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Biogenesis of reactive sulfur species for signaling by hydrogen sulfide oxidation pathways

Nature Chemical Biology volume 11, pages 457–464 (2015)Cite this article

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Abstract

The chemical species involved in H2S signaling remain elusive despite the profound and pleiotropic physiological effects elicited by this molecule. The dominant candidate mechanism for sulfide signaling is persulfidation of target proteins. However, the relatively poor reactivity of H2S toward oxidized thiols, such as disulfides, the low concentration of disulfides in the reducing milieu of the cell and the low steady-state concentration of H2S raise questions about the plausibility of persulfide formation via reaction between an oxidized thiol and a sulfide anion or a reduced thiol and oxidized hydrogen disulfide. In contrast, sulfide oxidation pathways, considered to be primarily mechanisms for disposing of excess sulfide, generate a series of reactive sulfur species, including persulfides, polysulfides and thiosulfate, that could modify target proteins. We posit that sulfide oxidation pathways mediate sulfide signaling and that sulfurtransferases ensure target specificity.

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Figure 1: Structures of some biologically relevant RSS chemotypes.
Figure 2: Models for H2S interaction with heme proteins.
Figure 3: Potential mechanisms for persulfidation and the resolution of this modification.
Figure 4: Potential complexity associated with uncatalyzed protein modification by polysulfides.
Figure 5: Rhodanese homology domain proteins and persulfide relay system for transpersulfidation.
Figure 6: Sulfide oxidation pathways.

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Acknowledgements

This work was supported in part by the US National Institutes of Health (GM112455 and HL58984).

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  1. Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan, USA

    Tatiana V Mishanina, Marouane Libiad & Ruma Banerjee

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Mishanina, T., Libiad, M. & Banerjee, R. Biogenesis of reactive sulfur species for signaling by hydrogen sulfide oxidation pathways. Nat Chem Biol 11, 457–464 (2015). https://doi.org/10.1038/nchembio.1834

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