The sulfur atom found on cysteine residues can bond with an additional sulfur atom containing a hydrogen atom. This process is called sulfhydration and can occur when compounds such as hydrogen sulfide are present in the cell. Cysteine residues found in proteins that have undergone sulfhydration play important roles in diverse biological functions. Mouse aortic endothelial cells were treated with H2S and various polysulfides. We compared the differences in protein targets in the cells modified by the added sulfides utilizing a modified biotin thiol assay (BTA). The modified cysteines produced were identified by LC-MS analysis. The results show that free H2S and polysulfides select for different subsets of proteins in the cells. The classification of the proteins in each subset using bioinformatics methods is in progress.

Selectivity of protein sulfhydration

253rd National Meeting (2017)

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