Protein cysteine oxidation in redox signaling: Caveats on sulfenic acid detection and quantification.
Oxidation of critical signaling protein cysteines regulated by H2O2has been considered to involve sulfenic acid (RSOH) formation. RSOH may subsequently form either a sulfenyl amide (RSNHR') with a neighboring amide, or a mixed disulfide (RSSR') with another protein cysteine or glutathione. Previous studies have claimed that RSOH can be detected as an adduct (e.g., with 5,5-dimethylcyclohexane-1,3-dione; dimedone). Here, kinetic data are discussed which indicate that few proteins can form RSOH under physiological signaling conditions. We also present experimental evidence that indicates that (1) dimedone reacts rapidly with sulfenyl amides, and more rapidly than with sulfenic acids, and (2) that disulfides can react reversibly with amides to form sulfenyl amides. As some proteins are more stable as the sulfenyl amide than as a glutathionylated species, the former may account for some of the species previously identified as the "sulfenome" - the cellular complement of reversibly-oxidized thiol proteins generated via sulfenic acids.
Andrus Gerontology Center of the Leonard Davis School of Gerontology, University of Southern California, 3715 McClintock Ave, Los Angeles, CA 90089-0191, USA. Electronic address: peroxideman@gmail.com.
Henry Jay
HJ
Forman
Department of Biomedical Science, Panum Institute, University of Copenhagen, Blegdamsvej 3, Copenhagen 2200, Denmark.
Michael J
MJ
Davies
Department of Biomedical Science, Panum Institute, University of Copenhagen, Blegdamsvej 3, Copenhagen 2200, Denmark.
Anna C
AC
Krämer
Department of Molecular Medicine, University of Padova, Viale G. Colombo 3, I-35121, Padova, Italy.
Giovanni
G
Miotto
Department of Molecular Medicine, University of Padova, Viale G. Colombo 3, I-35121, Padova, Italy.
Mattia
M
Zaccarin
Andrus Gerontology Center of the Leonard Davis School of Gerontology, University of Southern California, 3715 McClintock Ave, Los Angeles, CA 90089-0191, USA.
Hongqiao
H
Zhang
Department of Molecular Medicine, University of Padova, Viale G. Colombo 3, I-35121, Padova, Italy.
Fulvio
F
Ursini
D000577:Amides / Q000737:chemistry; D003512:Cyclohexanones / Q000737:chemistry*; D003545:Cysteine / Q000737:chemistry*; D004220:Disulfides / Q000737:chemistry; D005978:Glutathione / Q000737:chemistry; D006801:Humans; D006861:Hydrogen Peroxide / Q000737:chemistry; D007700:Kinetics; D013058:Mass Spectrometry; D010084:Oxidation-Reduction; D010100:Oxygen / Q000737:chemistry*; D054562:Protein Tyrosine Phosphatase, Non-Receptor Type 1 / Q000737:chemistry; D015398:Signal Transduction; D013434:Sulfenic Acids / Q000737:chemistry*; D013438:Sulfhydryl Compounds / Q000737:chemistry
D000577:Amides; D003512:Cyclohexanones; D004220:Disulfides; D013434:Sulfenic Acids; D013438:Sulfhydryl Compounds; C004774:dimedone; D006861:Hydrogen Peroxide; C516607:PTPN1 protein, human; D054562:Protein Tyrosine Phosphatase, Non-Receptor Type 1; D005978:Glutathione; D003545:Cysteine; D010100:Oxygen
Glutathione; Hydrogen peroxide; Redox signaling; Sulfenyl amide; Thiolate
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