Modeling the inhibition of peptide deformylase by hydroxamic acids: influence of the sulfur donor.
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.
Galardon
Erwan
E
Laboratoire de Chimie et Biochimie Toxicologiques et Pharmacologiques, UMR8601 CNRS, Université René Descartes, 45 rue des St-Pères, 75270, Paris Cedex 06, France.
Giorgi
Michel
M
Artaud
Isabelle
I
D000581:Amidohydrolases / Q000037:antagonists & inhibitors*; D018360:Crystallography, X-Ray; D006868:Hydrolysis; D006877:Hydroxamic Acids / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology*; D007202:Indicators and Reagents; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D008958:Models, Molecular; D011480:Protease Inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D012997:Solvents; D013457:Sulfur Compounds / Q000737:chemistry*
D006877:Hydroxamic Acids; D007202:Indicators and Reagents; D011480:Protease Inhibitors; D012997:Solvents; D013457:Sulfur Compounds; D000581:Amidohydrolases; C084507:peptide deformylase