Enzyme Activity Measurement of Formylmethanofuran Dehydrogenase

Creative enzymes is a company which focuses on enzyme related products and services for various industrial applications. Our services of enzyme activity assays have gained good reputation from thousands of customers. We provide precise testing methods with accurate and reproducible results. We are specialized in testing oxidoreductase such as formylmethanofuran dehydrogenase.

Formylmethanofuran dehydrogenase is a multi-subunit molybdenum iron-sulfur protein found in methanogenic and sulfate-reducing archaea. This enzyme needs pterin as a cofactor to carry its catalysis activity. Besides, molybdate can also be replaced by tungstate. The reaction catalyzed by formylmethanofuran dehydrogenase is the reversible conversion from formylmethanofuran (formyl-MFR) to methanofuran (MFR’), accompanied by the generation of CO₂ and a small molecule electron acceptor in the reduced form. For example, methyl viologen and benzyl viologen can act as acceptors.

Nowadays, more and more studies have been done on methanogenic bacteria considering the emerging need of clean energy. The biochemical steps in methanogenesis from CO₂ are well known and start being employed in the industrial production system. Formylmethanofuran dehydrogenase catalyzes the first step involved in the methanogenesis pathway from CO₂. This is an energy-consuming step and dependent on reduced ferredoxin. This enzyme also participates in methanogenesis from H₂ and CO₂ and oxidation of methyl-coenzyme M into CO₂, both of which are important metabolism pathway for methane production. Meanwhile, the fmdE gene encoding the catalytic subunits is isolated from anaerobic marine sediments and identified to have a significant impact on the global environment by consuming methane (reverse methanogenesis), affecting the levels of atmospheric methane as a greenhouse gas. It can be seen that the central role of formylmethanofuran dehydrogenase in multiple industries is irreplaceable. Up till now, an increasing number of research on its functions, characteristics, catalysis mechanisms, and applications is in progress. The crystal structure of Methanothermobacter wolfii formylmethanofuran dehydrogenase recently published on “Science” also greatly promoted related research. Creative Enzymes would like to further facilitate the research activities by providing rapid and accurate activity measurement of the enzymes.

Figure: The crystal structure of tungsten-containing from Methanothermobacter wolfii, orthorhombic form.
Reference: Wagner, T et al. Science. 2016 354: 114-117

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