Bovine serum amine oxidase (BSAO) reacts with 2-hydrazinopyridine, which binds the organic co-factor 2,4,5-trihydroxyphenylalanine quinone, forming a band at 435 nm. The band shifts to 526 nm around 60 degrees C, to 415 nm upon denaturation, but only shifts to 429 nm upon Cu2+ depletion. Its wavelength and intensity suggest that the adduct has the azo conformation, whilst the same adduct of crystalline Escherichia coli amine oxidase (ECAO) shows the hydrazone conformation in the X-ray structure.. The steady state kinetics of aminomethyl- and aminoethylpyridines confirm that the formation of the product Schiff base, analogous to the azo form of the 2-hydrazinopyridine adduct, is not hindered in solution. The structural stability of the adduct in the absence of Cu2+ is taken to imply hydrogen bonding of the pyridyl nitrogen to a conserved aspartate, as in the ECAO adduct. Thus the ECAO adduct provides a good model for a transient intermediate leading to formation of the BSAO azo adduct. On the basis of this model and of the catalytic competence of Co2+-substituted BSAO, confirmed by the present data, a catalytic reaction scheme is proposed.

The metal function in the reactions of bovine serum amine oxidase with substrates and hydrazine inhibitors / Giovanna De, Matteis; Agostinelli, Enzo; Mondovi', Bruno; L., Morpurgo. - In: JBIC. - ISSN 0949-8257. - 4:3(1999), pp. 348-353. [10.1007/s007750050321]

The metal function in the reactions of bovine serum amine oxidase with substrates and hydrazine inhibitors

AGOSTINELLI, Enzo;MONDOVI', Bruno;
1999

Abstract

Bovine serum amine oxidase (BSAO) reacts with 2-hydrazinopyridine, which binds the organic co-factor 2,4,5-trihydroxyphenylalanine quinone, forming a band at 435 nm. The band shifts to 526 nm around 60 degrees C, to 415 nm upon denaturation, but only shifts to 429 nm upon Cu2+ depletion. Its wavelength and intensity suggest that the adduct has the azo conformation, whilst the same adduct of crystalline Escherichia coli amine oxidase (ECAO) shows the hydrazone conformation in the X-ray structure.. The steady state kinetics of aminomethyl- and aminoethylpyridines confirm that the formation of the product Schiff base, analogous to the azo form of the 2-hydrazinopyridine adduct, is not hindered in solution. The structural stability of the adduct in the absence of Cu2+ is taken to imply hydrogen bonding of the pyridyl nitrogen to a conserved aspartate, as in the ECAO adduct. Thus the ECAO adduct provides a good model for a transient intermediate leading to formation of the BSAO azo adduct. On the basis of this model and of the catalytic competence of Co2+-substituted BSAO, confirmed by the present data, a catalytic reaction scheme is proposed.
1999
cobalt-substituted amine oxidase; copper amine oxidase; hydrazine inhibitors; trihydroxyphenylalanine quinone
01 Pubblicazione su rivista::01a Articolo in rivista
The metal function in the reactions of bovine serum amine oxidase with substrates and hydrazine inhibitors / Giovanna De, Matteis; Agostinelli, Enzo; Mondovi', Bruno; L., Morpurgo. - In: JBIC. - ISSN 0949-8257. - 4:3(1999), pp. 348-353. [10.1007/s007750050321]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/243539
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