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Photoreduction and validation of haem?ligand intermediate states in protein crystals by in situ single-crystal spectroscopy and diffraction

Kekilli, D and Moreno-Chicano, T and Chaplin, AK and Horrell, S and Dworkowski, FSN and Worrall, JAR and Strange, RW and Hough, MA (2017) 'Photoreduction and validation of haem?ligand intermediate states in protein crystals by in situ single-crystal spectroscopy and diffraction.' IUCrJ, 4 (3). 263 - 270. ISSN 2052-2525

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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.

Item Type: Article
Uncontrolled Keywords: X-ray photoreduction; laser photoreduction of haem; haem; in crystallo optical spectroscopy
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Science and Health > Biological Sciences, School of
Depositing User: Jim Jamieson
Date Deposited: 29 Jun 2017 14:22
Last Modified: 18 Sep 2018 11:15
URI: http://repository.essex.ac.uk/id/eprint/19914

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