Methyl-coenzyme M reductase (MCR) is the key enzyme in both the biological formation of methane by methanogenic Archaea and in the anaerobic oxidation of methane by their methanotrophic counterparts. Although MCR and methanogenic Archaea have received attention in the past for possible biological methane production there is now also interest in the possible engineering of these organisms for the conversion of methane into a liquid biofuel. Since this might require the expression of recombinant enzyme it is important to understand all the requirements to obtain an active enzyme. First of all, MCR contains the hydroporphinoid nickel complex coenzyme F<sub>430</sub> in its active site, and the Ni center has to be in its Ni(I) valence state for the enzyme to be active. Until now, no in vitro method that fully converted the inactive MCRsilent-Ni(II) form to the active MCRred1-Ni(I) form has been described. We recently purified the whole activating enzyme complex (A3a) and showed that the activation process, using electrons from molecular hydrogen, would require and electron bifurcation step and an ATP hydrolysis step, couple to iron-sulfur-cluster-based electron transfer. Currently the different enzymatic components are being expressed and their role in the whole activation process studied. This work will be presented.

Activation of methyl-coenzyme M reductase, the enzyme involved in methane production or consumption in Archaea

251st National Meeting (2016)

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