Protein sulfhydration

Protein sulfhydration

Protein sulfhydration PY2015 IR95 glutathione, hydrogen sulfide, cysteine

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Protein sulfhydration PY2015 IR95 glutathione, hydrogen sulfide, cysteine

https://pubmed.ncbi.nlm.nih.gov/25747476/

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Methods Enzymol

. 2015;555:79-90.  doi: 10.1016/bs.mie.2014.11.021.  Epub 2015 Jan 14.

Protein sulfhydration

Bindu D Paul  1 , Solomon H Snyder  2

Affiliations

1 The Solomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA.

2 The Solomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA; Department of Pharmacology, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA; Department of Psychiatry, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA. Electronic address: ssnyder@jhmi.edu.

PMID: 25747476  DOI: 10.1016/bs.mie.2014.11.021

Abstract

Hydrogen sulfide (H2S) is one of the gasotransmitters that modulates various biological processes and participates in multiple signaling pathways. H2S signals by a process termed sulfhydration. Sulfhydration has recently been recognized as a posttranslational modification similar to nitrosylation. Sulfhydration occurs at reactive cysteine residues in proteins and results in the conversion of an -SH group of cysteine to an -SSH or a persulfide group. Sulfhydration is highly prevalent in vivo, and aberrant sulfhydration patterns have been observed under several pathological conditions ranging from heart disease to neurodegenerative diseases such as Parkinson's disease. The biotin switch assay, originally developed to detect nitrosylation, has been modified to detect sulfhydration. In this chapter, we discuss the physiological roles of sulfhydration and the methodologies used to detect this modification.

Keywords: Hydrogen sulfide; Maleimide assay; Modified biotin switch; Nitrosylation; Sulfhydration.

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