Chemical assembly of multiple metal cofactors : The heterologously expressed multidomain [FeFe]-hydrogenase from Megasphaera elsdenii. Article - Novembre 2016

Georgio Caserta, Agnieszka Adamska-Venkatesh, Ludovic Pecqueur, Mohamed Atta, Artero Vincent, Souvik Roy, Edward Reijerse, Wolfgang Lubitz, Marc Fontecave

Georgio Caserta, Agnieszka Adamska-Venkatesh, Ludovic Pecqueur, Mohamed Atta, Artero Vincent, Souvik Roy, Edward Reijerse, Wolfgang Lubitz, Marc Fontecave, « Chemical assembly of multiple metal cofactors : The heterologously expressed multidomain [FeFe]-hydrogenase from Megasphaera elsdenii.  », Biochimica biophysica acta (BBA) - Bioenergetics, novembre 2016, pp. 1734-1740. ISSN 0005-2728

Abstract

[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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