Ikemura Kenichiro, Mukai Masahiro, Shimada Hideo, Tsukihara Tomitake, Yamaguchi Satoru, Shinzawa-Itoh Kyoko, Yoshikawa Shinya, Ogura Takashi
Department of Life Science, Graduate School of Life Science, University of Hyogo, Hyogo, Japan.
J Am Chem Soc. 2008 Nov 5;130(44):14384-5. doi: 10.1021/ja805735g. Epub 2008 Oct 11.
The Raman excitation profile of the nuFe O mode of horseradish peroxidase compound II exhibits a maximum at 580 nm. This maximum is located within an absorption band with a shoulder assignable to an oxygen-to-iron charge transfer band on the longer wavelength side of the alpha-band. Resonance Raman bands of the nuFe O mode of various ferryl-oxo type hemoproteins measured at 590 nm excitation indicate that many hemoproteins in the ferryl-oxo state have an oxygen-to-iron charge transfer band in the visible region. Since this red-excited resonance Raman technique causes much less photochemical damage in the proteins relative to blue-excited resonance Raman spectroscopy, it produces a higher signal-to-noise ratio and thus represents a powerful tool for investigations of ferryl-oxo intermediates of hemoproteins.
辣根过氧化物酶化合物II的νFe O模式的拉曼激发谱在580 nm处出现最大值。该最大值位于一个吸收带内，该吸收带在α带较长波长一侧有一个可归因于氧到铁电荷转移带的肩峰。在590 nm激发下测量的各种高铁-氧型血红素蛋白的νFe O模式的共振拉曼带表明，许多处于高铁-氧状态的血红素蛋白在可见光区域有一个氧到铁的电荷转移带。由于相对于蓝激发共振拉曼光谱，这种红激发共振拉曼技术对蛋白质造成的光化学损伤要小得多，它产生的信噪比更高，因此是研究血红素蛋白高铁-氧中间体的有力工具。
