Compounds containing the sulfur-sulfur double bond

Kutney, Gerald; Turnbull, Kenneth

doi:10.1021/cr00050a001

Cited by 96 publications

(43 citation statements)

References 51 publications

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“…As mentioned above, the persulfides would react with electrophiles rather than with nucleophiles (Artaud and Galardon 2014;Bailey et al 2014), and when they do react with nucleophiles (such as other free thiols), this reaction leads to the release of H 2 S (which represents the basis of one of the methods for persulfide detection: reduction with DTT). The reaction with nucleophiles could only go as an attack to sulfane sulfur, but that leads to the formation of a mixed disulfide and elimination of H 2 S. Some literature data exist suggesting that persulfides could exist in the tautomeric thiosulfoxide form (Scheme 1), which would then act as a perfect donor of sulfane sulfur (Kutney and Turnbull 1982;Steudel et al 1997). However, it is worth noting that although this may be true for the extreme case of F 2 S 2 , neither experimental nor computational data support the existence of this tautomeric form (Steudel et al 1997).…”

Section: "Trans-persulfidation" By Polythiolated Cysteine or Glutathionementioning

confidence: 99%

Persulfidation (S-sulfhydration) and H2S

Filipovic

2015

Handbook of Experimental Pharmacology

170

152

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The past decade has witnessed the discovery of hydrogen sulfide (H2S) as a new signalling molecule. Its ability to act as a neurotransmitter, regulator of blood pressure, immunomodulator or anti-apoptotic agent, together with its great pharmacological potential, is now well established. Notwithstanding the growing body of evidence showing the biological roles of H2S, the gap between the macroscopic descriptions and the actual mechanism(s) behind these processes is getting larger. The reactivity towards reactive oxygen and nitrogen species and/or metal centres cannot explain this plethora of biological effects. Therefore, a mechanism involving modification of protein cysteine residues to form protein persulfides is proposed. It is alternatively called S-sulfhydration. Persulfides are not particularly stable and show increased reactivity when compared to free thiols. Detection of protein persulfides is still facing methodological limitations, and mechanisms by which H2S causes this modification are still largely scarce. Persulfidation of protein such as KATP could contribute to H2S-induced vasodilation, while S-sulfhydration of GAPDH and NF-κB inhibits apoptosis. H2S regulates endoplasmic reticulum stress by causing persulfidation of PTP-1B. Several other proteins have been found to be regulated by this posttranslational modification of cysteine. This review article provides a critical overview of the current state of the literature addressing protein S-sulfhydration, with particular emphasis on the challenges and future research directions in this particular field.

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Section: "Trans-persulfidation" By Polythiolated Cysteine or Glutathionementioning

confidence: 99%

Persulfidation (S-sulfhydration) and H2S

Filipovic

2015

Handbook of Experimental Pharmacology

170

152

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“…A very important as well as interesting reaction of S 0 is its transfer between sulfur structures through the formation of thiosulfoxide tautomer (eq. 12) [51,272]. With an empty orbital, the sulfoxide sulfur in the tautomer can interact with a nucleophile (Nu) and consequently S 0 is transferred (eq.…”

Section: H2s Reaction With Thiol Derivatives (Or Thiol Reaction Wimentioning

confidence: 99%

Chemical foundations of hydrogen sulfide biology

2013

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Following nitric oxide (nitrogen monoxide) and carbon monoxide, hydrogen sulfide (or its newer systematic name sulfane, H2S) became the third small molecule that can be both toxic and beneficial depending on the concentration. In spite of its impressive therapeutic potential, the underlying mechanisms for its beneficial effects remain unclear. Any novel mechanism has to obey fundamental chemical principles. H2S chemistry was studied long before its biological relevance was discovered, however, with a few exceptions, these past works have received relatively little attention in the path of exploring the mechanistic conundrum of H2S biological functions. This review calls attention to the basic physical and chemical properties of H2S, focuses on the chemistry between H2S and its three potential biological targets: oxidants, metals and thiol derivatives, discusses the applications of these basics into H2S biology and methodology, and introduces the standard terminology to this youthful field.

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“…23 In the substratefree SseA structure an observed water molecule hydrogen bonded to His66 might mimic the position of the carbonyl oxygen atom of the bound 3-mercaptopyruvate molecule (Figure 3(b)). The mixed disulfide formed between Cys237 and 3-mercaptopyruvate contains a labile sulfur atom, transferrable to cyanide via the formation of thiosulfoxide intermediate, 24 conformation (as observed in SseA chain A) would position the carboxylate group of Asp262 next to the active site covalent intermediate (Figure 3(b)). This shift could sequentially (1) cause the activation of a nucleophilic species (e.g.…”

Section: -Mercaptopyruvate Sulfurtransferasementioning

confidence: 99%