Thiol-containing plant proteins and glutathione (GSH)

Thiol-containing plant proteins and glutathione (GSH) constitute the primary antioxidant defense system in botanical organisms, playing a pivotal role in maintaining cellular redox homeostasis (Meyer, 2008) [1]. Glutathione is a tripeptide (gamma-glutamyl-cysteinyl-glycine) that serves as a major reservoir of non-protein reduced sulfur and acts as a cofactor for enzymes like glutathione S-transferases (GSTs) (Noctor et al., 2012) [2]. These molecules are essential for the detoxification of both endogenous reactive oxygen species and exogenous xenobiotics, such as herbicides and heavy metals (PubChem CID 124886) [3]. In agricultural science, many herbicides, including chloroacetanilides, target or are detoxified by this system, making it a focal point for studying herbicide resistance and selectivity (Fuerst, 1987) [4]. From a human health perspective, while not a direct therapeutic target, plant-derived thiols are significant as dietary antioxidants that can modulate human Phase II detoxification enzymes (Dixon et al., 2002) [5]. Depletion of these thiol pools can lead to severe oxidative stress, impaired protein function, and eventual cell death. Consequently, this group of molecules is a key subject in environmental toxicology, plant physiology, and nutritional biochemistry.

Other names

Plant thiolsPhytoglutathioneSulfhydryl-containing plant proteinsReduced glutathione

The primary mechanism involves the nucleophilic attack of the thiol (-SH) group on electrophilic centers of xenobiotics, a process often facilitated by glutathione S-transferases (GSTs) to form non-toxic conjugates that can be sequestered or excreted (Fuerst, 1987; Dixon et al., 2002) [4, 5].