Evidence of His61 imidazolate bridge rupture in reduced crystalline Cu,Zn superoxide dismutase

被引:24
作者
Ascone, I
Castañer, R
Tarricone, C
Bolognesi, M
Stroppolo, ME
Desideri, A
机构
[1] Univ Paris 11, Utilisat Rayonnement Electromagnet Lab, Fac Orsay, F-91405 Orsay, France
[2] Univ Pavia, Dip Genet & Microbiol, I-27100 Pavia, Italy
[3] Univ Genoa, INFM, I-16146 Genoa, Italy
[4] Univ Genoa, Ctr Biotecnol Avanzate, I-16146 Genoa, Italy
[5] Univ Rome Tor Vergata, Dept Biol, I-00173 Rome, Italy
关键词
bovine Cu; Zn superoxide dismutase; XAS; copper co-ordination; redox states; bridging ligands;
D O I
10.1006/bbrc.1997.7777
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
X-ray absorption spectroscopy has been carried out on the copper K edge in oxidized and reduced bovine Cu,Zn SOD in solution and in crystalline state. The results indicate that the copper coordination geometry is unaffected by the solution or by the crystalline state of the protein, in both oxidation states. Moreover the two oxidation states of the active copper ion are reflected under, all the experimental conditions, by distinct coordination spheres around the catalytic metal, which is four-coordinated and three-coordinated in the Cu(II) and in the Cu(I) enzyme, respectively. (C) 1997 Academic Press.
引用
收藏
页码:119 / 121
页数:3
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