The intermediate CuI-semiquinone radical species in the catalytic mechanism of copper-amine oxidase from Lens esculenta and Pisum sativum seedlings has been studied by optical, Raman resonance and ESR spectroscopies and by stopped-flow and temperature-jump measurements. Treatment of highly purified enzyme preparations with good, poor or suicide substrates, under anaerobic and aerobic conditions, at different pH values and temperatures, makes it possible to generate, detect and characterize this free radical intermediate.

Medda, R., Padiglia, A., Bellelli, A., Pedersen, J., Agrò, A., Floris, G. (1999). CuI-semiquinone radical species in plant copper-amine oxidases. FEBS LETTERS, 453(1-2), 1-5.

CuI-semiquinone radical species in plant copper-amine oxidases

Pedersen JZ;
1999-06-18

Abstract

The intermediate CuI-semiquinone radical species in the catalytic mechanism of copper-amine oxidase from Lens esculenta and Pisum sativum seedlings has been studied by optical, Raman resonance and ESR spectroscopies and by stopped-flow and temperature-jump measurements. Treatment of highly purified enzyme preparations with good, poor or suicide substrates, under anaerobic and aerobic conditions, at different pH values and temperatures, makes it possible to generate, detect and characterize this free radical intermediate.
18-giu-1999
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore BIO/10 - BIOCHIMICA
English
Amine Oxidase (Copper-Containing); Fabaceae; Free Radicals; Metalloproteins; Models, Chemical; Copper; Plants, Medicinal; Quinones
Medda, R., Padiglia, A., Bellelli, A., Pedersen, J., Agrò, A., Floris, G. (1999). CuI-semiquinone radical species in plant copper-amine oxidases. FEBS LETTERS, 453(1-2), 1-5.
Medda, R; Padiglia, A; Bellelli, A; Pedersen, J; Agrò, A; Floris, G
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/210860
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