Abstract
The kinetics of nanosecond geminal recombination and bimolar association of molecular oxygen with the horse-heart myoglobin has been investigated by laser flash photolysis. The influence of Zn(II) ions on the dioxygenation and rebonding of myoglobin to a ligand has been considered. The kinetics of the geminal recombination was analyzed within the framework of the model of four states with a side path of ligand motion in the protein matrix. It is shown that an increase in the affinity of myoglobin to O2 in the presence of Zn(II) ions is predominantly caused by an increase in the rate constant of recombination of molecular oxygen from the primary intraprotein site.
Similar content being viewed by others
REFERENCES
J. Wittenberg, Physiol. Rev., 50, 559–636 (1970).
B. A. Springer, S. G. Sligar, J. S. Olson, and G. N. Phillips, Chem. Rev., 94, 699–714 (1994).
M. Brunori, Trends Biochem. Sci., 26, 21–23 (2001).
M. W. J. Cleeter, J. M. Cooper, V. M. Darley-Usmar, S. Moncada, and A. H. V. Schapira, FEBS Lett., 345, 50–54 (1994).
S. Herold, FEBS Lett., 443, 81–84 (1999).
Q. H. Gibson, Biochem. J., 71, 293–303 (1959).
R. H. Austin, K. W. Beeson, L. Eisenstein, H. Frauenfelder, and I. C. Gunsalus, Biochemistry, 14, 5355–5373 (1975).
E. E. Scott and Q. H. Gibson, Biochemistry, 36, 11909–11917 (1997).
G. Eichhorn (Ed.), Inorganic Biochemistry [Russian translation], Vols. 1, 2, Mir, Moscow (1978).
P. T. Manoharan, K. Alson, and J. M. Rifkind, Biochemistry, 28, 7148–7153 (1989).
E. A. Skekhovtsova, E. V. Goraev, V. S. Sivozhelezov, and G. B. Postnikov, Biofizika, 50, 39–48 (2005).
L. J. Banaszak, H. C. Watson, and J. C. Kendrew, J. Mol. Biol., 12, 130–137 (1965).
E. Breslow and F. R. N. Gurd, J. Biol. Chem., 238, 1332–1342 (1963).
J. M. Rifkind, M. H. Keyes, and R. Lumry, Biochemistry, 16, 5564–5568 (1977).
J. R. Cann, Biochemistry, 3, 714–722 (1964).
S. V. Evans and G. D. Brayer, J. Biol. Chem., 263, 4263–4268 (1988).
S. V. Lepeshkevich, J. Karpiuk, I. V. Sazanovich, and B. M. Dzhagarov, Biochemistry, 43, 1675–1684 (2004).
B. M. Dzhagarov and S. V. Lepeshkevich, Chem. Phys. Lett., 390, 59–64 (2004).
S. Hirota, T. Li, G. N. Fillips Jr, J. S. Olsen, M. Mukai, and T. Kitagawa, J. Am. Chem. Soc., 118, 7845–7846 (1996).
M. D. Chatfeld, K. N. Walda, and D. Magde, J. Am. Chem. Soc., 112, 4680–4687 (1990).
X. Ye, A. Demidov, and P. M. Champion, J. Am. Chem. Soc., 124, 5914–5924 (2002).
B. M. Dzhagarov, V. A. Galievskii, N. N. Kruk, and M. D. Yakutovich, Dokl. Ross. Akad. Nauk, 366, 121–124 (1999).
E. E. Scott, Q. H. Gibson, and J. S. Olson, J. Biol. Chem., 276, 5177–5188 (2001).
K. Nienhaus, P. Deng, J. S. Olson, J. J. Warren, and G. U. Nienhaus, J. Biol. Chem., 278, 42532–42544 (2003).
R. Elber and M. Karpius, J. Am. Chem. Soc., 112, 9161–9175 (1990).
R. F. Tilton, Jr, I. D. Kuntz, Jr, and G. A. Petsko, Biochemistry, 23, 2849–2857 (1984).
D. Bourgeois, B. Vallone, F. Schotte, A. Arcovito, A. E. Miele, G. Sciara, M. Wulff, P. Anfinrud, and M. Brunoni, Proc. Natl. Acad. Sci. USA, 100, 8704–8709 (2003).
S. Franzen, B. Bohr, C. Poyart, and J. L. Martin, Biochemistry, 34, 1224–1237 (1995).
U. Samuni, D. Dantsker, A. Ray, J. B. Wittenberg, B. A. Wittenberg, D. Dewilde, L. Moens, Y. Oucllet, M. Guertin, and J. M. Friedman, J. Biol. Chem., 278, 27241–27250 (2003).
D. G. Lambright, S. Balasubramanian, S. M. Decatur, and S. G. Boxer, Biochemistry, 33, 5518–5525 (1994).
Author information
Authors and Affiliations
Corresponding author
Additional information
__________
Translated from Zhurnal Prikladnoi Spektroskopii, Vol. 72, No. 5, pp. 670–677, September–October, 2005.
Rights and permissions
About this article
Cite this article
Lepeshkevich, S.V., Poznyak, A.L. & Dzhagarov, B.M. Influence of Zinc Ions on the Geminal and Bimolecular Stages of the Horse-Myoglobin Oxygenation. J Appl Spectrosc 72, 735–743 (2005). https://doi.org/10.1007/s10812-005-0141-2
Received:
Issue Date:
DOI: https://doi.org/10.1007/s10812-005-0141-2