Hydrogen Sulfide and Persulfides Oxidation by Biologically Relevant Oxidizing Species

Abstract

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.

H2S and reactive sulfur signaling at the host-bacterial pathogen interface

“…Their Janus character, enhanced nucleophilicity, and superior reducing capabilities make RSSH, along with organic polysulfides and their inorganic counterparts, potent antioxidants (Fig. 1B, bottom) (43,51,52). These properties may well be responsible for many of the beneficial traits attributed to H 2 S, including protection against oxidative stress and antibiotics in the infected host (21,26,47).…”

“…Oxidation of RSS results in the production of inorganic sulfur-containing molecules sulfite, thiosulfate, and sulfate ( Fig. 2B) (51). ROS can also drive the formation of low-molecular weight (LMW) thiol disulfides (RSSR) and sulfenic acids (RSOH), a major physiological marker of H 2 O 2 reactivity, which reacts with HSto form Figure 1.…”

“…Biogenesis and clearance of organic and inorganic RSS in bacteria. A and B, biogenesis of inorganic (A) and organic (B) RSS via enzymatic or nonenzymatic processes(43,51). In A, the biogenesis of thiosulfate shown is a schematic rendering only.…”

Monitoring the Redox Status in Multiple Sclerosis

“…Hydrogen sulfide (H 2 S) increases the activity of N -methyl-D-aspartate receptor and β-adrenergic receptors through a cAMP-dependent protein kinase and activates NOS and the hemoxygenase favoring the formation of Nitric oxide (NO) and carbon monoxide (CO) from heme metabolism [ 134 ]. Hydrogen sulfide (H 2 S) is a metal ligand that reacts with other biological electrophilic sulfur species such as hydropersulfide (RSSR) and sulfenic acid (RSOH) [ 135 ]. Cysteine residues in GSH were found to be readily oxidized by superoxide anions (O 2 −• ) to form singlet oxygen (O 2 1 Δ g ), glutathione disulfide (GSSG), and glutathione sulfonate (GSO 3 − ) in a reaction involved with peroxysulphenyl radical (RSOO • ).…”

“…Disulfide (RSSR) is electrophilic RSS that can be reduced to thiol (RSH). Hydropolysulfide (RSS n H) and dialkyl polysulfide (RSS n R) are like hydropersulfide (RSSH) [ 135 ]. RSS can interact with ROS, generating sulfur oxides such as peroxysulphenyl radical (RSOO • ), sulfenate (RSO − ), sulfinate (RSO 2 − ), sulfonate (RSO 3 − ), thiosulmonate (S 2 O 3 2− ), and SO 4 2 − [ 138 ].…”