Thiol

A thiol is an organosulfur compound with a sulfhydryl group (–SH) bonded to carbon. Its sulfur–hydrogen bond gives it distinctive reactivity and often a strong odor.

Thiol–disulfide exchange: A reaction in which a thiolate attacks a disulfide, exchanging sulfur partners. This reaction links thiol chemistry to reversible sulfur-bond formation.
Sulfhydryl group: The –SH functional group consisting of sulfur bonded to hydrogen. It is the defining structural feature of a thiol.
Cysteine: A proteinogenic amino acid whose side chain contains a thiol group. Cysteine supplies most biologically relevant protein thiols.
Thiol tautomerism: Tautomeric interconversion between a thiol form and a thione form through proton and double-bond shifts. Some compounds called thiols favor a thione structure, complicating simple functional-group assignments.
William Christopher Zeise: A Danish chemist known for early studies of sulfur-containing organic compounds and organometallic chemistry. His nineteenth-century work helped establish the chemistry of sulfur compounds related to thiols.
Thiol acidity: The tendency of an S–H bond to release a proton, producing a thiolate anion. Deprotonation creates the more nucleophilic species involved in many thiol reactions.
Sulfur: A chemical element with atomic number 16 that forms diverse bonds in inorganic and organic compounds. Thiol chemistry depends on sulfur's bonding and polarizability.
Glutathione: A tripeptide with a cysteine thiol that serves as a major cellular antioxidant. Its thiol cycles between reduced and disulfide forms to buffer cellular redox conditions.
Thione: An organosulfur compound containing a carbon–sulfur double bond, commonly represented as C=S. Thiones are constitutional and tautomeric counterparts to many thiols.
Mercaptan: A traditional name for a thiol, derived from the Latin phrase for capturing mercury. The name records thiols' strong tendency to bind mercury.

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