photoreduction and validation of haem–ligand intermediate states in protein crystals by in situ single-crystal spectroscopy and diffraction
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ID: 190951
2017
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Abstract
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.
| Reference Key |
kekilli2017iucrjphotoreduction
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|---|---|
| Authors | ;Demet Kekilli;Tadeo Moreno-Chicano;Amanda K. Chaplin;Sam Horrell;Florian S. N. Dworkowski;Jonathan A. R. Worrall;Richard W. Strange;Michael A. Hough |
| Journal | european journal of orthopaedic surgery & traumatology : orthopedie traumatologie |
| Year | 2017 |
| DOI |
10.1107/S2052252517002159
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