Stavrov S S
Sackler Institute of Molecular Medicine, Sackler Faculty of Medicine, Tel Aviv University, Ramat Aviv, Israel.
Biophys J. 1993 Nov;65(5):1942-50. doi: 10.1016/S0006-3495(93)81265-7.
The causes of the strong coupling of the iron-histidine vibration to the Soret resonance in the resonance Raman spectra of deoxyhemoglobin, myoglobin, and peroxidase are explored, using the vibronic theory. It is shown that the extent of the iron displacement out of the plane of the porphyrin nitrogens is the main structural parameter controlling the Fe-NHis band features, such as the dependence of its frequency and intensity on the protein conformation and number of the axial ligands, time evolution after the photolysis of the diatomic complexes of the proteins under consideration, and inverse relationship between the changes Fe-NHis and v4 porphyrin breathing mode frequencies.
利用电子振动理论，探究了脱氧血红蛋白、肌红蛋白和过氧化物酶的共振拉曼光谱中铁 - 组氨酸振动与索雷特共振强耦合的原因。结果表明，铁原子偏离卟啉氮平面的位移程度是控制铁 - 氮组氨酸谱带特征的主要结构参数，例如其频率和强度对蛋白质构象及轴向配体数量的依赖性、所研究蛋白质的双原子配合物光解后的时间演化，以及铁 - 氮组氨酸变化与卟啉呼吸模式v4频率之间的反比关系。
