Essentiality of the Active-site Arginine Residue for the Normal Catalytic Activity of Cu,Zn Superoxide Dismutase

Overview

Journal Biochem J

Specialty Biochemistry

Date 1985 Sep 15

PMID 4062877

Citations 6

Authors

C L Borders Jr

J E Saunders

D M Blech

I Fridovich

Affiliations

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Abstract

Chemical modification of bovine and yeast Cu,Zn superoxide dismutases with phenylglyoxal diminishes the catalytic activities by greater than or equal to 98%, and treatment of these enzymes with butanedione plus borate leads to greater than or equal to 96% inactivation. The activity loss is accompanied by the modification of less than two arginine residues per subunit with no concomitant loss of Cu or Zn. The phenylglyoxal-modified enzymes require at least a 20-fold greater concentration of cyanide for 50% inhibition than do the corresponding native enzymes. Polyacrylamide-gel electrophoresis and activity staining of the phenylglyoxal-inactivated enzymes demonstrate that the residual activity is largely associated with modified forms that bear lower net positive charge than the native superoxide dismutases.

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