The reaction of hydrogen peroxide with the dimethyl ester heme derivative of cytochrome c peroxidase.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference16 articles.
1. Kinetic study of the reaction between cytochrome c peroxidase and hydrogen peroxide. Dependence on pH and ionic strength
2. A Kinetic Study of the Reaction of Horseradish Peroxidase with Hydrogen Peroxide
3. Kinetics of formation of the primary compound (compound I) from hydrogen peroxide and turnip peroxidases
4. Comparisons between hog intestinal peroxidase and bovine lactoperoxidase—Compound I formation and inhibition by benzhydroxamic acid
5. Horseradish peroxidase. XXXVII. Compound I formation from reconstituted enzyme lacking free carboxyl groups as heme side chains
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1. The Janus nature of heme;Natural Product Reports;2007
2. Role of histidine 42 in ascorbate peroxidase;European Journal of Biochemistry;2002-07
3. Histidine 52 is a critical residue for rapid formation of cytochrome c peroxidase compound I;Biochemistry;1993-09-21
4. Carbon monoxide recombination in cytochrome c peroxidase: effect of the local heme environment on carbon monoxide binding explored through site-directed mutagenesis;Biochemistry;1990-02-20
5. Site-directed mutagenesis of yeast cytochrome c peroxidase shows histidine 181 is not required for oxidation of ferrocytochrome c;Biochemistry;1988-12
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