An unexpected formation of the spectroscopic Cu(I)-semiquinone radical by xenon-induced self-catalysis of a copper quinoprotein

Biochimie
R MeddaG Floris

Abstract

Plant copper/quinone amine oxidases are homodimeric enzymes containing Cu(II) and a quinone derivative of a tyrosyl residue (2,4,5-trihydroxyphenylalanine, TPQ) as cofactors. These enzymes catalyze the oxidative deamination of primary amines by a classical ping-pong mechanism, i.e. two distinct half-reactions, enzyme reduction by substrate followed by its re-oxidation by molecular oxygen. In the first half-reaction two forms of the reduced TPQ have been observed, the colorless Cu(II)-aminoquinol and the yellow Cu(I)-semiquinolamine radical so that this enzyme may be referred to as a "protein-radical enzyme". The interaction of xenon, in aqueous solutions, with the copper/TPQ amine oxidase from lentil (Lens esculenta) seedlings has been investigated by NMR and optical spectroscopy. NMR data indicate that xenon binds to the protein. Under 10 atm gaseous xenon and in the absence of substrates more than 60% native enzyme is converted into Cu(I)-semiquinolamine radical species, showing for the first time that both monomers in the dimer can generate the radical. Under the same experimental conditions the copper-free lentil enzyme is able to generate an intermediate absorbing at about 360 nm, which is assigned to the product Schiff ba...Continue Reading

References

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Citations

Jun 28, 2008·Journal of the American Chemical Society·Arnab MukherjeeJustine P Roth
Apr 6, 2007·The Journal of Biological Chemistry·Bryan J JohnsonCarrie M Wilmot
Apr 17, 2007·The FEBS Journal·Anna MuraRosaria Medda
Apr 16, 2009·The Journal of Physical Chemistry. B·Roberto AneddaPaolo Ruggerone
Apr 22, 2015·Accounts of Chemical Research·Eric M Shepard, David M Dooley

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