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Rapid and irreversible inhibition of creatine kinase by peroxynitrite. FEBS Lett 1998 May 08;427(2):171-4

Date

06/02/1998

Pubmed ID

9607305

DOI

10.1016/s0014-5793(98)00413-x

Scopus ID

2-s2.0-0032496422 (requires institutional sign-in at Scopus site)   140 Citations

Abstract

We examined the ability of peroxynitrite and other .NO-derived oxidants to inhibit creatine kinase (CK). Peroxynitrite potently inhibited CK activity and depleted protein thiols. The rate constant for this reaction was 8.85x10(5) M(-1) s(-1). Glutathione did not reactivate CK activity nor did it regenerate protein thiol content. In contrast, glutathione reactivated CK, and regenerated protein thiols, after inhibition by either .NO or oxidized glutathione (GSSG). Peroxynitrite did not irreversibly inhibit CK after it had been treated with GSSG to block protein thiols. We conclude that thiol oxidation is a critical event leading to inactivation of CK by peroxynitrite.

Author List

Konorev EA, Hogg N, Kalyanaraman B

Authors

Neil Hogg PhD Associate Dean, Professor in the Biophysics department at Medical College of Wisconsin
Balaraman Kalyanaraman PhD Professor in the Biophysics department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Acetonitriles
Animals
Creatine Kinase
Enzyme Activation
Enzyme Inhibitors
Enzyme Reactivators
Glutathione
Glutathione Disulfide
Kinetics
Molsidomine
Morpholines
Nitrates
Nitric Oxide
Oxidants
Rabbits
Sulfhydryl Compounds
Superoxides