| Literature DB >> 8766820 |
L A Marquez1, M Quitoriano, B A Zilinskas, H B Dunford.
Abstract
Sufficient highly purified native pea cytosolic ascorbate peroxidase was obtained to characterize some of its kinetic and spectral properties. Its rate constant for compound I formation from reaction with H2O2 is 4.O x 10(7) M-1 s-1, somewhat faster than is typical for peroxidases. Compound I has the typical optical spectrum of an iron(IV)-porphyrin-pi-cation radical, despite considerable homology with yeast cytochrome c peroxidase. The rate constant for compound I reduction by ascorbate is extremely fast (8.0 x 10(7) M-1 S-1 at pH 7.8), again in marked contrast to the behavior of the yeast enzyme. The pH-rate profile for compound I formation indicates a pKa value of 5.0 for a group affecting the active site reaction.Entities:
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Year: 1996 PMID: 8766820 DOI: 10.1016/0014-5793(96)00562-5
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124