Effect of Reactive Oxygen Species on Structure of CuZn-SOD by 1HNMR

被引:0
作者
李培峰
方允中
涂光忠
机构
[1] BeijingInstituteofRadiationMedicine,Beijing,PRC,BeijingInstituteofRadiationMedicine,Beijing,PRC,BeijingInstituteofMicrochemistry,Beijing,PRC
关键词
HNMR; reactive oxygen species; cupro-zinc superoxide dismutase;
D O I
暂无
中图分类号
Q945 [植物生理学];
学科分类号
0903 ;
摘要
<正> 1 Introduction Cupro-zlnc superoxide dlsmutase(CuZn-SOD)1s a dimeric enzyme,inade of two identical SUbunits,each contai ning a Cu(Ⅱ)ion and a Zn(Ⅱ)ion.His44,His46,His61,His118 and one molecule of H2O are involved in the binding of Cu(Ⅱ),while His61,His69,His78 and ASP81 coordinate to Zn(Ⅱ). A great deal of evidence indicates that CuZnSOD is resistant to many chemical reagents or phySical treatment,whereas itis quite susceptible to reactiVe OXygen species SUCh as H2O2 or ascorbate-Fe(Ⅲ)system,demonstrating inactivation and physicochernical properties alterations.It is of biological significance to study the inactiVation mechanism of CuZn-SOD by reactive Oxygen species,because the enzyme plays an important role in disproportioning superoxide radical(O2?),thus preventing the damaging effect of O2? or its derivatives on biomacromolecules.A seties of studies has focused on tbe
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页码:2081 / 2085
页数:5
相关论文
共 13 条
[1]  
Blech D M,Borders CL Jr.H ydroperoxide anion,H O 2,is and affinity gentfor inactivation ofyheast cn/zn superoxide dism utase m odification of histreaidenepersubunit. A rch Biochem Biophys . 1983
[2]  
Richardson, J. S,Thomas, K. A,Rubin, B. H. et al. Proceedings of the National Academy of Sciences of the United States of America . 1975
[3]  
Li, P. F,Fang, Y. Z,Li, Y. Z. Medical Science Research . 1993
[4]  
Li, P. F,Fang, Y. Z,Li, Y. Z. Medical Science Research . 1993
[5]  
McCord, J. M,Fridovich, I. Journal of Biological Chemistry . 1969
[6]  
Fang ZY,Li WJ.Free Radical and Enzyme. . 1989
[7]  
Anthony, E. G,Cass, H,Allen, O. et al. Biochemical Journal . 1977
[8]  
Paci,M,Desideri,A,Sette,M,Ciriolo,MR,Rotilio,G.Assignment of imidazole resonances from two-dimensional proton NMR spectra of bovine Cu, Zn superoxide dismutase. Evidence for similar active site conformation in the oxidized and reduced enzyme. FEBS Letters . 1990
[9]  
Li, Y. X,Fang, Y. Z. Progress in Biochemistry and Biophysics . 1983
[10]  
Anthony, E. G,Cass, H,Allen, O. et al. Biochemical Journal . 1979