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The role of sulfenic acids in cellular redox signaling: Reconciling chemical kinetics and molecular detection strategies.
Arch Biochem Biophys. 2017 02 15; 616:40-46.AB

Abstract

The reversible oxidation of protein cysteine residues is well recognized as an important regulatory mechanism in redox-dependent cell signaling. Cysteine oxidation is diverse in nature and involves various post-translational modifications (sulfenic acids, disulfides, etc.) and the specific functional or structural impact of these specific oxidative events is still poorly understood. The proximal product of protein cysteine oxidation by biological reactive oxygen species (ROS) is sulfenic acid (Cys-SOH), and experimental evidence is accruing for the formation of Cys-SOH as intermediate in protein cysteine oxidation in various biological settings. However, the plausibility of protein Cys-SH oxidation by ROS has often been put in question because of slow reaction kinetics compared to more favorable reactions with abundant thiol-based reductants such as peroxiredoxins (Prx) or glutathione (GSH). This commentary aims to address this controversy by highlighting the unique physical properties in cells that may restrict ROS diffusion and allow otherwise less favorable cysteine oxidation of proteins. Some limitations of analytical tools to assess Cys-SOH are also discussed. We conclude that formation of Cys-SOH in biological systems cannot always be predicted based on kinetic analyses in homogenous solution, and may be facilitated by unique structural and physical properties of Cys-containing proteins within e.g. signaling complexes.

Authors+Show Affiliations

Department of Pathology and Laboratory Medicine, University of Vermont, Burlington, VT 05405, United States.Department of Pathology and Laboratory Medicine, University of Vermont, Burlington, VT 05405, United States.Department of Pathology and Laboratory Medicine, University of Vermont, Burlington, VT 05405, United States. Electronic address: albert.van-der-vliet@uvm.edu.

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural

Language

eng

PubMed ID

28126370

Citation

Heppner, David E., et al. "The Role of Sulfenic Acids in Cellular Redox Signaling: Reconciling Chemical Kinetics and Molecular Detection Strategies." Archives of Biochemistry and Biophysics, vol. 616, 2017, pp. 40-46.
Heppner DE, Janssen-Heininger YMW, van der Vliet A. The role of sulfenic acids in cellular redox signaling: Reconciling chemical kinetics and molecular detection strategies. Arch Biochem Biophys. 2017;616:40-46.
Heppner, D. E., Janssen-Heininger, Y. M. W., & van der Vliet, A. (2017). The role of sulfenic acids in cellular redox signaling: Reconciling chemical kinetics and molecular detection strategies. Archives of Biochemistry and Biophysics, 616, 40-46. https://doi.org/10.1016/j.abb.2017.01.008
Heppner DE, Janssen-Heininger YMW, van der Vliet A. The Role of Sulfenic Acids in Cellular Redox Signaling: Reconciling Chemical Kinetics and Molecular Detection Strategies. Arch Biochem Biophys. 2017 02 15;616:40-46. PubMed PMID: 28126370.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The role of sulfenic acids in cellular redox signaling: Reconciling chemical kinetics and molecular detection strategies. AU - Heppner,David E, AU - Janssen-Heininger,Yvonne M W, AU - van der Vliet,Albert, Y1 - 2017/01/23/ PY - 2016/12/21/received PY - 2017/01/20/revised PY - 2017/01/22/accepted PY - 2017/1/28/pubmed PY - 2017/5/16/medline PY - 2017/1/28/entrez SP - 40 EP - 46 JF - Archives of biochemistry and biophysics JO - Arch. Biochem. Biophys. VL - 616 N2 - The reversible oxidation of protein cysteine residues is well recognized as an important regulatory mechanism in redox-dependent cell signaling. Cysteine oxidation is diverse in nature and involves various post-translational modifications (sulfenic acids, disulfides, etc.) and the specific functional or structural impact of these specific oxidative events is still poorly understood. The proximal product of protein cysteine oxidation by biological reactive oxygen species (ROS) is sulfenic acid (Cys-SOH), and experimental evidence is accruing for the formation of Cys-SOH as intermediate in protein cysteine oxidation in various biological settings. However, the plausibility of protein Cys-SH oxidation by ROS has often been put in question because of slow reaction kinetics compared to more favorable reactions with abundant thiol-based reductants such as peroxiredoxins (Prx) or glutathione (GSH). This commentary aims to address this controversy by highlighting the unique physical properties in cells that may restrict ROS diffusion and allow otherwise less favorable cysteine oxidation of proteins. Some limitations of analytical tools to assess Cys-SOH are also discussed. We conclude that formation of Cys-SOH in biological systems cannot always be predicted based on kinetic analyses in homogenous solution, and may be facilitated by unique structural and physical properties of Cys-containing proteins within e.g. signaling complexes. SN - 1096-0384 UR - https://www.unboundmedicine.com/medline/citation/28126370/The_role_of_sulfenic_acids_in_cellular_redox_signaling:_Reconciling_chemical_kinetics_and_molecular_detection_strategies_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0003-9861(16)30581-1 DB - PRIME DP - Unbound Medicine ER -