Modification of creatine kinase by S-nitrosothiols: S-nitrosation vs. S-thiolation. Free Radic Biol Med 2000 Jun 01;28(11):1671-8
Date
08/12/2000Pubmed ID
10938464DOI
10.1016/s0891-5849(00)00281-1Scopus ID
2-s2.0-0034209724 (requires institutional sign-in at Scopus site) 68 CitationsAbstract
Creatine kinase is reversibly inhibited by incubation with S-nitrosothiols. Loss of enzyme activity is associated with the depletion of 5,5'-dithiobis (2-nitrobenzoic acid)-accessible thiol groups, and is not due to nitric oxide release from RSNO. Full enzymatic activity and protein thiol content are restored by incubation of the S-nitrosothiol-modified protein with glutathione. S-nitroso-N-acetylpenicillamine, which contains a more sterically hindered S-nitroso group than S-nitrosoglutathione, predominantly modifies the protein thiol to an S-nitrosothiol via a transnitrosation reaction. In contrast, S-nitrosoglutathione modifies creatine kinase predominantly by S-thiolation. Both S-nitroso-N-acetylpenicillamine and S-nitrosoglutathione modify bovine serum albumin to an S-nitroso derivative. This indicates that S-thiolation and S-nitrosation are both relevant reactions for S-nitrosothiols, and the relative importance of these reactions in biological systems depends on both the environment of the protein thiol and on the chemical nature of the S-nitrosothiol.
Author List
Konorev EA, Kalyanaraman B, Hogg NAuthors
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
AnimalsCattle
Creatine Kinase
Enzyme Inhibitors
Free Radicals
Glutathione
In Vitro Techniques
Nitroso Compounds
Penicillamine
Rabbits
S-Nitroso-N-Acetylpenicillamine
S-Nitrosoglutathione
Serum Albumin, Bovine
Sulfhydryl Compounds
