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

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...

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Published in中国科学通报:英文版 no. 24; pp. 2081 - 2085
Main Author 李培峰 方允中 涂光忠
Format Journal Article
LanguageEnglish
Published 1994
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Summary: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
Bibliography:11-1785/N
LI Pei-Feng FANG Yun-Zhong(Beijing Institute of Radiation Medicine, Beijing 100850, PRC)and TU Guang-Zhong(Beijing Institute of Microchemistry, Beijing 100091, PRC)
ISSN:1001-6538
1861-9541