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Hyperfine structure resolved by 2 to 4 GHz EPR of cytochrome c oxidase.

  • W. Froncisz*
  • , C. P. Scholes
  • , J. S. Hyde
  • , Y. H. Wei
  • , T. E. King
  • , R. W. Shaw
  • , H. Beiner
  • *Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

61 Scopus citations

Abstract

Using low frequency 2 to 4 GHz EPR at 10 K, we have resolved previously unseen hyperfine structure associated with the EPR-detectable copper signal of cytochrome c oxidase. The observed hyperfine structure appears consistent with hyperfine coupling to copper; although to account for all of the observed structure, an additional magnetic interaction is required as well. This work points out the utility of the 2 to 4 GHz EPR technique for resolving electronic hyperfine structural information from copper and possibly other paramagnetic sites in biomolecules when random variation in electronic g values is a cause of EPR line-broadening.

Original languageEnglish
Pages (from-to)7482-7484
Number of pages3
JournalJournal of Biological Chemistry
Volume254
Issue number16
DOIs
StatePublished - 25 08 1979
Externally publishedYes

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