摘要
以标记在ATP酶(F_1)催化部位的TNP-ATP为荧光探针,比较测定了F_1与其抑制蛋白(IF_1)结合前后的TNP-ATP荧光光谱、荧光寿命和荧光偏振光谱。结果表明在IF1的作用下,酶分子催化部位的极性下降,TNP-ATP分子运动的自由度减小,提示IF_1引起了F_1催化部位的构象改变。
The regulatory function of mitochondrial ATPase inhibitor (IF1) on catalytic portion of ATPase (F1) was investigated by using labelled F1 with fluorescent ATP derivatve 2’, 3’,-0(2, 4, 6-trinitrocyclohexadienylidene) adenosine 5’-triphosphate (TNP-ATP).The fluorescent parameters including fluorescent spectra, fluorescent lifetime and polarization spectra were determined for TNP-ATP-F1 and IF1-TNP-ATP-F1. These data indicate that IF1 significantly alters the polarity of the catalytic portion of F1 and the catalytic portion became more constricted under the action of IF1.
基金
国家自然科学基金
关键词
线粒体
腺苷三磷酸酶
抑制蛋白
酶
构象
ATPase inhibitor protein
Fluorescence spectra
Polarization spectra
Fluorescencelifetime