Aralkyl Hydrodisulfides. IV. The Reaction of Benzyl Hydrodisulfide with Several Nucleophiles

Kawamura, Shunichi; Otsuji, Yoshio; Nakabayashi, Takeshige; Kitao, Teijiro; Tsurugi, Jitsuo

doi:10.1021/jo01019a048

Cited by 33 publications

(15 citation statements)

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“…This interpretation may indicate a primary signaling/regulatory function associated with persulfides (because of their prevalence and established biosynthesis through both CSE and CBS) and that H 2 S may be a marker for persulfide formation (although this view does not preclude possible physiological function for H 2 S). The release of H 2 S from persulfides can occur through reduction of persulfides by other thiol-based reductants or through the actions of GSR, because both pathways are known to release H 2 S from persulfides (18,19). Clearly, H 2 S is known to react with oxidized thiol species to generate persulfides (15).…”

Section: Discussionmentioning

confidence: 99%

Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling

Ida¹,

Sawa

Ihara

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

811

1,236

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Using methodology developed herein, it is found that reactive persulfides and polysulfides are formed endogenously from both small molecule species and proteins in high amounts in mammalian cells and tissues. These reactive sulfur species were biosynthesized by two major sulfurtransferases: cystathionine β-synthase and cystathionine γ-lyase. Quantitation of these species indicates that high concentrations of glutathione persulfide (perhydropersulfide >100 μM) and other cysteine persulfide and polysulfide derivatives in peptides/proteins were endogenously produced and maintained in the plasma, cells, and tissues of mammals (rodent and human). It is expected that persulfides are especially nucleophilic and reducing. This view was found to be the case, because they quickly react with H 2 O 2 and a recently described biologically generated electrophile 8-nitroguanosine 3′,5′-cyclic monophosphate. These results indicate that persulfides are potentially important signaling/effector species, and because H 2 S can be generated from persulfide degradation, much of the reported biological activity associated with H 2 S may actually be that of persulfides. That is, H 2 S may act primarily as a marker for the biologically active of persulfide species.thiol redox | hydrogen sulfide | electrophilic signaling | polysulfidomics H ydrogen sulfide (H 2 S) has been suggested to be an endogenous small molecule signaling species (1) by unknown mechanisms. Our laboratory recently showed that the presence of hydrogen sulfide anion (HS − ) may be responsible for the regulation and metabolism of various important electrophilic species [e.g., 8-nitroguanosine 3′,5′-cyclic GMP (8-nitro-cGMP)] (2). However, these studies also indicated that reactive intermediates other than HS − likely react with the electrophiles of interest. These previous studies alluded to the generation of a more reactive sulfur species capable of reacting with electrophiles, such as 8-nitro-cGMP. As reported herein, it was determined that reactive sulfur intermediates, such as hydropersulfides (RSSH) and polysulfides [RS(S) n H and RS(S) n SR], are formed in appreciable amounts during sulfur amino acid metabolism and possess important chemical and biological properties. Some of these sulfide species have long been known as sulfane sulfur compounds, which were suggested to exist endogenously in mammalian systems (1,(3)(4)(5). Reports also indicated that a hydropersulfide moiety with the general molecular formula RSSH may be formed on specific protein cysteine (Cys) residues, most typically of sulfur-transferring enzymes (i.e., sulfurtransferases) during enzymatic reactions (1, 5). Although such persulfide chemical reactivity is thought to be involved in the catalytic activity of particular enzymes (e.g., rhodanese, Cys desulfurases, and sulfide:quinone oxidoreductase) (6, 7), the more general physiological function and occurrence of Cys persulfides (CysSSH) and related species in cells and tissues, especially mammals, were unclear. Moreover, the exact chemical nature ...

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Section: Discussionmentioning

confidence: 99%

Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling

Ida¹,

Sawa

Ihara

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

811

1,236

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“…The outer sulfur can react with cyanide, thiolates, sulfite [133,135], amines [136], hydroxide [137], and tertiary phosphines [138,139]. Persulfides and cyanide react to form the corresponding thiol and thiocyanate, which, in the presence of ferric ions, forms a colored complex that can be quantified spectrophotometrically.…”

Section: Chemistry and Biology Of Persulfidesmentioning

confidence: 99%

Hydrogen Sulfide and Persulfides Oxidation by Biologically Relevant Oxidizing Species

et al. 2019

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Hydrogen sulfide (H2S/HS–) can be formed in mammalian tissues and exert physiological effects. It can react with metal centers and oxidized thiol products such as disulfides (RSSR) and sulfenic acids (RSOH). Reactions with oxidized thiol products form persulfides (RSSH/RSS–). Persulfides have been proposed to transduce the signaling effects of H2S through the modification of critical cysteines. They are more nucleophilic and acidic than thiols and, contrary to thiols, also possess electrophilic character. In this review, we summarize the biochemistry of hydrogen sulfide and persulfides, focusing on redox aspects. We describe biologically relevant one- and two-electron oxidants and their reactions with H2S and persulfides, as well as the fates of the oxidation products. The biological implications are discussed.

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“…The generation of − SCN from cyanolysis (Reaction 1) implies that CN − attacks the terminal sulfane 1 sulfur (assuming a single step process, which is not necessarily the case and discussed below). Previous studies have examined the reaction of other nucleophiles with hydropersulfides and reported that many factors can control the site of nucleophilic attack with both sulfur atoms being possible targets [for example, 50,51,52]. More recently Bailey and coworkers [53] generated an organic hydropersulfide and examined its reaction with various nucleophiles and bases in methylene chloride.…”

Section: Discussionmentioning

confidence: 99%

“…However, previous work indicates that nucleophilic attack at the internal sulfur atom is also possible [for example, 50–53] (Reaction 7).

normalN normalu c^{-} + normalR normalS normalS normalH \to normalN normalu normalc - normalS normalR + normalH S^{-}

Indeed, based on the relative pK a values for RSH (pK a approx.…”

Section: Discussionmentioning

confidence: 99%

The chemical biology of hydropersulfides (RSSH): Chemical stability, reactivity and redox roles

Saund

Sosa

Henriquez

et al. 2015

Archives of Biochemistry and Biophysics

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Recent reports indicate the ubiquitous prevalence of hydropersulfides (RSSH) in mammalian systems. The biological utility of these and related species is currently a matter of significant speculation. The function, lifetime and fate of hydropersulfides will be assuredly based on their chemical properties and reactivity. Thus, to serve as the basis for further mechanistic studies regarding hydropersulfide biology, some of the basic chemical properties/reactivity of hydropersulfides were studied. The nucleophilicity, electrophilicity and redox properties of hydropersulfides were examined under biological conditions. These studies indicate that hydropersulfides can be nucleophilic or electrophilic, depending on the pH (i.e. the protonation state) and can act as good one- and two-electron reductants. These diverse chemical properties in a single species make hydropersulfides chemically distinct from other, well-known sulfur containing biological species, giving them unique and potentially important biological function.

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Aralkyl Hydrodisulfides. IV. The Reaction of Benzyl Hydrodisulfide with Several Nucleophiles

Cited by 33 publications

References 0 publications

Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling

Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling

Hydrogen Sulfide and Persulfides Oxidation by Biologically Relevant Oxidizing Species

The chemical biology of hydropersulfides (RSSH): Chemical stability, reactivity and redox roles

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