Kinetic and spectral properties of pea cytosolic ascorbate peroxidase.

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Marquez LA,Quitoriano M,Zilinskas BA,Dunford HB

doi

10.1016/0014-5793(96)00562-5

subject

Has Abstract

pub_date

1996-07-01 00:00:00

pages

153-6

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(96)00562-5

journal_volume

389

pub_type

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