Bacterial enzymes and proteins containing thiol residues

Bacterial enzymes and proteins containing thiol residues represent a broad class of molecular targets essential for microbial survival, encompassing roles in metabolism, structural stability, and redox regulation (Russell & Hugo, 1994). Thiol (sulfhydryl) groups, primarily found on cysteine residues, are critical for the catalytic function of numerous enzymes and the maintenance of cellular homeostasis (NIH, 2023). Antimicrobial agents such as silver ions, organomercurials, and auranofin exert their bactericidal effects by covalently binding to these thiol groups, which results in enzyme inactivation and protein denaturation (PNAS, 2013; NIH, 2023). This process often triggers the production of reactive oxygen species (ROS), further damaging the bacterial cell (MDPI, 2023). While these targets are highly effective for broad-spectrum activity, their ubiquity in human cells poses significant risks of systemic toxicity and adverse effects like argyria or neurotoxicity (NIH, 2020; NIH, 2023). Modern research focuses on identifying specific bacterial thiol-dependent systems, such as thioredoxin reductase, to develop more selective and safer therapeutic agents (PNAS, 2013).

Other names

Bacterial thiol-dependent enzymesBacterial sulfhydryl-containing proteinsBacterial cysteine-containing enzymesBacterial thiol-dependent redox systems

Antimicrobial agents target these proteins by covalently binding to the sulfhydryl (-SH) groups of cysteine residues, which inactivates essential enzymes and denatures structural proteins (Russell & Hugo, 1994; NIH, 2023). This interaction disrupts the bacterial redox balance, often leading to the accumulation of reactive oxygen species (ROS) and subsequent cell death (PNAS, 2013; MDPI, 2023).