Wu Yunhua
Key Lab for Biotechnology of National Commission for Nationalities, College of Life Science, The South Central University for Nationalities, Wuhan 430074, PR China.
J Pharm Biomed Anal. 2007 Jul 27;44(3):796-801. doi: 10.1016/j.jpba.2007.03.016. Epub 2007 Mar 25.
The interaction between catalase (CAT) and salicylic acid (SA) was studied by fluorescence and UV-vis spectroscopic techniques. The quenching mechanism of fluorescence of BSA by CAT was discussed to be a static quenching procedure. The number of binding sites n and apparent binding constant K was measured by fluorescence quenching method. The thermodynamics parameter DeltaH, DeltaG, DeltaS were calculated. The results indicate the binding reaction was both entropy-driven and the enthalpy-driven, and the hydrogen bond and van der Waals force played major role in the binding reaction. The binding sites of SA with CAT was investigated to be approached the microenvironment of Trp by the synchronous fluorescence spectrometry. The distance r between donor (CAT) and acceptor (SA) was obtained according to Förster theory of non-radioactive energy transfer.
采用荧光光谱和紫外可见光谱技术研究了过氧化氢酶（CAT）与水杨酸（SA）之间的相互作用。探讨了CAT对牛血清白蛋白（BSA）荧光的猝灭机制为静态猝灭过程。通过荧光猝灭法测定了结合位点的数目n和表观结合常数K。计算了热力学参数ΔH、ΔG、ΔS。结果表明，结合反应是熵驱动和焓驱动的，氢键和范德华力在结合反应中起主要作用。采用同步荧光光谱法研究了SA与CAT的结合位点，发现其靠近色氨酸的微环境。根据Förster非辐射能量转移理论，获得了供体（CAT）与受体（SA）之间的距离r。
