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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >HEME GEOMETRY IN THE 10 K PHOTOPRODUCT FROM SPERM WHALE CARBONMONOXYMYOGLOBIN
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HEME GEOMETRY IN THE 10 K PHOTOPRODUCT FROM SPERM WHALE CARBONMONOXYMYOGLOBIN

机译：精鲸中碳氧合单糖的10 K磷酸酯产物中的血红素几何

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We have measured the Soret band of the photoproduct obtained by complete photolysis of sperm whale carbon-monoxymyoglobin at 10 K. The experimental spectrum has been modeled with an analytical expression that takes into account the homogeneous bandwidth, the coupling of the electronic transition with both high and low frequency vibrational modes, and the effects of static conformational heterogeneity. The comparison with deoxymyoglobin at low temperature reveals three main differences. In the photoproduct, the Soret band is shifted to red. The band is less asymmetric, and an enhanced coupling to the heme vibrational mode at 674 cm(-1) is observed. These differences reflect incomplete relaxation of the active site after ligand dissociation. The smaller band asymmetry of the photoproduct can be explained by a smaller displacement of the iron atom from the mean porphyrin plane, in quantitative agreement with the X-ray structure analysis, The enhanced vibrational coupling is attributed to a subtle heme distortion from the planar geometry that is barely detectable in the X-ray structure. [References: 41]
机译：我们已经测量了抹香鲸碳单氧肌红蛋白在10 K时完全光解所获得的光产物的Soret带。已通过解析表达式对实验光谱建模，该表达式考虑了均匀带宽，电子跃迁与高光谱的耦合。和低频振动模式，以及静态构象异质性的影响。与低温下的脱氧肌红蛋白的比较显示出三个主要差异。在照片产品中，Soret带变为红色。该带不太对称，并观察到在674 cm（-1）处血红素振动模式的增强耦合。这些差异反映了配体解离后活性位点的不完全松弛。与X射线结构分析定量吻合，光产物的较小带不对称性可以用铁原子相对于平均卟啉平面的较小位移来解释。增强的振动耦合归因于平面几何形状的细微血红素畸变在X射线结构中几乎无法检测到。 [参考：41]

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