Chemical assembly of multiple metal cofactors: The heterologously expressed multidomain [FeFe]-hydrogenase from Megasphaera elsdenii. - Laboratoire de Chimie des Processus Biologiques Accéder directement au contenu
Article Dans Une Revue Biochimica biophysica acta (BBA) - Bioenergetics Année : 2016

Chemical assembly of multiple metal cofactors: The heterologously expressed multidomain [FeFe]-hydrogenase from Megasphaera elsdenii.

Résumé

[FeFe]-hydrogenases are unique and fascinating enzymes catalyzing the reversible reduction of protons into hydrogen. These metalloenzymes display extremely large catalytic reaction rates at very low overpotential values and are, therefore, studied as potential catalysts for bioelectrodes of electrolyzers and fuel cells. Since they contain multiple metal cofactors whose biosynthesis depends on complex protein machineries, their preparation is difficult. As a consequence still few have been purified to homogeneity allowing spectroscopic and structural characterization. As part of a program aiming at getting easy access to new hydrogenases we report here a methodology based on a purely chemical assembly of their metal cofactors. This methodology is applied to the preparation and characterization of the hydrogenase from the fermentative anaerobic rumen bacterium Megasphaera elsdenii, which has only been incompletely characterized in the past.
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Dates et versions

hal-01353393 , version 1 (06-10-2016)

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Georgio Caserta, Agnieszka Adamska-Venkatesh, Ludovic Pecqueur, Mohamed Atta, Artero Vincent, et al.. Chemical assembly of multiple metal cofactors: The heterologously expressed multidomain [FeFe]-hydrogenase from Megasphaera elsdenii.. Biochimica biophysica acta (BBA) - Bioenergetics, 2016, 1857 (11), pp.1734-1740. ⟨10.1016/j.bbabio.2016.07.002⟩. ⟨hal-01353393⟩
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