The binding of platinum hexahalides (Cl, Br and I) to hen egg-white lysozyme and the chemical transformation of the PtI6octahedral complex to a PtI3moiety bound to His15

Simon W M Tanley, Laurina Victoria Starkey, Lucinda Lamplough, Surasek Kaenket, John R. Helliwell

    Research output: Contribution to journalArticlepeer-review

    Abstract

    © 2014 International Union of Crystallography. All rights reserved.This study examines the binding and chemical stability of the platinum hexahalides K2PtCl6, K2PtBr6and K2PtI6when soaked into pre-grown hen egg-white lysozyme (HEWL) crystals as the protein host. Direct comparison of the iodo complex with the chloro and bromo complexes shows that the iodo complex is partly chemically transformed to a square-planar PtI3 complex bound to the Nδatom of His15, a chemical behaviour that is not exhibited by the chloro or bromo complexes. Each complex does, however, bind to HEWL in its octahedral form either at one site (PtI6) or at two sites (PtBr6and PtCl6). As heavy-atom derivatives of a protein, the octahedral shape of the hexahalides could be helpful in cases of difficult-to-interpret electron-density maps as they would be recognisable 'objects'.
    Original languageEnglish
    Pages (from-to)1132-1134
    Number of pages2
    JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
    Volume70
    Issue number9
    DOIs
    Publication statusPublished - 29 Aug 2014

    Keywords

    • hen egg-white lysozyme
    • platinum hexahalides
    • PtI3ligand bound to histidine
    • X-ray lasers

    Fingerprint

    Dive into the research topics of 'The binding of platinum hexahalides (Cl, Br and I) to hen egg-white lysozyme and the chemical transformation of the PtI6octahedral complex to a PtI3moiety bound to His15'. Together they form a unique fingerprint.

    Cite this