Insights into the role of zinc(II) sites in hydrolytic enzymes: Study of the ZnII/X/(py)2CO (X = Cl-, N3-, SO42-; (py)2CO=di-2-pyridyl ketone) reaction systems

Kenichi Nishioka, Judd C. Rice, Kavitha Sarma, Hediye Erdjument-Bromage, Janis Werner, Yanming Wang, Sergei Chuikov, Pablo Valenzuela, Paul Tempst, Ruth Steward, John T. Lis, C. David Allis, Danny Reinberg

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A bioinorganic model approach for the investigation of substrate activation by zinc active sites in hydrolytic enzymes has been initiated. Several reaction schemes involving the substrate analogue di-2-pyridyl ketone, (py)2CO, and Zn(II) sources afforded the new complexes [ZnCl2{(py)2CO}](1), [ZnCl2{(py)2C(OMe)(OH)}](2), [Zn2Cl2{(py)2C(OMe)O}2](3), [Zn2(N3)2{(py)2C(OMe) O}2](4) and [Zn2(SO4)2{(py)2C(OMe) (OH)}2(MeOH)2](5), which have been characterized by single-crystal X-ray crystallography and spectroscopic techniques. The chemical and structural identity of the products depends on the solvent, the hydroxide concentration and the nature of the inorganic anion. The biological relevance of the prepared complexes is also discussed.

Original languageEnglish (US)
Pages (from-to)719-723
Number of pages5
JournalInorganic Chemistry Communications
Issue number9
StatePublished - Sep 1 2002

All Science Journal Classification (ASJC) codes

  • Physical and Theoretical Chemistry
  • Inorganic Chemistry
  • Materials Chemistry


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