Structural and electronic mimics of the active site of cobalt(II)-substituted zinc metalloenzymes.
Complexes of cobalt(II) and zinc(II) which involve monodentate coordination of two alkyl carboxylate and two imidazole ligands in a slightly distorted tetrahedral fashion have visible and magnetic circular dichroism spectra remarkably similar to the cobalt(II)-substituted proteolytic enzymes thermolysin and carboxypeptidase A. Single crystal x-ray structure determinations on [Co(C2H5COO)2Im2], Im = imidazole, and its zinc counterpart reveal only minor structural differences between the cobalt and zinc species. Electron paramagnetic resonance spectra of cobalt(II) doped into zinc(II) complexes with known structures demonstrate the extreme sensitivity of the g-values to minor structural differences.
D001665:Binding Sites; D002264:Carboxylic Acids; D002268:Carboxypeptidases / Q000378:metabolism; D043422:Carboxypeptidases A; D003035:Cobalt / Q000494:pharmacology; D007093:Imidazoles; D008024:Ligands; D008667:Metalloproteins; D013053:Spectrophotometry; D013820:Thermolysin / Q000378:metabolism; D014961:X-Ray Diffraction; D015032:Zinc
D002264:Carboxylic Acids; D007093:Imidazoles; D008024:Ligands; D008667:Metalloproteins; D003035:Cobalt; D002268:Carboxypeptidases; D043422:Carboxypeptidases A; D013820:Thermolysin; D015032:Zinc