Electron paramagnetic resonance studies of the soluble Cu(A) protein from the cytochrome ba3 of Thermus thermophilus

Biophysical Journal

Volumn 71, Issue 5, 1996, Pages 2823-2829

  Karpefors, Martin ^a   Slutter, Claire E ^c   Fee, James A ^d   Aasa, Roland ^a   Kä̈llebring, Bruno ^a   Larsson, Sven ^b   Vänngård, Tore ^a  

^a UNIVERSITY OF GOTHENBURG   (Sweden)

^b CHALMERS UNIVERSITY OF TECHNOLOGY   (Sweden)

^c California Institute of Technology   (United States)

^d UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; COPPER ION; CYTOCHROME;

ARTICLE; ELECTRON SPIN RESONANCE; NONHUMAN; PROTEIN ANALYSIS; SPECTROSCOPY; THERMUS THERMOPHILUS;

BACTERIA (MICROORGANISMS); PARACOCCUS DENITRIFICANS; THERMUS THERMOPHILUS;

EID: 0029861646     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79478-X     Document Type: Article

References (25)

1. Aasa, R., S. P. J. Albracht, K.-E. Falk, B. Lanne, and T. Vänngård. 1976. EPR signals from cytochrome c oxidase. Biochim. Biophys. Acta. 422: 260-272.
2. Aasa, R., and T. Vänngård. 1975. EPR signal intensity and powder shapes: a reexamination. J. Magn. Res. 19:308-315.
3. Abragam, A., and B. Bleaney. 1970. Electron Paramagnetic Resonance of Transition Ions. Clarendon Press, Oxford. 181-191.
4. Adman, E. T. 1991. Copper protein structure. Adv. Protein Chem. 42: 145-197.
5. Antholine, W. E., D. H. W. Kastrau, G. C. M. Steffens, G. Buse, W. G. Zumft, and P. M. H. Kroneck. 1992. A comparative EPR investigation of the multicopper proteins nitrous-oxide reductase and cytochrome c oxidase. Eur. J. Biochem. 209:875-891.
6. Beinert, H., D. E. Griffiths, D. C. Wharton, and R. H. Sands. 1962. Properties of the copper associated with cytochrome oxidase as studied by paramagnetic resonance spectroscopy. J. Biol. Chem. 237: 2337-2346.
7. Boça, R. 1987. Inclusion of relativistic effects into ZDO methods. 1. A quasi-relativistic CNDO/1. Int. J. Quant. Chem. 31:941-950.
8. Broo, A., and S. Larsson. 1992. Ab initio and semiempirical studies of electron-transfer and spectra of binuclear complexes with organic bridges. Chem. Phys. 161:363-378.
9. 3 subunit II from Thermus thermophilus. Biochem. Biophys. Res. Commun. 212:77-83.
10. Froncisz, W., C. P. Scholes, J. S. Hyde, Y.-H. Wei, T. E. King, R. W. Shaw, and H. Beinert. 1979. Hyperfine structure resolved by 2 to 4 GHz EPR of cytochrome c oxidase. J. Biol. Chem. 254:7482-7484.
11. Gewirth, A. A., S. L. Cohen, H. J. Schugar, and E. I. Solomon. 1987. Spectroscopic and theoretical studies of the unusual EPR parameters of distorted tetrahedral cupric sites: correlations to x-ray spectral features of core levels. Inorg. Chem. 26:1133-1146.
12. 3 from Thermus thermophilus. J. Am. Chem. Soc. 115: 10888-10894.
13. Iwata, S., C. Ostermeier, B. Ludwig, and H. Michel. 1995. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature. 376:660-669.
14. Keijzers, C. P., and E. de Boer. 1975. E. S. R. study of copper and silver N,N-dialkyldiselenocarbamates. Part II. Interpretation of spectra measured in host lattices with monomeric structures. Mol. Phys. 29: 1007-1020.
15. Kroneck, P. M. H., W. E. Antholine, J. Rister, and W. G. Zumft. 1988. The cupric site in nitrous oxide reductase contains a mixed-valence [Cu(II),Cu(I)] binuclear center: a multifrequency electron paramagnetic resonance investigation. FEBS Lett. 242:70-74.
16. Larsson, S., A. Broo, B. Källebring, and A. Volosov. 1988. Long distance electron transfer. Int. J. Quant. Chem. QBS. 15:1-22.
17. Lu, Y., E. B. Gralla, J. A. Roe, and J. S. Valentine. 1992. Redesign of a type 2 into a type 1 copper protein: construction and characterization of yeast copper-zinc superoxide dismutase mutants. J. Am. Chem. Soc. 114:3560-3562.
18. Malmström, B. G. 1994. Rack-induced bonding in blue-copper proteins. Eur. J. Biochem. 223:711-718.
19. A center in cytochrome c oxidase. FEBS Lett. 325:1-2.
20. Pilbrow, J. R. 1990. Transition Ion Electron Paramagnetic Resonance. Clarendon Press, Oxford.
21. 3 subunit II from Thermus thermophilus. Biochemistry. 35:3387-3395.
22. Solomon, E. I., and M. D. Lowery. 1993. Electronic structure contributions to function in bioinorganic chemistry. Science. 259:1575-1581.
23. Tsukihara, T., H. Aoyama, E. Yamashita, T. Tomizaki, H. Yamaguchi, K. Shinzawa-Itoh, R. Nakashima, R. Yaono, and S. Yoshikawa. 1995. Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 Å. Science. 269:1069-1074.
24. Vänngård, T. 1972. Copper proteins. In Biological Applications of Electron Spin Resonance. H. M. Swartz, J. R. Bolton, and D. C. Borg, editors. John Wiley and Sons, New York. 411-447.
25. Wilmanns, M., P. Lappalainen, M. Kelly, E. Sauer-Eriksson, and M. Saraste, 1995. Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper center. Proc. Natl. Acad. Sci. USA. 92:11955-11959.