Elucidation of the mechanism of selenoprotein glutathione peroxidase (GPx)-catalyzed hydrogen peroxide reduction by two glutathione molecules: A density functional study

Biochemistry

Volumn 44, Issue 35, 2005, Pages 11864-11871

  Prabhakar, Rajeev ^a   Vreven, Thorn ^b   Morokuma, Keiji ^a   Musaev, Djamaladdin G ^a  

^a EMORY UNIVERSITY   (United States)

^b GAUSSIAN INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; HYDROGEN PEROXIDE; KETONES; PROTONS;

CATALYTIC MECHANISM; GLUTATHIONE;

PROTEINS;

DISULFIDE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; OXYGEN; SELENOPROTEIN; WATER;

ARTICLE; CATALYSIS; CHEMICAL REACTION; DENSITY FUNCTIONAL THEORY; ENERGY; ENZYME ACTIVITY; PRIORITY JOURNAL; PROTON TRANSPORT; REACTION ANALYSIS;

CATALYSIS; DISULFIDES; GLUTATHIONE; GLUTATHIONE PEROXIDASE; HYDROGEN PEROXIDE; MODELS, CHEMICAL; OXIDATION-REDUCTION; QUANTUM THEORY; SELENIUM COMPOUNDS;

EID: 24344490265     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050815q     Document Type: Article

References (31)

1. Combs, G. F., Jr., and Lü, J. (2001) Selenium Its Molecular Biology ami Role in Human Health (Hatfield, D. L., Ed.) p 205, Kluwer Academic Publishers, Boston, MA.
2. Zhao, L., Cox, A. G., Ruzicka, J. A., Bhat, A. A., Zhang, W., and Taylor, E. W. (2000) Molecular modeling and in vitro activity of an HIV-1-encoded glutathione peroxidase, Proc. Natl. Acad. Sci. U.S.A. 97, 6356.
3. Birringer, M., Pilawa, S., and Flohè, L. (2002) Trends in selenium chemistry, Nat. Prod. Rep. 19, 693-718.
4. Mills, G. C. (1957) Hemoglobin catabolism. 1. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown, J. Biol. Chem. 229, 189-197.
5. Flohè, L. (1989) Glutathione (Dolphin, D., Avramovic, O., and Poulson, R., Eds.) pp 644-731, John Wiley and Sons, New York, 1989.
6. Björnstedt, M., Xue, J., Huang, W., Akesson, B., and Holmgren, A. (1994) The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase, J. Biol. Chem. 269, 29382.
7. Godeas, C., Sandri, G., and Panfili, E. (1994) Distribution of phospholipid hydroperoxide glutathione peroxidase (PHGPx) in rat testis mitochondria, Biochim. Biophys. Acta 1191, 147.
8. Roveri, A., Ursini, F., Flohé, L., and Maiorino, M. (2001) PHGPx and spermatogenesis, Biofactors 14, 213.
9. Epp, O., Ladenstein, R., and Wendel, A. (1983) The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution, Eur. J. Biochem. 133, 51-69.
10. Ren, B., Huang, W., Åkesson, B., and Ladenstein, R. (1997) The crystal structure of seleno-glutathione peroxidase from human plasma at 2.9 Å resolution, J. Mol. Biol. 268, 869-885.
11. Prohaska, J. R., Oh, S. H., Hoekstra, W. G., and Ganther, H. E. (1977) Glutathione peroxidase: Inhibition by cyanide and release of selenium, Biochem. Biophys. Res. Commun. 74, 64-71.
12. Forstrom, J. W., Zakowski, J. J., and Tappel, A. L. (1978) Identification of the catalytic site of rat liver glutathione peroxidase as selenocysteine, Biochemistry 17, 2639-2644.
13. Wendel, A., Pilz, W., Ladenstein, R., Sawatzki, G., and Weser, U. (1975) Substrate-induced redox change of selenium in glutathione peroxidase studied by X-ray photoelectron spectroscopy, Biochim. Biophys. Acta 377, 211-215.
14. Ladenstein, R., Epp, O., Bartels, K., Jones, A., Huber, R., and Wendel, A. (1979) Structure analysis and molecular model of the selenoenzyme glutathione peroxidase at 2.8 Å resolution, J. Mol. Biol. 134, 199-218.
15. Kraus, R. J., and Ganther, H. E. (1980) Reaction of cyanide with glutathione peroxidase, Biochem. Biophys. Res. Commun. 96, 1116-1122.
16. Ursini, F., Maiorino, M., Brigelius-Flohé, R., Aumann, K. D., Roveri, A., Schomburg, D., and Flohé, L. (1995) Diversity of glutathione peroxidases, Methods Enzymol. 252, 38-53.
17. Sies, H., and Masumoto, H. (1997) Ebselen as a glutathione peroxidase mimic and as a scavenger of peroxynitrite, Adv. Pharmacol. 38, 229-246.
18. Musaev, D. G., and Hirao, K. (2003) Reactivity of [1,2-benzisotellurazol- 3(2H)-one] with peroxynitrous acid: Comparison with Ebselen analogues, J. Phys. Chem. A 107, 9984-9990.
19. Musaev, D. G., Geletii, Y. V., Hill, C. L., and Hirao, K. (2003) Can the Ebselen derivatives catalyze the isomerization of peroxynitrite to nitrate? J. Am. Chem. Soc. 125, 3877-3888.
20. Flohé, L., Loschen, G., Gunzler, W. A., and Eichele, E. (1972) Glutathione peroxidase, V. The kinetic mechanism, Hoppe-Seyler's Z. Physiol. Chem. 353, 987-999.
21. Roy, G., Nethaji, M., Mugesh, G. (2004) Biomimetic studies on anti-thyroid drugs and thyroid hormone synthesis, J. Am. Chem. Soc. 126, 2712-2713.
22. Mugesh, G., du Mont, W., and Sies, H. (2001) Chemistry of biologically important synthetic organoselenium compounds, Chem. Rev. 101, 2125-2179.
23. Frisch, M. J. et al. (2004) Gaussian 03 (revision C1), Gaussian, Inc., Pittsburgh, PA.
24. Becke, A. D. (1988) Density-functional exchange-energy approximation with correct asymptotic behavior, Phys. Rev. A 38, 3098-3100.
25. (b) Lee, C., Yang, W., and Parr, R. G. (1988) Development of the Colle-Salvetti correlation energy formula into a functional of the electron density, Phys. Rev. B 37, 785-789.
26. (c) Becke, A. D. J. (1993) Density-functional thermochemistry. III. The role of exact exchange, Chem. Phys. 98, 5648-5652.
27. Siegbahn, P. E. M., and Blomberg, M. R. A. (2000) Transition-metal systems in biochemistry studied by high-accuracy quantum chemical methods, Chem. Rev. 100, 421-437.
28. Cances, E., Mennucci, B., and Tomasi, J. (1997) A new integral equation formalism for the polarizable continuum model: Theoretical background and applications to isotropic and anisotropic dielectrics, J. Chem. Phys. 107, 3032-3041.
29. Prabhakar, R., Musaev, D. G., Khavrutskii, I. V., and Morokuma, K. (2004) Does the active site of mammalian glutathione peroxidase (GPx) contain water molecules? An ONIOM study, J. Phys. Chem. B 108, 12643-12645.
30. Prabhakar, R., Blomberg, M. R. A., and Siegbahn, P. E. M. (2000) A density functional theory study of a concerted mechanism for proton exchange between amino acid side chains and water, Theor. Chem. Acc. 104, 461-470.
31. Barondeau, D. P., Kassmann, C. J., Bruns, C. K., Tainer, J. A., and Getzoff, E. D. (2004) Nickel superoxide dismutase structure and mechanism, Biochemistry 43, 8038-8047.