Folding of deoxymyoglobin triggered by electron transfer

Journal of Physical Chemistry A

Volumn 102, Issue 28, 1998, Pages 5599-5601

  Wittung Stafshede, Pernilla ^a   Malmström, Bo G ^a,b   Winkler, Jay R ^a   Gray, Harry B ^a  

^a CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

^b UNIVERSITY OF GOTHENBURG   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 9244259984     PISSN: 10895639     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp9802228     Document Type: Article

References (20)

1. Pascher, T.; Chesick, J. P.; Winkler, J. R.; Gray, H. B. Science 1996, 271, 1558.
2. Mines, G. A.; Pascher, T.; Lee, S. C.; Winkler, J. R.; Gray, H. B. Chem. Biol. 1996, 3, 491.
3. Wittung-Stafshede, P.; Gray, H. B.; Winkler, J. R. J. Am. Chem. Soc. 1997, 119, 9562.
4. Antonini, E.; Brunori, M. Hemoglobin and Myoglobin in their Reactions with Ligands; North-Holland Publishing Co. : Amsterdam, 1971.
5. Hargrove, M. S.; Olson, J. S. Biochemistry 1996, 35, 11310.
6. Telford, J. R.; Tezcan, F. A.; Gray, H. B.; Winkler, J. R. To be submitted for publication.
7. Orii, Y. Biochemistry 1993, 32, 11910.
8. Ballew, R. M.; Sabelko, J.; Gruebele, M. Nature Struct. Biol. 1996, 3, 923.
9. Jennings, P. A.; Wright, P. E. Science 1993, 262, 892.
10. Gilmanshin, R.; Williams, S.; Callender, R. H.; Woodruff, W. H.; Dyer, R. B. Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 3709.
11. Chiba, K.; Ikai, A.; Kawamura-Konishi, Y.; Kihara, H. Proteins 1994, 19, 110.
12. Elizir, D.; Chiba, K.; Tsuruta, H.: Doniach, S.; Hodgson, K. O.; Kihara, H. Biophys. J. 1993, 65, 912.
13. Stowell, M. B. H.; Larsen, R. W.; Winkler, J. R.; Rees, D. C.; Chan, S. I. J. Phys. Chem. 1993, 97, 3054.
14. Lieber, C. M.; Karas, J. L.; Gray, H. B. J. Am. Chem. Soc. 1987, 109, 2778.
15. Churg, A. L.; Warshel. A. Biochemistry 1986, 25, 1675.
16. Dixon, D. W.; Hong, X.; Woehler, S. E. Biophys. J. 1989, 56, 339.
17. Wittung-Stafshede, P.; Hill, M. G.; Gomez, E.; DiBilio, A.; Karlsson, B. G.; Leckner, J.; Winkler, J. R.; Gray, H. B.; Malmström, B. G. JBIC 1997. In press.
18. Hamada, K.; Bethge, P. H.; Mathews, F. S. J. Mol. Biol. 1995, 247, 947.
19. Takano, T.; Dickerson, R. E. J. Mol. Biol 1981, 153, 79.
20. Minor differences between steady-state and time-resolved spectra are due to the presence of dithionite used as a reductant, and to the fact that, upon photochemical reduction, only 20-25% of the protein refolds.