REDUCED ANION-BINDING AFFINITY OF CU,ZN SUPEROXIDE DISMUTASES CHEMICALLY MODIFIED AT ARGININE

被引：40

作者：

BERMINGHAMMCDONOGH, O

DEFREITAS, DM

KUMAMOTO, A

SAUNDERS, JE

BLECH, DM

BORDERS, CL

VALENTINE, JS

机构：

[1] UNIV CALIF LOS ANGELES, DEPT CHEM & BIOCHEM, LOS ANGELES, CA 90024 USA

[2] UNIV CALIF LOS ANGELES, INST MOLEC BIOL, LOS ANGELES, CA 90024 USA

[3] COLL WOOSTER, DEPT CHEM, WOOSTER, OH 44691 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1982年 / 108卷 / 04期

关键词：

D O I：

10.1016/S0006-291X(82)80058-2

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 spectroscopic and anion-bining properties of bovine and yeast Cu,Zn superoxide dismutases which were chemically modified at 1 arginine/subunit by phenylglyoxal were studied. This modification is known to inactivate these proteins as superoxide dismutases. The visible absorption and ESR spectra of the modified proteins are consistent with a shift toward a more nearly axial coordination geometry about Cu(II) and the affinities of these proteins for the anions CN-, N3-, NCS- and NCO- are substantially reduced.

引用

页码：1376 / 1382

页数：7

共 23 条

[1] SUPEROXIDE DISMUTASE-THIOCYANATE - A STUDY OF THE BINDING-SITES OF ANIONS ON COPPER(II) IN SUPEROXIDE-DISMUTASE [J].