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Neuroglobin Provides a Convenient Scaffold to Investigate the Triplet-State Properties of Porphyrins by Time-Resolved EPR Spectroscopy and Magnetophotoselection
Applied Magnetic Resonance ( IF 1 ) Pub Date : 2021-09-04 , DOI: 10.1007/s00723-021-01421-3
Susanna Ciuti 1 , Antonio Barbon 1 , Marco Bortolus 1 , Alessandro Agostini 1, 2 , Marilena Di Valentin 1, 3 , Donatella Carbonera 1, 3 , Elisabetta Bergantino 4 , Caterina Martin 4
Affiliation  

The photo-excited triplet state of Zn-protoporphyrin IX located in the heme pocket of human neuroglobin has been investigated by time-resolved EPR coupled to magnetophotoselection. The triplet state in the protein matrix has been compared with the model complex in organic glass, considering both non-coordinating and coordinating solvent mixtures. The protein matrix plays an important role in stabilizing the coordination of the embedded chromophore, resulting in a more homogeneous environment relative to that of the chromophore in a glassy solvent, even in the presence of an axial nitrogenous ligand like pyridine. The EPR spectral parameters point out a slow Jahn–Teller interconversion between slightly different triplet states, both in organic solvent and in the protein matrix. The EPR-magnetophotoselection allows us to propose a reinterpretation of the assignment of the Q bands in the electronic absorption spectrum.



中文翻译:

神经红蛋白为通过时间分辨 EPR 光谱和磁光选择研究卟啉的三重态特性提供了方便的支架

已通过时间分辨 EPR 与磁光选择耦合研究了位于人神经红蛋白血红素口袋中的 Zn-原卟啉 IX 的光激发三重态。考虑到非配位和配位溶剂混合物,蛋白质基质中的三重态已与有机玻璃中的模型复合物进行了比较。蛋白质基质在稳定嵌入的发色团的配位方面起着重要作用,即使在存在轴向含氮配体(如吡啶)的情况下,相对于发色团在玻璃溶剂中的环境也会产生更均匀的环境。EPR 光谱参数指出在有机溶剂和蛋白质基质中略有不同的三重态之间存在缓慢的 Jahn-Teller 相互转换。

更新日期:2021-09-04
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