A study of biomimetic system: Exploration of factors modulating the catalytic capacity of glutathione peroxidase mimics

Journal of Molecular Catalysis A: Chemical

Volumn 277, Issue 1-2, 2007, Pages 193-201

  Dong, Zeyuan ^a   Liang, Kai ^a   Wang, Chunyu ^a   Huang, Xin ^a   Mao, Shizhong ^a   Li, Xiangqiu ^a   Xu, Jiayun ^a   Liu, Junqiu ^a   Luo, Guimin ^a   Shen, Jiacong ^a  

^a JILIN UNIVERSITY   (China)

Author keywords

Cyclodextrin; Glutathione peroxidases; Hydrophobic interaction; Mimics; Recognition

Indexed keywords

BINDING SITES; CATALYST ACTIVITY; CYCLODEXTRINS; ENZYME INHIBITION; SUBSTRATES;

CATALYTIC CAPACITY; ENZYME MIMICS; GLUTATHIONE PEROXIDASES; SINGLE RECOGNITIONS;

BIOMIMETICS;

EID: 35348819925     PISSN: 13811169     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcata.2007.08.003     Document Type: Article

References (55)

1. Girotti A.W. J. Lipid Res. 39 (1998) 1529
2. Chaudiere J., and Ferrari-Iliou R. Food Chem. Toxicol. 37 (1999) 949
3. Sies H. Oxidative Stress (1985), Academic Press, London
4. Rice-Evans C., Halliwell B., and Lunt G.G. Free Radicals and Oxidative Stress: Environment, Drugs and Food Additives (1995), Portland Press, London
5. Sies H. Exp. Physiol. 82 (1997) 291
6. Sies H. Eur. J. Biochem. 215 (1993) 213
7. Klotz L.-O., Kroncke K.-D., Buchczyk D.P., and Sies H.J. Nutrition 133 (2003) 1448
8. Ursini F., Maiorino M., Brigelius-Flohé R., Aumann K.D., Roveri A., Schomburg D., and Flohé L. Methods Enzymol. 252 (1995) 38
9. Burk R.F. Selenium in Biology and Human Health (1994), Springer, New York
10. Flohé L. Curr. Top. Cell Regul. 27 (1985) 473
11. Tappel A.L. Curr. Top. Cell. Regul. 24 (1984) 87
12. Flohé L., Loschen G., Günzler W.A., and Eichele E. Hoppe-Seyler's Z. Physiol. Chem. 353 (1972) 987
13. Stadtman T.C. J. Biol. Chem. 266 (1991) 16257
14. Mugesh G., du Mont W.-W., and Sies H. Chem. Rev. 101 (2001) 2125
15. Epp O., Ladenstein R., and Wendel A. Eur. J. Biochem. 133 (1983) 51
16. Ren B., Huang W., Åkesson B., and Ladenstein R. J. Mol. Biol. 268 (1997) 869
17. Karen L., House R., Dunlap B., Odom J.D., Wu Z.-P., and Hilvert D. J. Am. Chem. Soc. 114 (1992) 8573
18. Iwaoka M., and Tomoda S. J. Am. Chem. Soc. 116 (1994) 2557
19. Mugesh G., Panda A., Singh H.B., Punekar N.S., and Butcher R.J. J. Am. Chem. Soc. 123 (2001) 839
20. Mugesh G., and Singh H.B. Chem. Soc. Rev. 29 (2000) 347
21. Luo G., Ren X., Liu J., Mu Y., and Shen J. Curr. Med. Chem. 10 (2003) 1151
22. Dong Z., Liu J., Mao S., Huang X., Yang B., Ren X., Luo G., and Shen J. J. Am. Chem. Soc. 126 (2004) 16395
23. Mao S., Dong Z., Liu J., Li X., Liu X., Luo G., and Shen J. J. Am. Chem. Soc. 127 (2005) 11588
24. Yu H., Liu J., Bo{combining double acute accent}ck A., Li J., Luo G., and Shen J. J. Biol. Chem. 280 (2005) 11930
25. Dong Z., Huang X., Mao S., Liang K., Liu J., Luo G., and Shen J. Chem. Eur. J. 12 (2006) 3575
26. Breslow R., and Dong S.D. Chem. Rev. 98 (1998) 1997
27. Murakami Y., Kikuchi J.I., Hisaeda Y., and Hayashida O. Chem. Rev. 96 (1996) 72
28. Szejtli J. Chem. Rev. 98 (1998) 1743
29. Breslow R., and Zhang B.L. J. Am. Chem. Soc. 119 (1997) 1676
30. Breslow R., Greenspoon N., Guo T., and Zarzycki R. J. Am. Chem. Soc. 111 (1989) 8296
31. Cacciapaglia R., Stefano S.D., and Mandolini L. Examples of some catalytic receptors recognizing double substates by hydrogen-bonding interactions. Acc. Chem. Res. 37 (2004) 113
32. Iwaoka M., and Tomoda S. J. Am. Chem. Soc. 118 (1996) 8077
33. You Y., Ahsan K., and Detty M.R. J. Am. Chem. Soc. 125 (2003) 4918
34. Ren X., Xue Y., Liu J., Zhang K., Zheng J., Luo G., Guo C., Mu Y., and Shen J. Chem. BioChem. 3 (2002) 356
35. Dong Z., Liu J., Mao S., Huang X., Luo G., and Shen J. J. Incl. Phenom. Macro. 56 (2006) 179
36. McNaughton M., Engman L., Birmingham A., Powis G., and Cotgreave I.A. J. Med. Chem. 47 (2004) 233
37. Dong Z., Li X., Liang K., Mao S., Huang X., Yang B., Liu J., Luo G., and Shen J. J. Org. Chem. 72 (2007) 606
38. Silver M. Methods Enzymol. 62D (1979) 135
39. Wu Z.P., and Hilvert D. J. Am. Chem. Soc. 112 (1990) 5647
40. Bell I.M., Fisher M.L., Wu Z.P., and Hilvert D. Biochemistry 32 (1993) 3754
41. MIS., Molecular Simulation, Inc., Currently Accelrys Inc., San Diego, CA, 1999.
42. U. Dinur, A.T. Hagler, In Reviews in Computational Chemistry; K.B. Lipkowitz, D.B. Boyd, Ed.; VCH Publishers: New York, 1991; Vol. 2, p. 99.
43. Comba P., and Hambley T.W. Molecular Modeling (1995), Weinheim, New York
44. Engman L., Stern D., Pelcman M., and Andersson C.M. J. Org. Chem. 59 (1994) 1973
45. Kanda T., Engman L., Cotgreave I.A., and Powis G. J. Org. Chem. 64 (1999) 8161
46. Wilson S.R., Zucker P.A., Huang R.-R.C., and Spector A. J. Am. Chem. Soc. 111 (1989) 5936
47. Svensson R., Pamedytytė V., Juodaitytė J., Makuška R., and Morgenstern R. Toxicology 168 (2001) 251
48. Dwars T., Paetzold E., and Oehme G. Angew. Chem., Int. Ed. 44 (2005) 7174
49. Huang X., Dong Z., Liu J., Mao S., Xu J., Luo G., and Shen J. Langmuir 23 (2007) 1518
50. Huang X., Dong Z., Liu J., Mao S., Xu J., Luo G., and Shen J. Macromol. Rapid Commun. 27 (2006) 2101
51. Sarma B.K., and Mugesh G. J. Am. Chem. Soc. 127 (2005) 11477
52. Oshikiri T., Takashima Y., Yamaguchi H., and Harada A. J. Am. Chem. Soc. 127 (2005) 12186
53. Takebe G., Yarimizu J., Saito Y., Hayashi T., Nakamura H., Yodoi J., Nagasawa S., and Takahashi K. J. Bio. Chem. 277 (2002) 41254
54. Flohé L., Günzler W.A., Jung G., Schaich E., and Schneider F. Hoppe-Seyler's Z. Physiol. Chem. 352 (1971) 159
55. Flohé L. In: Dolphin D., Poulson R., and Avamovic O. (Eds). Glutathione: Chemical, Biochemical, and Medical Aspects (1989), Wiley, New York 644