Metal Binding and Active Site Structure of Di-Zinc Streptomyces griseus Aminopeptidase
Lin, L.-Y.; Park, H. I.; Ming, L.-J.*
Department of Chemistry and Institute for Biomolecular Science, University of South Florida, Tampa, FL 33620
Streptomyces griseus aminopeptidase has been characterized to have a dinuclear active site and to follow a dinuclear hydrolytic mechanism by means of activity assay, optical, and NMR spectroscopy. A sequential binding of Co2+ to the dinuclear sites in 20 mM Mes buffer at pH 6.1 has also been established. The results from these studies suggest that the two metal sites have a five-coordination sphere, with at least one coordinated His each. A di-Cu2+-substituted derivative of the enzyme has been prepared which exhibits a H-1 NMR spectrum with sharp hyperfine-shifted signals, again indicating the presence of a dinuclear active site. This H-1 NMR spectrum with sharp hyperfine-shifted features represents a first of its kind for a di-Cu2+ center in metalloproteins.
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