A 1H NMR study of cobalt(II) arsanilazocarboxypeptidase A.
Cobalt(II) arsanilazotyrosine-248 carboxypeptidase A has been characterized through 1H NMR spectroscopy. The ability of the azoenzyme to form binary and ternary complexes with L- and D-phenylalanine and azide has been investigated. Comparison with the 1H NMR results obtained on unmodified cobalt(II) carboxypeptidase provides direct information on the specific effect of the presence of the azo group on the reactivity of the system. Marked differences in the interaction with D-phenylalanine have been observed, and structural inferences are drawn.
Bertini
I
I
Department of Chemistry, University of Florence, Italy.
Hirose
J
J
Messori
L
L
Monnanni
R
R
D002268:Carboxypeptidases / Q000378:metabolism*; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D010649:Phenylalanine / Q000378:metabolism; D011485:Protein Binding
C019731:arsanilazocarboxypeptidase A; D010649:Phenylalanine; D006859:Hydrogen; D002268:Carboxypeptidases