In order to investigate the role of the reduced coenzyme in the tritium exchange reaction, we have studied this reaction substituting for the natural reduced coenzyme two of its analogues devoid of enzymatic redox power. Using tetrahydropyridine TPN, both the pH curve and the pK of the group involved in the binding of the cofactor to the enzyme are shifted toward lower pH values. These findings are interpreted to be due to the different basicity of the pyridine nitrogens of the cofactors.

A role for the pyridine nitrogen of reduced triphosphopyridinenucleotide in an enzymatic catalysis

RIPPA, Mario;SIGNORINI, Marco;DALLOCCHIO, Franco Pasquale Filippo
1973

Abstract

In order to investigate the role of the reduced coenzyme in the tritium exchange reaction, we have studied this reaction substituting for the natural reduced coenzyme two of its analogues devoid of enzymatic redox power. Using tetrahydropyridine TPN, both the pH curve and the pK of the group involved in the binding of the cofactor to the enzyme are shifted toward lower pH values. These findings are interpreted to be due to the different basicity of the pyridine nitrogens of the cofactors.
1973
Rippa, Mario; Signorini, Marco; Dallocchio, Franco Pasquale Filippo
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11392/1683812
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