Article
Subtle changes in endochin-like quinolone structure alter the site of inhibition within the cytochrome bc1 complex of Plasmodium falciparum.
Antimicrobial agents and chemotherapy - 1 Apr 2015
Stickles Allison M, de Almeida Mariana Justino, Morrisey Joanne M, Sheridan Kayla A, Forquer Isaac P, Nilsen Aaron, Winter Rolf W, Burrows Jeremy N, Fidock David A, Vaidya Akhil B, Riscoe Michael K
Abstract excerpt
The cytochrome bc1 complex (cyt bc1) is the third component of the mitochondrial electron transport chain and is the target of several potent antimalarial compounds, including the naphthoquinone atovaquone (ATV) and the 4(1H)-quinolone ELQ-300. Mechanistically, cyt bc1 facilitates the transfer of electrons from ubiquinol to cytochrome c and contains both oxidative (Qo) and reductive (Qi) catalytic sites that are...
Topics
- Animals
- Antimalarials
- Cytochromes b
- Drug Resistance
- Electron Transport Complex III
- Models, Molecular
- Mutation
- Plasmodium falciparum
- Protein Binding
- Quinolones
- Structure-Activity Relationship