Enzyme inhibitor modeling with TpZn complexes of functional hydroxamates and oximates

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• 作者：T. Tekeste ; H. Vahrenkamp
• 关键词：Zinc complexes ; Chelate ligands ; Hydroxamates ; Oximates ; Enzyme modeling
• 刊名：Inorganica Chimica Acta
• 出版年：2007
• 出版时间：1 April 2007
• 年：2007
• 卷：360
• 期：5
• 页码：1523-1528
• 全文大小：211 K

文摘

Salicylhydroxamic acid reacts with the enzyme model Tp^Ph,MeZn-OH to form the O,O-chelating hydroxamate complex 1. The hydrogen bonding capacity of zinc enzyme bound hydroxamates is reproduced by cocrystallization of two molecules if 1 with two molecules of methanol and by cocrystallization of one molecule of Tp^Ph,MeZn-acetohydroxamate with one molecule of 3-phenyl-5-methylpyrazole. The complex formed from Tp^Ph,MeZn-OH and N-tosylproline hydroxamic acid, according to its spectra, contains the hydroxamate as an N,N-chelating ligand. In contrast, the oximate derived from pyruvic aldehyde does not act as a chelating ligand, but is monodentate via the oximate oxygen.