Copper electron-nuclear double resonance of cytochrome c oxidase.

B. M. Hoffman*, J. E. Roberts, M. Swanson, S. H. Speck, E. Margoliash

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

50 Scopus citations

Abstract

Electron-nuclear double resonance of copper was observed while monitoring the "intrinsic copper" electron paramagnetic resonance signal of cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) near g = 2. This unambiguously establishes the presence of the metal (Cua) in the redox center responsible for this signal. The hyperfine couplings to copper are largely istropic and the maximum value is about half that seen in type I blue copper proteins. The magnetic properties of this oxidized copper center are not consistent with those of a thiyl radical (R-S) coordinated to Cu(I), and thus favor the identification of this redox center as a Cu(II) ion in a unique environment.

Original languageEnglish (US)
Pages (from-to)1452-1456
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume77
Issue number3
DOIs
StatePublished - Mar 1980

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Copper electron-nuclear double resonance of cytochrome c oxidase.'. Together they form a unique fingerprint.

Cite this