ISSN:
1432-1327
Schlagwort(e):
Key words Aminopeptidase
;
Streptomyces
;
Dinuclear
;
NMR
;
Co2+
;
Cu2+
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Biologie
,
Chemie und Pharmazie
Notizen:
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.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/s007750050190
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