Electron-nuclear double resonance of the hydrogen peroxide compound of cytochrome c peroxidase: identification of the free radical site with a methionyl cluster.

Abstract:

:The results of electron-nuclear double resonance and electron paramagnetic resonance (EPR) studies on the hydrogen peroxide compound of yeast cytochrome c peroxidase are inconsistent with previous proposals for the source of the EPR signal in this compound, in particular with its identification with an aromatic amino acid radical such as would arise by oxidation of a tryptophanyl side chain. The present observations lead us to propose that the EPR signal is associated with a cluster containing at least one methionine and in which proximate side chains share the charge created by loss of one electron.

authors

Hoffman BM,Roberts JE,Brown TG,Kang CH,Margoliash E

doi

10.1073/pnas.76.12.6132

subject

Has Abstract

pub_date

1979-12-01 00:00:00

pages

6132-6

issue

12

eissn

0027-8424

issn

1091-6490

journal_volume

76

pub_type

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