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Advances in Hydrogen Sulfide Biology pp 1–16Cite as

A Common Molecular Switch for H2S to Regulate Multiple Protein Targets

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 1315))

Abstract

Hydrogen sulfide, a small molecule, produced by endogenous enzymes, such as CTH, CBS, and MPST using L-cysteine as substrates, has been reported to have numerous protective effects. However, the key problem that the target of H2S and how it can affect the structure and activity of biological molecules is still unknown. Till now, there are two main theories of its working mechanism. One is that H2S can modify the free thiol in cysteine to produce the persulfide state of the thiol and the sulfhydration of cysteine can significantly change the structure and activity of target proteins. The other theory is that H2S, as an antioxidant molecule, can directly break the disulfide bond in target proteins, and the persulfide state of thiol can be an intermediate product during the reaction. Both phenomena exit for no doubt since they are both supported by large amounts of experiments. Here, we will summarize both theories and try to discuss which one is the more effective or direct mechanism for H2S and what is the relationship between them. Therefore, we will discover more protein targets of H2S with the mechanism and understand more about the effect of this small molecule.

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Acknowledgments

This work was supported by the funding of innovative research team of high-level local universities in Shanghai and a key laboratory program of the Education Commission of Shanghai Municipality (ZDSYS14005 to Yi-Chun Zhu). This work was supported by Ying Chen (Department of Physiology and Pathophysiology of Fudan University) in sketch drawing.

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  1. Shanghai Key Laboratory of Bioactive Small Molecules and Shanghai Key Laboratory of Clinical Geriatric Medicine, Department of Physiology and Pathophysiology, School of Basic Medical Sciences, Fudan University, Shanghai, China

    Bei-Bei Tao & Yi-Chun Zhu

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Correspondence to Yi-Chun Zhu .

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  1. Department of Physiology and Pathophysiology, Fudan University Shanghai Medical College, Shanghai Key Laboratory of Bioactive Small Molecules, School of Basic Medical Sciences, Shanghai, China

    Yi-Chun Zhu

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Tao, BB., Zhu, YC. (2021). A Common Molecular Switch for H2S to Regulate Multiple Protein Targets. In: Zhu, YC. (eds) Advances in Hydrogen Sulfide Biology. Advances in Experimental Medicine and Biology, vol 1315. Springer, Singapore. https://doi.org/10.1007/978-981-16-0991-6_1

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