Structure-function correlation of intramolecular electron transfer in wild type and single-site mutated azurins

Chemical Physics

Volumn 204, Issue 2-3 SPEC. ISS., 1996, Pages 271-277

  Farver, Ole ^a   Skov, Lars K ^b   Gilardi, Gianfranco ^c   Van Pouderoyen, Gertie ^d   Canters, Gerard W ^d   Wherland, Scot ^e   Pecht, Israel ^f  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

^b UNIVERSITY OF COPENHAGEN   (Denmark)

^c IMPERIAL COLLEGE LONDON   (United Kingdom)

^d LEIDEN UNIVERSITY   (Netherlands)

^e WASHINGTON STATE UNIVERSITY   (United States)

^f WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0030531089     PISSN: 03010104     EISSN: None     Source Type: Journal    
DOI: 10.1016/0301-0104(95)00294-4     Document Type: Article

References (24)

1. M.J. Clarke et al., eds., Struct. Bond. 75 (1991) 1.
2. R.A. Marcus and N. Sutin, Biochim. Biophys. Acta 811 (1985) 265.
3. O. Farver and I. Pecht, Biophys. Chem. 50 (1994) 203.
4. O. Farver and I. Pecht, in: Copper proteins and copper enzymes, Vol. 1, ed. R. Lontie (CRC Press, Boca Raton, 1984) p. 183.
5. E.N. Baker, J. Mol. Biol. 203 (1988) 1071.
6. H. Nar, A. Messerschmidt, R. Huber, M. Van de Kamp and G.W. Canters, J. Mol. Biol. 218 (1991) 427; 221 (1991) 765.
7. H. Nar, A. Messerschmidt, R. Huber, M. Van de Kamp and G.W. Canters, J. Mol. Biol. 218 (1991) 427; 221 (1991) 765.
8. (a) O. Farver and I. Pecht, Proc. Natl. Acad. Sci. USA 86 (1989) 6968;
9. (b) O. Farver and I. Pecht, J. Am. Chem. Soc. 114 (1992) 5764;
10. (c) O. Farver, L.K. Skov, M. Van de Kamp, G.W. Canters and I. Pecht, Eur. J. Biochem. 210 (1992) 399;
11. (d) O. Farver, L.K. Skov, T. Pascher, B.G. Karlsson, M. Nordling, L.G. Lundberg, T. Vänngård and I. Pecht, Biochemistry 32 (1993) 7317.
12. M. Goldberg and I. Pecht, Biochemistry 15 (1976) 4197.
13. G. Van Pouderoyen, D.M. Mazumdar, N.I. Hunt, H.A.O. Hill and G.W. Canters, Eur. J. Biochem. 222 (1994) 583.
14. G. Gilardi, G. Mei, N. Rosato, G.W. Canters and A. Finazzi-Agró, Biochemistry 33 (1994) 1425.
15. P. Dauper-Osguthorpe, V.A. Roberts, D.J. Osguthorpe, J. Wolff, M. Genest and A.T. Hagler, Proteins: Struct. Funct. Genet. 4 (1988) 31.
16. D.N. Beratan, J.N. Betts and J.N. Onuchic, Science 252 (1991) 1285.
17. M.H. Klapper and M. Faraggi, Quart. Rev. Biophys. 12 (1979) 465; M. Faraggi and M.H. Klapper, J. Am. Chem. Soc. 110 (1988) 5753.
18. M.H. Klapper and M. Faraggi, Quart. Rev. Biophys. 12 (1979) 465; M. Faraggi and M.H. Klapper, J. Am. Chem. Soc. 110 (1988) 5753.
19. J. Jortner and M. Bixon, Mol. Cryst. Liquid Cryst. 234 (1993) 29.
20. A. Broo and S. Larsson, Chem. Phys. 148 (1990) 103.
21. C.C. Moser, J.M. Keske, K. Warncke, R.S. Farid and P.L. Dutton, Nature 355 (1992) 802; R.S. Farid, C.C. Moser and P.L. Dutton, Curr. Opinion Struct. Biol. 3 (1993) 225
22. C.C. Moser, J.M. Keske, K. Warncke, R.S. Farid and P.L. Dutton, Nature 355 (1992) 802; R.S. Farid, C.C. Moser and P.L. Dutton, Curr. Opinion Struct. Biol. 3 (1993) 225
23. J.N. Onuchic, D.N. Beratan, J.R. Winkler and H.B. Gray, Annu. Rev. Biophys. Biomol. Struct. 21 (1992) 349.
24. J.J. Regan, S.M. Risser, D.N. Beratan and J.N. Onuchic, J. Phys. Chem. 97 (1993) 13083.