Woodruff W H, Dallinger R F, Antalis T M, Palmer G
Biochemistry. 1981 Mar 3;20(5):1332-8. doi: 10.1021/bi00508a045.
Resonance Raman studies of oxidized and reduced cytochrome oxidase and liganded derivatives of the oxidized enzyme have been performed by using direct-Soret excitation at 413.1 and 406.7 nm, as well as near-Soret excitation (457.9 nm) and alpha-band excitation (604.6 nm). The Soret results clearly show selective enhancement of Raman modes of the hemes of cytochromes a and a3, depending upon the excitation wavelength chosen. For the preparations employed in this study, photoreduction of cytochrome oxidase in the laser beam was not a significant problem. Resonance Raman frequencies sensitive to oxidation state and spin state or core expansion of the a and a3 hemes are identified and correlated with those previously identified for other heme proteins. An unusual low-frequency (less than 500 cm(-1)) spectrum is observed for oxidized high-spin cytochrome a3, which may be due to axial nonheme structures in this cytochrome.
通过在413.1和406.7nm处进行直接索雷特激发，以及近索雷特激发（457.9nm）和α带激发（604.6nm），对氧化型和还原型细胞色素氧化酶以及氧化酶的配位衍生物进行了共振拉曼研究。索雷特结果清楚地表明，根据所选择的激发波长，细胞色素a和a3血红素的拉曼模式有选择性增强。对于本研究中使用的制剂，激光束中细胞色素氧化酶的光还原不是一个重大问题。确定了对a和a3血红素的氧化态、自旋态或核心膨胀敏感的共振拉曼频率，并将其与先前为其他血红素蛋白确定的频率相关联。观察到氧化型高自旋细胞色素a3有异常的低频（小于500cm-1）光谱，这可能是由于该细胞色素中的轴向非血红素结构所致。
