QCR10 Inhibitors

Chemical inhibitors of QCR10 target various components of the mitochondrial electron transport chain (ETC) in which this protein is a key participant. Antimycin A operates by binding to the Q_i site of the cytochrome bc1 complex, where QCR10 is located, thereby blocking the transfer of electrons from ubiquinol to cytochrome c1. This action results in the inhibition of the QCR10-associated cytochrome bc1 complex activity. Similarly, Myxothiazol inhibits QCR10 by attaching itself to the Q_o site of the cytochrome b subunit within the same complex, blocking electron transfer from the Rieske iron-sulfur protein to cytochrome c1. Stigmatellin also targets the ubiquinol oxidation site of the cytochrome bc1 complex, obstructing the path of electron transfer and, consequently, QCR10's role in this process. These inhibitors effectively disrupt the critical function of QCR10 in the mitochondrial ETC by obstructing the normal electron flow through the complex.

Beyond the direct inhibitors of the bc1 complex, other chemicals indirectly hinder the function of QCR10 by diminishing the electron flow to the complex where this protein operates. Atpenin A5 and Carboxin inhibit complex II, which reduces the supply of electrons to the downstream complexes, including the cytochrome bc1 complex that houses QCR10. Thenoyltrifluoroacetone disrupts various dehydrogenases, leading to a decreased supply of electrons to the ETC and, by extension, to QCR10. Rotenone and Piericidin A, by inhibiting complex I, also diminish the electron flow to QCR10. Zinc Pyrithione acts at multiple points within the ETC, which can result in a reduced flow of electrons to QCR10. Celastrol disrupts mitochondrial function broadly, affecting the entire ETC and consequently reducing the functional capacity of QCR10. Lastly, Tetracycline hampers mitochondrial protein synthesis, which can lead to suboptimal assembly and function of the ETC complexes, including the one associated with the activity of QCR10.