A biosensor based on rotary molecular motors

A biosensor based on FoF₁-ATPase with immunological and biochemical techniques to achieve the goal of clenbuterol detection is constructed. The enzyme FoF₁-ATPase is a molecular motor that converts the chemical energy stored in the molecule adenosine tri-phosphate (ATP) into mechanical rotation of its gamma sub-unit. During steady state catalysis, the three catalytic sites of FoF₁-ATPase operate in a cooperative fashion such that at every instant each site is in a different conformation corresponding to a different stage along the catalytic cycle. Notwithstanding a large amount of biochemical and, recently, structural data we still lack an understanding of how ATP hydrolysis in FoF₁-ATPase is coupled to mechanical motion and how the catalytic sites achieve cooperativity during rotatory catalysis. It´s found that different loads onto the subunit of chromatophores could affect its synthesis activity to different extent. The detecting mechanism was depended on proton-flux driven by rotary catalytic ATP synthesis. The results clearly showed that the detection of clenbuterol by the biosensor was 10^-12g/L. The results showed that the new biosensor may prove to be a useful nano-device for super-sensitive detection. The activity of FoF₁-ATPase is affected with different loads of rotary molecular motors.