Interpretation of the reactivity of peroxidase compounds I and II with phenols by the Marcus equation.

Abstract:

:The catalytic cycle of heme peroxidases involves two reactive states, compound I and compound II. Although their reduction potentials at pH 7 are similar, compound I is in general more reactive towards organic substrates than compound II. The different reactivities have until now remained unexplained. In this study, the reactions of compounds I and II of peroxidase from horseradish with phenols were analyzed using the Marcus equation of electron-transfer. Both reactions exhibit similar reorganization energies, and the different reactivities of the two enzyme states can be ascribed to a higher apparent rate of activationless electron-transfer in the compound I reactions. This can be attributed to the shorter electron-tunneling distance on electron-transfer to the porphyrin radical cation in compound I, compared to electron-transfer to the iron ion in compound II.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Folkes LK,Candeias LP

doi

10.1016/s0014-5793(97)00792-8

subject

Has Abstract

pub_date

1997-07-28 00:00:00

pages

305-8

issue

2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(97)00792-8

journal_volume

412

pub_type

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