NDUFB8 Inhibitors

Chemical inhibitors of NDUFB8 primarily target the mitochondrial electron transport chain, specifically complex I, where NDUFB8 is a subunit. Rotenone is a well-known inhibitor of mitochondrial complex I, binding directly to the complex and disrupting electron transport, thus inhibiting the function of NDUFB8 within the complex. The inhibition of electron transport by Rotenone leads to a reduction in ATP production, which is a direct consequence of NDUFB8 inhibition. Similarly, Piericidin A competes with coenzyme Q at the complex I level, diminishing the electron transfer capabilities of the complex and consequently inhibiting NDUFB8 activity. Amytal also binds to complex I, resulting in a blockade of electron transport and a subsequent decrease in NDUFB8 function as part of the complex. Parthenolide further inhibits NDUFB8 by modifying cysteine residues within complex I, interfering with its proper function and leading to decreased electron transport.

Additionally, Capsazepine disrupts mitochondrial function by inhibiting complex I, which indirectly reduces the activity of NDUFB8 by affecting its role in electron transfer. Rolliniastatin-2 and Deguelin both act as inhibitors of mitochondrial complex I, binding to the complex and obstructing electron transport, which in turn decreases the efficiency of NDUFB8. Fenpyroximate and Pyridaben selectively inhibit complex I, disrupting the normal electron transport function and thereby reducing the activity of NDUFB8 within the complex. Tolyporphin, through its binding to complex I, impairs electron transport and decreases the activity of the complex, including NDUFB8. Stigmatellin inhibits the ubiquinone reduction site of complex I, leading to a decrease in electron transfer activity and inhibiting the function of NDUFB8. Harmane, by interfering with electron transfer within mitochondrial complex I, effectively decreases the function of NDUFB8, highlighting the critical role this protein plays in the energy production process of cells.