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Review
. 2016 Jan;58(1):7-15.
doi: 10.3164/jcbn.15-91. Epub 2015 Dec 8.

Chemical tools for the study of hydrogen sulfide (H2S) and sulfane sulfur and their applications to biological studies

Yoko Takano  1 , Kazuhito Shimamoto  1 , Kenjiro Hanaoka  1
Affiliations
Review

Chemical tools for the study of hydrogen sulfide (H2S) and sulfane sulfur and their applications to biological studies

Yoko Takano et al. J Clin Biochem Nutr. 2016 Jan.

Abstract

Hydrogen sulfide (H2S) functions in many physiological processes, including relaxation of vascular smooth muscles, mediation of neurotransmission, inhibition of insulin signaling, and regulation of inflammation. On the other hand, sulfane sulfur, which is a sulfur atom with six valence electrons but no charge, has the unique ability to bind reversibly to other sulfur atoms to form hydropersulfides (R-S-SH) and polysulfides (-S-Sn-S-). H2S and sulfane sulfur always coexist, and recent work suggests that sulfane sulfur species may be the actual signaling molecules in at least some biological phenomena. For example, one of the mechanisms of activity regulation of proteins by H2S is the S-sulfhydration of cysteine residues (protein Cys-SSH). In this review, we summarize recent progress on chemical tools for the study of H2S and sulfane sulfur, covering fluorescence probes utilizing various design strategies, H2S caged compounds, inhibitors of physiological H2S-producing enzymes (cystathionine γ-lyase, cystathionine β-synthase and 3-mercaptopyruvate sulfurtransferase), and labeling reagents. Fluorescence probes offer particular advantages as chemical tools to study physiological functions of biomolecules, including ease of use and real-time, nondestructive visualization of biological processes in live cells and tissues.

Keywords: caged compound; enzyme inhibitor; fluorescence probe; hydrogen sulfide; sulfane sulfur.

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Figures

Fig. 1
Fig. 1
Fluorescence probes for H2S: (a) Probes utilizing reduction of an azide group. (b) Mitochondrially targeted probes utilizing reduction of azide. (c) Probes based on reduction of a nitro group.
Fig. 2
Fig. 2
Fluorescence probes for H2S utilizing nucleophilic reaction of HS−.
Fig. 3
Fig. 3
Fluorescence probes based on the fluorescence quenching effect of Cu2+.
Fig. 4
Fig. 4
(a) Chemical structures of SPD-1 and SPD-2. (b) Photoreaction mechanism of ketoprofenate-based caged compounds. (c) Reaction mechanism of caged gem-dithiol.
Fig. 5
Fig. 5
S-Sulfhydration reaction: (a) Sulfane sulfur is much more effective for the illustrated reaction than H2S. (b) Proposedmechanism of S-sulfhydration reaction mediated by sulfane sulfur and tautomerization of hydropersulfide.
Fig. 6
Fig. 6
Chemical structures and reaction mechanisms of (a) SSPs and (b) DSPs with sulfane sulfur and hydrogen persulfide. (c) Two-photon excitation and NIR fluorescence probes for hydrogen persulfide utilizing 2-fluoro-5-nitrobenzoate as the H2S2/H2Sn recognition moiety, and a fluorescence probe for hydrogen persulfide utilizing an aziridine ring as a H2S2/H2Sn recognition moiety.
Fig. 7
Fig. 7
(a) Chemical structures of inhibitors of CSE and CBS. (b) Chemical structure of AzMC. (c) Screening schemes for 3MST and CSE inhibitors. (d) Tag-switching technique for detecting protein Cys S-sulfhydration.
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