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PMID: 16005861 Published · ppublish English Journal Article Review

Protein S-nitrosation: biochemistry and characterization of protein thiol-NO interactions as cellular signals.

Clinical biochemistry ·Vol. 38 ·No. 9 ·2005-09-00 ·Pages 777-91

Miersch S, Mutus B

Abstract

The interaction of nitric oxide with thiols is complex and still an active area of research. Herein, we provide an overview of the ways in which nitric oxide can be biologically transformed into species capable of adding an NO moiety to protein sulfhydryls, emphasizing how protein S-nitrosation differs from nitrosation of low molecular weight thiols. Protein S-nitrosation is being revealed as a post-translational means of chemically modifying and functionally altering proteins. Changes in protein function, which persist on a physiologically relevant time scale, effectively transmit biological signals and thus provide a framework for elucidating signaling networks. A description of recently developed methodology facilitating inquiry into this area is provided, along with a sketch of various proteins reported to be targets for nitrosation and the functional consequences therein. Protein denitrosation appears to be an active and perhaps enzymatically catalyzed process. Here, we summarize the evidence that suggests this and proffer a précis of proteins possessing denitrosation activity.

MeSH Terms
Humans Nitric Oxide/chemistry,metabolism Nitrosation Proteins/chemistry,metabolism Signal Transduction Sulfhydryl Compounds/chemistry,metabolism
Chemicals
Proteins Sulfhydryl Compounds Nitric Oxide
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Miersch Shane
Department of Chemistry and Biochemistry, University of Windsor, 401 Sunset Avenue, Windsor, Ontario, Canada N9B 3P4.
Mutus Bulent
Article Info
Journal
Clinical biochemistry
Abbr.
Clin Biochem
ISSN
0009-9120
Published
2005-09-00
Pages
777-91
Language
English
Region
United States
NLM ID
0133660
Subset
IM
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