Exploring quinone‐binding sites as targets for pesticides

Quinones, such as ubiquinone and plastoquinone, are essential components of most photosynthetic and respiratory electron transfer chains. Proteins with quinone‐binding sites (Q‐sites) regulate the oxidation and reduction of these molecules that mediate processes vital for sustaining life. Due to their function as mobile electron carriers, quinones bind relatively weakly at Q‐sites, making them vulnerable to disruption by potent inhibitors that interfere with essential biological functions. As a result, Q‐sites have emerged as key targets for numerous pesticides. Advances in X‐ray crystallography and cryo‐electron microscopy have revealed detailed structural insights into Q‐sites across a variety of proteins. While Q‐sites universally recognize quinones, their geometric and electronic configurations differ among proteins. These variations have supported the development of highly specific pesticides but have also enabled resistance through target‐site mutations that hinder pesticide binding. This review explores the unique features of individual Q‐site and the mechanisms of resistance linked to them. Additionally, we examine the physical properties of pesticides that interact with membrane‐embedded Q‐sites and compare the structural characteristics of these binding pockets.