Organic mercurial compounds are the most specific and sensitive reagents for reaction with the sulfhydryl groups (SHs) in peptides and proteins because of the strong mercury-sulfur affinity. Using the monofunctional organic mercury ion RHg(+) as a mass spectrometry (MS)-tag has the advantages of reacting with one sulfhydryl group, offering definite mass shift, and especially stable and characteristic nonradioactive isotopic distribution. Mass spectrometric analysis of derivatized sulfhydryls in peptides/proteins is thus an alternative for precisely counting the number of sulfhydryl groups and disulfide bonds (SS). Here the tags used include monomethylmercury chloride, monoethylmercury chloride, and 4-(hydroxymercuri) benzoic acid. The feasibility of this strategy is demonstrated using HPLC/ESI-MS to count SHs and SS in model peptides/proteins, i.e., glutathione, phytochelatins, lysozyme and beta-lactoglobulin, which contain increasing SHs and various SS linkages.
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Guo et al. (2008) studied this question.