Mar 31, 1981

Resonance Raman spectroscopy of arsanilazocarboxypeptidase A: mode of inhibitor binding and active-site topography

R K ScheuleH A Scheraga


The interaction of inhibitors with the active site of arsanilazocarboxypeptidase A has been investigated by means of resonance Raman spectroscopy. The resonance Raman bands of the active-site azotyrosine-248 residue have been shown previously to be sensitive to its state of ionization and its interactions with nearby groups. In particular, the azophenol form of azotyrosine-248 can adopt two different coexisting conformations that differ with respect to the presence or absence of an intramolecular hydrogen bond between the phenolic proton and a nitrogen atom of the azo group. Each of these conformations exhibits characteristic vNN and v phi N azo stretching frequencies. The relative concentrations of these two forms, revealed by resonance Raman spectroscopy, are a sensitive probe of the hydrogen bond accepting ability of the local environment. The present study shows that the binding of L-benzylsuccinate, phenylacetate, L-phenyllactate, and beta-phenylpropionate markedly perturbs the distribution of the intra- and intermolecularly hydrogen-bonded forms of azotyrosine-248 in water. In contrast, glycyl-L-tyrosine and L-phenylalanine leave this distribution unperturbed. These results, taken jointly with other data on inhibitor bind...Continue Reading

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Mentioned in this Paper

Raman Optical Activity Spectroscopy
Plasma Protein Binding Capacity
Arsanilazocarboxypeptidase A
Cobalt(II)-arsanilazocarboxypeptidase A

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