Rapid and irreversible inhibition of creatine kinase by peroxynitrite. FEBS Lett 1998 May 08;427(2):171-4
Date
06/02/1998Pubmed ID
9607305DOI
10.1016/s0014-5793(98)00413-xScopus ID
2-s2.0-0032496422 (requires institutional sign-in at Scopus site) 140 CitationsAbstract
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 BAuthors
Neil Hogg PhD Associate Dean, Professor in the Biophysics department at Medical College of WisconsinBalaraman Kalyanaraman PhD Professor in the Biophysics department at Medical College of Wisconsin
MESH terms used to index this publication - Major topics in bold
AcetonitrilesAnimals
Creatine Kinase
Enzyme Activation
Enzyme Inhibitors
Enzyme Reactivators
Glutathione
Glutathione Disulfide
Kinetics
Molsidomine
Morpholines
Nitrates
Nitric Oxide
Oxidants
Rabbits
Sulfhydryl Compounds
Superoxides