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

59 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
StatePublished - 25 08 1979

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