ISSN:
1432-1327
Keywords:
Key words Aminopeptidase
;
Streptomyces
;
Dinuclear
;
NMR
;
Co2+
;
Cu2+
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Abstract 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 1H NMR spectrum with sharp hyperfine-shifted signals, again indicating the presence of a dinuclear active site. This 1H NMR spectrum with sharp hyperfine-shifted features represents a first of its kind for a di-Cu2+ center in metalloproteins.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s007750050190
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