Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1980 Mar;77(3):1452–1456. doi: 10.1073/pnas.77.3.1452

Copper electron-nuclear double resonance of cytochrome c oxidase.

B M Hoffman, J E Roberts, M Swanson, S H Speck, E Margoliash
PMCID: PMC348513  PMID: 6246493

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.

Full text

PDF
1452

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. AKASAKA K. PARAMAGNETIC RESONANCE IN L-CYSTEINE HYDROCHLORIDE IRRADIATED AT 77K. J Chem Phys. 1965 Aug 15;43:1182–1184. doi: 10.1063/1.1696900. [DOI] [PubMed] [Google Scholar]
  2. Aasa R., Albracht P. J., Falk K. E., Lanne B., Vänngard T. EPR signals from cytochrome c oxidase. Biochim Biophys Acta. 1976 Feb 13;422(2):260–272. doi: 10.1016/0005-2744(76)90137-6. [DOI] [PubMed] [Google Scholar]
  3. BEINERT H., GRIFFITHS D. E., WHARTON D. C., SANDS R. H. Properties of the copper associated with cytochrome oxidase as studied by paramagnetic resonance spectroscopy. J Biol Chem. 1962 Jul;237:2337–2346. [PubMed] [Google Scholar]
  4. Beinert H., Shaw R. W. On the identity of the high spin heme components of cytochrome c oxidase. Biochim Biophys Acta. 1977 Oct 12;462(1):121–130. doi: 10.1016/0005-2728(77)90194-3. [DOI] [PubMed] [Google Scholar]
  5. Brill A. S., Bryce G. F. Cupric ion in blue proteins. J Chem Phys. 1968 May 15;48(10):4398–4404. doi: 10.1063/1.1668007. [DOI] [PubMed] [Google Scholar]
  6. Froncisz W., Scholes C. P., Hyde J. S., Wei Y. H., King T. E., Shaw R. W., Beiner H. Hyperfine structure resolved by 2 to 4 GHz EPR of cytochrome c oxidase. J Biol Chem. 1979 Aug 25;254(16):7482–7484. [PubMed] [Google Scholar]
  7. Greenaway F. T., Chan S. H., Vincow G. An EPR study of the lineshape of copper in cytochrome c oxidase. Biochim Biophys Acta. 1977 Jan 25;490(1):62–78. doi: 10.1016/0005-2795(77)90106-4. [DOI] [PubMed] [Google Scholar]
  8. Hartzell C. R., Beinert H. Components of cytochrome c oxidase detectable by EPR spectroscopy. Biochim Biophys Acta. 1974 Dec 19;368(3):318–338. doi: 10.1016/0005-2728(74)90178-9. [DOI] [PubMed] [Google Scholar]
  9. Hoffman B. M., Roberts J. E., Brown T. G., Kang C. H., Margoliash E. Electron-nuclear double resonance of the hydrogen peroxide compound of cytochrome c peroxidase: identification of the free radical site with a methionyl cluster. Proc Natl Acad Sci U S A. 1979 Dec;76(12):6132–6136. doi: 10.1073/pnas.76.12.6132. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hu V. W., Chan S. I., Brown G. S. X-ray absorption edge studies on oxidized and reduced cytochrome c oxidase. Proc Natl Acad Sci U S A. 1977 Sep;74(9):3821–3825. doi: 10.1073/pnas.74.9.3821. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Moss T. H., Shapiro E., King T. E., Beinert H., Hartzell C. The magnetic susceptibility of cytochrome oxidase in the 4.2-1.5 K range. J Biol Chem. 1978 Nov 25;253(22):8072–8073. [PubMed] [Google Scholar]
  12. Nicholls P., Petersen L. C., Miller M., Hansen F. B. Ligand-induced spectral changes in cytochrome c oxidase and their possible significance. Biochim Biophys Acta. 1976 Nov 9;449(2):188–196. doi: 10.1016/0005-2728(76)90132-8. [DOI] [PubMed] [Google Scholar]
  13. Peisach J., Blumberg W. E. Structural implications derived from the analysis of electron paramagnetic resonance spectra of natural and artificial copper proteins. Arch Biochem Biophys. 1974 Dec;165(2):691–708. doi: 10.1016/0003-9861(74)90298-7. [DOI] [PubMed] [Google Scholar]
  14. Powers L., Blumberg W. E., Chance B., Barlow C. H., Leigh J. S., Jr, Smith J., Yonetani T., Vik S., Peisach J. The nature of the copper atoms of cytochrome c oxidase as studied by optical and x-ray absorption edge spectroscopy. Biochim Biophys Acta. 1979 Jun 5;546(3):520–538. doi: 10.1016/0005-2728(79)90085-9. [DOI] [PubMed] [Google Scholar]
  15. Saxebøl G., Herskedal O. Electron spin resonance studies of electron-irradiated peptides. A single crystal of N-acetyl-L-cysteine at 77 k. Radiat Res. 1975 Jun;62(3):395–406. [PubMed] [Google Scholar]
  16. Solomon E. I., Hare J. W., Gray H. B. Spectroscopic studies and a structural model for blue copper centers in proteins. Proc Natl Acad Sci U S A. 1976 May;73(5):1389–1393. doi: 10.1073/pnas.73.5.1389. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Tweedle M. F., Wilson L. J. Electronic state of heme in cytochrome oxidase III. The magnetic susceptibility of beef heart cytochrome oxidase and some of its derivatives from 7-200 K. Direct evidence for an antiferromagnetically coupled Fe (III)/Cu (II) pair. J Biol Chem. 1978 Nov 25;253(22):8065–8071. [PubMed] [Google Scholar]
  18. Vanneste W. H., Ysebaert-Vanneste M., Mason H. S. The decline of molecular activity of cytochrome oxidase during purification. J Biol Chem. 1974 Dec 10;249(23):7390–7401. [PubMed] [Google Scholar]
  19. van Camp H. L., Wei Y. H., Scholes C. P., King T. E. Electron nuclear double resonance of cytochrome oxidase: nitrogen and proton ENDOR from the 'copper' EPR signal. Biochim Biophys Acta. 1978 Dec 20;537(2):238–246. doi: 10.1016/0005-2795(78)90507-x. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES