Modeling the inhibition of peptide deformylase by hydroxamic acids: influence of the sulfur donor

Dalton Trans. 2007 Mar 14:(10):1047-52. doi: 10.1039/b616212f. Epub 2007 Jan 23.

Abstract

The first complexes containing both a sulfur atom and a hydroxamate moiety coordinated to a biologically relevant transition metal were synthesized as models for the structure of inhibited peptide deformylases. Two of these [(N(2)S)Zn(hydroxamate)] complexes were characterized by X-ray crystallography. The first contains a thioether and a simple hydroxamate, the second a thiolate and a N-substituted hydroxamate. Isolation of a complex with a thiolate and a simple hydroxamate group was not possible.

MeSH terms

  • Amidohydrolases / antagonists & inhibitors*
  • Crystallography, X-Ray
  • Hydrolysis
  • Hydroxamic Acids / chemical synthesis
  • Hydroxamic Acids / chemistry*
  • Hydroxamic Acids / pharmacology*
  • Indicators and Reagents
  • Magnetic Resonance Spectroscopy
  • Mass Spectrometry
  • Models, Molecular
  • Protease Inhibitors / chemistry*
  • Protease Inhibitors / pharmacology*
  • Solvents
  • Sulfur Compounds / chemistry*

Substances

  • Hydroxamic Acids
  • Indicators and Reagents
  • Protease Inhibitors
  • Solvents
  • Sulfur Compounds
  • Amidohydrolases
  • peptide deformylase