Protoheme conformations in low-spin ferrohemoproteins. Resonance raman spectroscopy

A. Desbois , M. Lutz , R. Banerjee
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引用次数: 5

Abstract

The low-frequency regions of resonance Raman spectra of various low-spin ferrous forms of normal human hemoglobin, soybean leghemoglobin a and of horse myoglobin are reported. Differences observed among the spectra of oxygenated and nitrosyl forms of these hemoproteins show that their globins impose various low-spin heme structures. A quantitative correlation between the variable frequency of resonance Raman band II (215–271 cm−1) and the iron atom-heme plane distance was observed for hemoproteins and heme models, either ferrous or ferric, high-spin or low-spin. From this correlation, the iron atom-heme plane distance should be 0.3 Å in nitrosyl and oxymyoglobin (band II at 256 cm−1) whereas the iron position should be near to or in the heme plane for nitrosyl and oxy forms of hemoglobin and leghemoglobin (band II between 266 and 273 cm−1). A new method is proposed for monitoring the photodissociation processes in ferrohemoproteins.

低自旋铁血红蛋白中的原血红素构象。共振拉曼光谱学
报道了正常人血红蛋白、大豆豆血红蛋白a和马肌红蛋白的各种低自旋亚铁形式的共振拉曼光谱的低频区。在这些血红蛋白的氧合和亚硝基形式的光谱中观察到的差异表明,它们的球蛋白施加各种低自旋血红素结构。在铁质或铁质、高自旋或低自旋的血红蛋白和血红素模型中,观察到共振拉曼波段II (215-271 cm−1)的可变频率与铁原子-血红素平面距离之间的定量相关性。从这种相关性来看,亚硝基和氧基肌红蛋白中的铁原子-血红素平面距离应为0.3 Å(波段2在256 cm−1),而亚硝基和氧基血红蛋白和血红蛋白中的铁原子位置应该接近或在血红素平面内(波段2在266和273 cm−1之间)。提出了一种监测铁血蛋白光解过程的新方法。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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