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

B. M. Hoffman*, J. E. Roberts, T. G. Brown, C. H. Kang, E. Margoliash

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

62 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)6132-6136
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume76
Issue number12
DOIs
StatePublished - Dec 1979

ASJC Scopus subject areas

  • General

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