Abstract
For many years reactive oxygen and nitrogen species (ROS and RNS) have been recognized as key messengers in the process of thiol-based redox regulation. Relatively recently, literature reports began to mention reactive sulfur species (RSS) and their role in thiol regulation. This review is focused on biogenesis and biological properties of RSS, including: hydropersulfides, polysulfides and hydrogen sulfide (H2S). Based on the most up-to-date literature data, the paper presents biological significance of S-sulfhydration process. In this reaction, sulfane sulfur is transferred to the-SH groups forming hydropersulfides. Protein cysteine residues, called 'redox switches' are susceptible to such reversible modifications. In line with the most recent reports, it was emphasized that sulfane sulfur-containing compounds (mainly hydrogen persulfides and polysulfides) are real and better mediators of S-sulfhydration-based signalling than H2S. We also overviewed proteins participating in the formation and transport of RSS and in mitochondrial H2S oxidation. In addition, we reviewed many reports about proteins unrelated to sulfur metabolism which are modified by S-sulfhydration that influences their catalytic activity. We also addressed the problem of the regulatory function of S-sulfhydration reaction in the activation of KATP channels (vasorelaxant) and transcription factors (e.g. NFκB) as well as in the mechanism of therapeutic action of garlic-derived sulfur compounds. Some aspects of comparison between RNS and RSS are also discussed in this review.
Highlights
Reactive oxygen species (ROS), life threatening products of incomplete oxygen reduction, which damage biomolecules and impair their biological action, are an inevitable consequence of the appearance of oxygen and obligate aerobic organisms on the Earth billions of years ago
It is known that the physiological level of oxidants performs regulatory function whereas their high levels cause oxidative stress and cell damage which leads to pathological states
The commonly accepted key messengers of redox signal transduction in the cell include reactive oxygen species (ROS) [1,2] and reactive nitrogen species (RNS) [3] and reactive sulfur species (RSS) [4,5], which are the principal subject of this review
Summary
Reactive oxygen species (ROS), life threatening products of incomplete oxygen reduction, which damage biomolecules and impair their biological action, are an inevitable consequence of the appearance of oxygen and obligate aerobic organisms on the Earth billions of years ago. Protein –SH groups can be oxidized by one-electron oxidants, i.e. radical species, like ROS, RNS and RSS and by two-electron oxidants which can show a regulatory effect already at physiological concentrations, that was emphasized by Jones [41,42] These reversibly oxidized –SH groups are under control of glutathione (GSH), cysteine (Cys) and Trx, called ‘nodes’ and play an important role in signalling processes. This confirms a crucial role of S-sulfhydration reaction in regulatory processes [5,45], and this is why this process and its biological significance attract increasing interest. Ida et al [5] demonstrated that GSSH could react with glutathione disulfide (GSSG) which led to the formation of the trisulfide (GSSSG), and in subsequent reactions even higher GSH polysulfides could be generated (reaction 18)
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