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The binding of platinum hexahalides (Cl, Br and I) to hen egg‐white lysozyme and the chemical transformation of the PtI 6 octahedral complex to a PtI 3 moiety bound to His15
Author(s) -
Tanley Simon W. M.,
Starkey LaurinaVictoria,
Lamplough Lucinda,
Kaenket Surasek,
Helliwell John R.
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14014009
Subject(s) - octahedron , lysozyme , crystallography , chemistry , atom (system on chip) , platinum , stereochemistry , crystal structure , organic chemistry , biochemistry , computer science , embedded system , catalysis
This study examines the binding and chemical stability of the platinum hexahalides K 2 PtCl 6 , K 2 PtBr 6 and K 2 PtI 6 when 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 PtI 3 complex bound to the N δ atom 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 (PtI 6 ) or at two sites (PtBr 6 and PtCl 6 ). 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'.