F1-ATPase是一種膜蛋白,分別由三個α次單體(subunits)、三個β次單體與一個γ次單體所組合而成,且F1-ATPase可將ATP(Adenosine triphosphate)水解成ADP(Adenosine triphosphate)與磷酸(Pi)的活性功能。以基因重組的技術。將大腸桿菌的F1-ATPase α、β與γ次單體分別表現出來。再將單獨的α次單體與β次單體以重新重組的方式將α與β次單體組合成α3β3 complex,我們將α3β3 complex以化學修飾於矽線表面上,並利用矽奈米線場效應電晶體來觀察F1-ATPase與受質ATP的結合。實驗結果顯示,在β次單體或α3β3複合體中,加入 ATP會造成p型矽奈米線場效應電晶體的電流下降,表示ATP可以與β次單體或α3β3複合體結合。但實驗亦發現加入ATP進入修飾α次單體的奈米線不會造成電流的變化,證明ATP不會與α次單體反應。
F1-ATPase is a kind of membrane protein. It is composed of three α and three β and one γ subunits. F1-ATPase could hydrolyze ATP to ADP and phosphate. In this study, we cloned and expressed individually the recombinant of α, β and γ subunits of E.coli F1-ATPase. After purification, equal amounts of α and β subunits were mixed to obtain α3β3 complex in vitro. The α and β subunits and α3β3 complex were then modified on the surface of silicon nanowire field effect transistors (SiNW-FETs). Introduction of ATP into p-type SiNW-FET modified with β subunit and α3β3 complex resulted in a decrease in the nanowire current, indicating reaction of ATP with β subunit and α3β3 complex. Contrarily, it is found that adding ATP into SiNW-FETs did not cause device current to change, suggesting that ATP does not react with α subunit.