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Some of these functions have recently been ascribed to its oxidized form polysulfides (H<jats:sub>2<\/jats:sub>S<jats:sub>n<\/jats:sub>), which can be produced by 3\u2010mercaptopyruvate sulfurtransferase (MPST), also known as a H<jats:sub>2<\/jats:sub>S\u2010producing enzyme. H<jats:sub>2<\/jats:sub>S<jats:sub>n<\/jats:sub> activate ion channels, tumour suppressors, transcription factors, and protein kinases. H<jats:sub>2<\/jats:sub>S<jats:sub>n<\/jats:sub> <jats:italic>S<\/jats:italic>\u2010sulfurate (<jats:italic>S<\/jats:italic>\u2010sulfhydrate) cysteine residues of these target proteins to modify their activity by inducing conformational changes through the formation of a disulfide bridge between the two cysteine residues involved. The chemical interaction between H<jats:sub>2<\/jats:sub>S and NO also generates H<jats:sub>2<\/jats:sub>S<jats:sub>n<\/jats:sub>, which may be a chemical entity that exerts the synergistic effect of H<jats:sub>2<\/jats:sub>S and NO. MPST also produces redox regulators cysteine persulfide (CysSSH), GSH persulfide (GSSH), and persulfurated proteins. In addition to MPST, haemoproteins such as haemoglobin, myoglobin, neuroglobin, and catalase as well as SOD can produce H<jats:sub>2<\/jats:sub>S<jats:sub>n<\/jats:sub>, and sulfide quinone oxidoreductase and cysteinyl tRNA synthetase can make GSSH and CysSSH. This review focuses on the recent progress in the study of the production and physiological roles of these persulfurated and polysulfurated molecules.<\/jats:p><\/jats:sec><jats:sec><jats:title>Linked Articles<\/jats:title><jats:p>This article is part of a themed section on Hydrogen Sulfide in Biology &amp; Medicine. 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