Chemical and kinetic evidence for an essential histidine residue in the electron transfer from aromatic donor to horseradish peroxidase compound I.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference60 articles.
1. Isolation and Characterization of Five Neutral Isoenzymes of Horseradish Peroxidase1
2. Protein control of prosthetic heme reactivity. Reaction of substrates with the heme edge of horseradish peroxidase.
3. Structure and catalytic mechanism of horseradish peroxidase. Regiospecific meso alkylation of the prosthetic heme group by alkylhydrazines.
4. Elementary steps in the formation of horseradish peroxidase compound I: direct observation of compound 0, a new intermediate with a hyperporphyrin spectrum
5. Chemical and kinetic evidence for an essential histidine in horseradish peroxidase for iodide oxidation.
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