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

Caserta, Giorgio, Adamska-Venkatesh, Agnieszka, Pecqueur, Ludovic, Atta, Mohamed, Artero, Vincent, Roy, Souvik, Reijerse, Edward, Lubitz, Wolfgang and Fontecave, Marc (2016) Chemical assembly of multiple metal cofactors: The heterologously expressed multidomain [FeFe]-hydrogenase from Megasphaera elsdenii. Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1857 (11). pp. 1734-1740. ISSN 0005-2728

Full content URL: https://doi.org/10.1016/j.bbabio.2016.07.002

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Item Type:Article
Item Status:Live Archive

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.

Keywords:[FeFe]-hydrogenase, Megasphaera elsdenii, Synthetic maturation, H2 production
Subjects:C Biological Sciences > C720 Biological Chemistry
F Physical Sciences > F100 Chemistry
F Physical Sciences > F161 Organometallic Chemistry
Divisions:College of Science > School of Chemistry
ID Code:40674
Deposited On:17 Apr 2020 09:22

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