Sulfhydryl-containing proteins (None)

Sulfhydryl-containing enzymes and structural proteins represent a broad and heterogeneous class of biological molecules defined by the presence of reactive thiol (-SH) groups, typically located on cysteine residues (Source: Wikipedia). These groups are essential for the catalytic function of numerous enzymes, including those in the citric acid cycle and antioxidant pathways, and are vital for maintaining protein architecture through disulfide bridge formation (Source: NIH). In pharmacology and toxicology, these proteins are the primary targets for heavy metals such as mercury, lead, and arsenic, which form stable covalent bonds with the sulfhydryl groups, thereby inactivating the proteins and disrupting cellular homeostasis (Source: StatPearls). This non-specific binding leads to widespread cellular dysfunction, including the inhibition of energy production and the induction of oxidative stress (Source: PubChem). While not a specific target for modern drug design, the interaction with sulfhydryl groups is the basis for the antimicrobial action of certain mercurial antiseptics and the therapeutic rationale for using chelating agents to treat heavy metal poisoning (Source: PubMed).

Other names

Thiol-containing proteinsCysteine-rich proteinsSulfhydryl-dependent enzymesSH-containing proteins

Covalent binding to thiol groups leading to enzyme inactivation or structural protein denaturation.