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首页> 外文期刊>The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical >Fe vibrational Spectroscopy of myoglobin and cytochrome f
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Fe vibrational Spectroscopy of myoglobin and cytochrome f

机译：肌红蛋白和细胞色素f的铁振动光谱

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摘要

The Fe vibrational density of states (VDOS) has been determined for the heme proteins deoxymyoglobin, metmyoglobin, and cytochrome f in the oxidized and reduced states, using nuclear resonance vibrational spectroscopy (NRVS). For cytochrome f in particular, the NRVS spectrum is compared with multiwavelength resonance Raman spectra to identify those Raman modes with significant Fe displacement. Modes not seen by Raman due to optical selection rules appear in the NRVS spectrum. The mean Fe force constant extracted from the VDOS illustrates how Fe dynamics varies among these four monoheme proteins, and is correlated with oxidation and spin state trends seen in model heme compounds. The protein's contribution to Fe motion is dominant at low frequencies, where coupling to the backbone tightly constrains Fe displacements in cytochrome f, in contrast to enhanced heme flexibility in myoglobin.
机译：使用核共振振动光谱法（NRVS）已确定氧化和还原态下血红素蛋白脱氧肌红蛋白，血肌红蛋白和细胞色素f的Fe振动态密度（VDOS）。特别是对于细胞色素f，将NRVS光谱与多波长共振拉曼光谱进行比较，以确定那些具有明显Fe位移的拉曼模式。由于光学选择规则，拉曼无法看到的模式出现在NRVS光谱中。从VDOS中提取的平均Fe力常数说明了Fe动态在这四种单血红素蛋白之间如何变化，并且与模型血红素化合物中的氧化和自旋态趋势相关。蛋白质对铁运动的贡献在低频时占主导地位，与骨架连接紧密地限制了细胞色素f中的铁置换，这与增强的肌红蛋白血红素柔性相反。

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