Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1979 Jan 1;177(1):29–39. doi: 10.1042/bj1770029

Some magnetic properties of Pseudomonas cytochrome oxidase.

T A Walsh, M K Johnson, C Greenwood, D Barber, J P Springall, A J Thomson
PMCID: PMC1186337  PMID: 218561

Abstract

The magnetic properties of the haem groups of Pseudomonas cytochrome oxidase and its cyanide-bound derivatives were studied in both the oxidized and reduced states by means of m.c.d. (magnetic circular dichroism) at low temperatures. In addition, the oxidized forms of the enzyme were also investigated by e.p.r. (electron-paramagnetic-resonance) spectroscopy, and a parallel study, using both e.p.r. and m.c.d., was made on Pseudomonas cytochrome c-551 to aid spectral assignments. For ascorbate-reduced Pseudomonas cytochrome oxidase, the temperature-independence of those features in the m.c.d. spectrum corresponding to the haem c, and the temperature-dependence of those signals corresponding to the haem d1, showed the former to be low-spin and the latter to be high-spin (s = 2). However, addition of cyanide to the reduced enzyme gave a form of the protein that was completely low-spin. The e.p.r. and m.c.d. sectra of oxidized Pseudomonas cytochrome oxidase and its cyanide derivative were consistent with the haem c and d1 components being low-spin in both cases. Pseudomonas cytochrome c-551 was found to be low-spin in both its oxidized and reduced redox states.

Full text

PDF
29

Selected References

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

  1. Barber D., Parr S. R., Greenwood C. The reactions of Pseudomonas cytochrome c-551 oxidase with potassium cyanide. Biochem J. 1978 Oct 1;175(1):239–249. doi: 10.1042/bj1750239. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Greenwood C., Barber D., Parr S. R., Antonini E., Brunori M., Colosimo A. The reaction of Pseudomonas aeruginosa cytochrome c-551 oxidase with oxygen. Biochem J. 1978 Jul 1;173(1):11–17. doi: 10.1042/bj1730011. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Gudat J. C., Singh J., Wharton D. C. Cytochrome oxidase from Pseudomonas aeruginosa. I. Purification and some properties. Biochim Biophys Acta. 1973 Feb 22;292(2):376–390. doi: 10.1016/0005-2728(73)90044-3. [DOI] [PubMed] [Google Scholar]
  4. HORIO T., HIGASHI T., SASAGAWA M., KUSAI K., NAKAI M., OKUNUKI K. Preparation of crystalline Pseudomonas cvtochrome c-551 and its general properties. Biochem J. 1960 Oct;77:194–201. doi: 10.1042/bj0770194. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. HORIO T., HIGASHI T., YAMANAKA T., MATSUBARA H., OKUNUKI K. Purification and properties of cytochrome oxidase from Pseudomonas aeruginosa. J Biol Chem. 1961 Mar;236:944–951. [PubMed] [Google Scholar]
  6. Kuronen T., Saraste M., Ellfork N. The subunit structure of Pseudomonas cytochrome oxidase. Biochim Biophys Acta. 1975 May 30;393(1):48–54. doi: 10.1016/0005-2795(75)90215-9. [DOI] [PubMed] [Google Scholar]
  7. Orii Y., Shimada H., Nozawa T., Hatano M. The interaction between the heme c and heme d moieties of Pseudomonas nitrite reductase as revealed by magnetic and natural circular dichroism studies. Biochem Biophys Res Commun. 1977 Jun 20;76(4):983–988. doi: 10.1016/0006-291x(77)90952-4. [DOI] [PubMed] [Google Scholar]
  8. Parr S. R., Barber D., Greenwood C. A purification procedure for the soluble cytochrome oxidase and some other respiratory proteins from Pseudomonas aeruginosa. Biochem J. 1976 Aug 1;157(2):423–430. doi: 10.1042/bj1570423. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Parr S. R., Barber D., Greenwood C., Brunori M. The electron-transfer reaction between azurin and the cytochrome c oxidase from Pseudomonas aeruginosa. Biochem J. 1977 Nov 1;167(2):447–455. doi: 10.1042/bj1670447. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Parr S. R., Wilson M. T., Greenwood C. The reaction of Pseudomonas aeruginosa cytochrome c oxidase with carbon monoxide. Biochem J. 1975 Oct;151(1):51–59. doi: 10.1042/bj1510051. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Shimada H., Orii Y. The nitric oxide compounds of Pseudomonas aeruginosa nitrite reductase and their probable participation in the nitrite reduction. FEBS Lett. 1975 Jun 15;54(2):237–240. doi: 10.1016/0014-5793(75)80082-2. [DOI] [PubMed] [Google Scholar]
  12. Springall J., Stillman M. J., Thomson A. J. Low temperature magnetic circular dichroism spectra of met- and myoglobin derivatives. Biochim Biophys Acta. 1976 Dec 22;453(2):494–501. doi: 10.1016/0005-2795(76)90145-8. [DOI] [PubMed] [Google Scholar]
  13. Thomson A. J., Brittain T., Greenwood C., Springall J. P. Variable-temperature magnetic-circular-dichroism spectra of cytochrome c oxidase and its derivatives. Biochem J. 1977 Aug 1;165(2):327–336. doi: 10.1042/bj1650327. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Vickery L. E., Palmer G., Wharton D. C. Heme c - heme d1 interaction in Pseudomonas cytochrome oxidase (nitrite reductase): a reappraisal of the spectroscopic evidence. Biochem Biophys Res Commun. 1978 Jan 30;80(2):458–463. doi: 10.1016/0006-291x(78)90699-x. [DOI] [PubMed] [Google Scholar]
  15. Williams-Smith D. L., Bray R. C., Barber M. J., Tsopanakis A. D., Vincent S. P. Changes in apparent pH on freezing aqueous buffer solutions and their relevance to biochemical electron-paramagnetic-resonance spectroscopy. Biochem J. 1977 Dec 1;167(3):593–600. doi: 10.1042/bj1670593. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. YAMANAKA T., KIJIMOTO S., OKUNUKI K. Biological significance of Pseudomonas cytochrome oxidase in Pseudomonas aeruginosa. J Biochem. 1963 May;53:416–421. doi: 10.1093/oxfordjournals.jbchem.a127716. [DOI] [PubMed] [Google Scholar]
  17. YAMANAKA T., OKUNUKI K. Crystalline Pseudomonas cytochrome oxidase. III. Properties of the prosthetic groups. Biochim Biophys Acta. 1963 Mar 12;67:407–416. doi: 10.1016/0006-3002(63)91846-8. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES