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001-es BibID:	bibKLT00006984
Első szerző:	Várnagy Katalin (vegyész)
Cím:	Copper(II) and zinc(II) complexes of peptides as models for collagenase inhibitors / Katalin Várnagy, H. Süli-Vargha
Dátum:	1997
Megjegyzések:	Imidazole nitrogen donor atoms of histidyl residues are common binding sites in various metalloenzymes. For example, in carbonic anhydrase zinc(II) is coordinated to three imidazoles [1], in carboxypeptidase to two imidazoles and a carboxylate [2]. In blue copper proteins the copper(II) ion is coordinated to two histidine imidazole nitrogen and two sulfur atoms from cysteine and methionine, respectively [3]. In metalloproteins the three-dimensional structure of the macromolecular ligand facilitates the coordination of metal ions by independent side-chain residues. Therefore, ligands containing two or more imidazole donors linked by aliphatic carbon chains may be able to mimic the binding sites and catalytic activities of the enzymes. Due to the remarkable stability of metal complexes of polyimidazole ligands these may serve as inhibitors in zinc enzymes. Specific enzyme inhibitors may be obtained by attaching bis(imidazolyl) ligands to the peptide site which is responsible for enzyme cleavage.
ISBN:	978-94-010-6174-2
Tárgyszavak:	Természettudományok Kémiai tudományok tanulmány, értekezés könyvrészlet
Megjelenés:	Molecular modeling and dynamics of bioinorganic systems / eds. Lucia Banci, Peter Comba. - p. 441-463. -
További szerzők:	Süli-Vargha Helga
Pályázati támogatás:	OTKA-T015709 OTKA OTKA-1646 OTKA OTKA-007512 OTKA
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
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