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. 1981 Mar;78(3):1652–1655. doi: 10.1073/pnas.78.3.1652

Spectroscopic characterization of compound C and related derivatives of cytochrome oxidase.

K R Carter, T M Antalis, G Palmer, N S Ferris, W H Woodruff
PMCID: PMC319190  PMID: 6262822

Abstract

Magnetic circular dichroism and resonance Raman spectra have been obtained for three "oxygenated" derivatives of cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1). The spectra are interpreted and four alternatives for the states of cytochrome a3 and Cuu are evaluated.

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Selected References

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

  1. Antonini E., Brunori M., Colosimo A., Greenwood C., Wilson M. T. Oxygen "pulsed" cytochrome c oxidase: functional properties and catalytic relevance. Proc Natl Acad Sci U S A. 1977 Aug;74(8):3128–3132. doi: 10.1073/pnas.74.8.3128. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Babcock G. T., Vickery L. E., Palmer G. Electronic state of heme in cytochrome oxidase. I. Magnetic circular dichroism of the isolated enzyme and its derivatives. J Biol Chem. 1976 Dec 25;251(24):7907–7919. [PubMed] [Google Scholar]
  3. Chance B., Graham N., Legallais V. Low temperature trapping method for cytochrome oxidase oxygen intermediates. Anal Biochem. 1975 Aug;67(2):552–579. doi: 10.1016/0003-2697(75)90331-0. [DOI] [PubMed] [Google Scholar]
  4. Chance B., Saronio C., Leigh J. S., Jr Functional intermediates in the reaction of membrane-bound cytochrome oxidase with oxygen. J Biol Chem. 1975 Dec 25;250(24):9226–9237. [PubMed] [Google Scholar]
  5. Clore G. M., Andréasson L. E., Karlsson B., Aasa R., Malmström B. G. Characterization of the intermediates in the reaction of mixed-valence state soluble cytochrome oxidase with oxygen at low temperatures by optical and electron-paramagnetic-resonance spectroscopy. Biochem J. 1980 Jan 1;185(1):155–167. doi: 10.1042/bj1850155. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Clore G. M., Andréasson L. E., Karlsson B., Aasa R., Malmström B. G. Characterization of the low-temperature intermediates of the reaction of fully reduced soluble cytochrome oxidase with oxygen by electron-paramagnetic-resonance and optical spectroscopy. Biochem J. 1980 Jan 1;185(1):139–154. doi: 10.1042/bj1850139. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Greenwood C., Wilson M. T., Brunori M. Studies on partially reduced mammalian cytochrome oxidase. Reactions with carbon monoxide and oxygen. Biochem J. 1974 Feb;137(2):205–215. doi: 10.1042/bj1370205. [DOI] [PMC free article] [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. Palmer G., Babcock G. T., Vickery L. E. A model for cytochrome oxidase. Proc Natl Acad Sci U S A. 1976 Jul;73(7):2206–2210. doi: 10.1073/pnas.73.7.2206. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Shaw R. W., Hansen R. E., Beinert H. A novel electron paramagnetic resonance signal of "oxygenated" cytochrome c oxidase. J Biol Chem. 1978 Oct 10;253(19):6637–6640. [PubMed] [Google Scholar]
  11. Shaw R. W., Hansen R. E., Beinert H. The oxygen reactions of reduced cytochrome c oxidase. Position of a form with an unusual EPR signal in the sequence of early intermediates. Biochim Biophys Acta. 1979 Nov 8;548(2):386–396. doi: 10.1016/0005-2728(79)90143-9. [DOI] [PubMed] [Google Scholar]
  12. Sievers G., Osterlund K., Ellfolk N. Resonance Raman study on yeast cytochrome c peroxidase. Effect of coordination and axial ligands. Biochim Biophys Acta. 1979 Nov 23;581(1):1–14. doi: 10.1016/0005-2795(79)90215-0. [DOI] [PubMed] [Google Scholar]
  13. 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]
  14. Vanneste W. H. The stoichiometry and absorption spectra of components a and a-3 in cytochrome c oxidase. Biochemistry. 1966 Mar;5(3):838–848. doi: 10.1021/bi00867a005. [DOI] [PubMed] [Google Scholar]
  15. Yammoto T., Palmer G. The valence and spin state of iron in oxyhemoglobin as inferred from resonance Raman spectroscopy. J Biol Chem. 1973 Jul 25;248(14):5211–5213. [PubMed] [Google Scholar]

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