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首页> 外文期刊>IUCrJ >Photoreduction and validation of haem–ligand intermediate states in protein crystals by in situ single-crystal spectroscopy and diffraction
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Photoreduction and validation of haem–ligand intermediate states in protein crystals by in situ single-crystal spectroscopy and diffraction

机译：通过原位单晶光谱和衍射对蛋白质晶体中血红素-配体中间态进行光还原和验证

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摘要

Powerful synergies are available from the combination of multiple methods to study proteins in the crystalline form. Spectroscopies which probe the same region of the crystal from which X-ray crystal structures are determined can give insights into redox, ligand and spin states to complement the information gained from the electron-density maps. The correct assignment of crystal structures to the correct protein redox and ligand states is essential to avoid the misinterpretation of structural data. This is a particular concern for haem proteins, which can occupy a wide range of redox states and are exquisitely sensitive to becoming reduced by solvated electrons generated from interactions of X-rays with water molecules in the crystal. Here, single-crystal spectroscopic fingerprinting has been applied to investigate the laser photoreduction of ferric haem in cytochrome c′. Furthermore, in situ X-ray-driven generation of haem intermediates in crystals of the dye-decolourizing-type peroxidase A (DtpA) from Streptomyces lividans is described.
机译：多种方法的结合可提供强大的协同作用，以研究晶体形式的蛋白质。光谱学探测晶体的相同区域，从中可以确定X射线晶体结构，可以深入了解氧化还原，配体和自旋态，以补充从电子密度图获得的信息。为了避免对结构数据的误解，将晶体结构正确分配给正确的蛋白质氧化还原和配体状态至关重要。对于血红素蛋白，这是一个特别关注的问题，血红素蛋白可以占据广泛的氧化还原状态，并且对X射线与晶体中水分子相互作用产生的溶剂化电子的还原非常敏感。在这里，单晶光谱指纹图谱已被用于研究细胞色素c'中铁血红素的激光光还原。此外，描述了原产于链霉菌的染料脱色型过氧化物酶A（DtpA）晶体中原位X射线驱动的血红素中间体的生成。

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