Conversion of S-phenylsulfonylcysteine residues to mixed disulfides at pH 4.0: utility in protein thiol blocking and in protein-S-nitrosothiol detection-Reference-Cited by-同舟云学术

Conversion of S-phenylsulfonylcysteine residues to mixed disulfides at pH 4.0: utility in protein thiol blocking and in protein-S-nitrosothiol detection

Published:2014 Issue:40 Volume:12 Page:7942-7956
ISSN:1477-0520
Container-title:Org. Biomol. Chem.
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Reeves B. D.¹²³,Joshi N.¹²³,Campanello G. C.⁴⁵⁶,Hilmer J. K.¹²³,Chetia L.¹²³,Vance J. A.¹²³,Reinschmidt J. N.¹²³,Miller C. G.¹²³,Giedroc D. P.⁴⁵⁶,Dratz E. A.¹²³,Singel D. J.¹²³,Grieco P. A.¹²³

Affiliation:

1. Department of Chemistry and Biochemistry

2. Montana State University

3. Bozeman, USA

4. Department of Chemistry

5. Indiana University

6. Bloomington, USA

Abstract

A protocol denoted as the thiosulfonate switch featuring sequential protein thiol blocking and conversion of protein-S-nitrosothiols to mixed disulfides bearing a fluorescent probe at pH 4.0 is reported.

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2014/OB/C4OB00995A

Reference61 articles.

1. Protein S-nitrosylation: purview and parameters

2. S-nitrosylation of proteins with nitric oxide: synthesis and characterization of biologically active compounds.

3. The Chemical Biology of S-Nitrosothiols

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

5. S-Nitrosylation signaling regulates cellular protein interactions

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