ADVANCES IN THE UNDERSTANDING OF THE STRUCTURE-FUNCTION RELATIONSHIP IN CU,ZN SUPEROXIDE-DISMUTASE

被引：18

作者：

BANCI, L

BERTINI, I

CABELLI, DE

HALLEWELL, RA

LUCHINAT, C

VIEZZOLI, MS

机构：

[1] UNIV FLORENCE, DEPT CHEM, VIA G CAPPONI 7, I-50121 FLORENCE, ITALY

[2] BROOKHAVEN NATL LAB, UPTON, NY 11973 USA

[3] UNIV BOLOGNA, INST AGR CHEM, I-40126 BOLOGNA, ITALY

[4] CHIRON CORP, EMERYVILLE, CA 94608 USA

来源：

FREE RADICAL RESEARCH COMMUNICATIONS | 1991年 / 12-3卷

关键词：

SUPEROXIDE DISMUTASE; METALLO PROTEIN; COPPER; ZINC; MUTANTS; SITE-DIRECTED MUTAGENESIS; ELECTROSTATIC EFFECTS;

D O I：

10.3109/10715769109145792

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：

The structure-function relationship in Cu,Zn superoxide dismutase has been partially elucidated by the combined use of many spectroscopic techniques (electronic spectroscopy, circular dichroism. EPR and NMR) and site-directed mutagenesis techniques. The comparison of the spectroscopic and catalytic properties of various mutants, in which some active site residues have been substituted through site-directed mutagenesis, allowed us to establish that the activity is in general more sensitive to electrostatic effects rather than to steric effects or changes in the copper hydration or coordination geometry. © 1991 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted.

引用

页码：239 / 251

页数：13

共 36 条

[1] WATER IN THE ACTIVE CAVITY OF COPPER-ZINC SUPEROXIDE-DISMUTASE - A WATER H-1-NUCLEAR-MAGNETIC-RELAXATION-DISPERSION STUDY [J].