxidase and its peroxide and its peroxide compound, Compound ES.

4. Identification of the stable free radical tyrosine residue in ribonucleotide reductase.

5. The Enzymes;Yonetani,1976

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