【摘要】 本文利用付立叶变换红外差示技术,获得了氨基酰化酶,脱Zn（Ⅱ）氨基酰化酶酶蛋白,和Co（Ⅱ）重组氨酰化酶水溶液的远红外吸收谱.结果表明,510cm^-1至500cm^-1的一个吸收峰是由活性部位中金属离子与其配位原子间的伸缩振动所引起.我们认为,付立叶变换红外光谱法可以为金属酶活性部位的结构与功能的研究直接提供有用的信息.更多还原

【Abstract】 Aminoacylase is a Zn metalloenzyme.The far infrared absorption spectra of aminoacylase, metal-free apoamino-acylase, and Co-substituted aminoacylase in aqueous solutions were studied in the frequency range of 530 cm-1 to 100 cm-1 with a Fourier Transform Infrared Spectrophotometer. The spectra have been obtained by subtracting the contribution of water from the spectra of the enzymes’ solutions. Aminoacylase has an obvious absorption peak between the wave numbers 510 cm-1 and 500 cm-1 when it contains the Zn(Ⅱ) ions, which are necessary for the enzymetic activity, and Co (Ⅱ) ions also, as incorporated in aminoacylase, which can reactivate inactive metal-free apoaminoacylase. But this absorption does not appear in the spectrum of the metal-free aminoacylase. As compared with that of Zn aminoacylase, the peak of Co-substituted aminoacylase shifts to a higher wave number for about 2 cm-1. In accordance with the results mentioned above, the peak is essentially assigned to the vibration absorption of the metal ions (Zn(Ⅱ), CO(Ⅱ)) with their coordinate atoms in the active sites. The absorption spectra of Co-substituted aminoacylase under different conditions were also compared.As far as we know, this is the first attemp to study metalloenzyme with far infrared spectroscopy. The results indicate that the direct information about the Zn(Ⅱ) ions in the active sites of aminoacylase can be demonstrate in the IR spectra clearly. We believe that this method could be used for advanced studying about the structure and function of the active sites in aminoacylase or other metalloenzyme.更多还原