Classification and enzyme kinetics of formate dehydrogenases for biomanufacturing via CO2 utilization

HarnessingEscherichia colifor bio-based production of formate under pressurized H2and CO2gases

“…It is often proposed that group-4 hydrogenases couple H2 production to the translocation of ions across the membrane -as it was recently demonstrated for the membrane-bound hydrogenase (Mbh) from Pyrococcus furiosus (McTernan et al, 2014;Yu et al, 2018). Indeed, the FHL-1 membrane arm exhibits two integral membrane subunits: HycD is predicted to be the membrane anchor for the soluble domain; while HycC is an antiporter-like protein predicted to translocate protons/ions (Schuchmann and Müller, 2013;Ceccaldi et al, 2017;Maia et al, 2017;Müller, 2019;Nielsen et al, 2019). Despite the similarity of the membrane arm of FHL-1 and the Complex I (Schwarz et al, 2018), it is has remained unclear if the E.coli enzyme is capable of translocating ions during disproportionation of formate.…”

Carbon Dioxide Utilisation—The Formate Route

“…FDHs are a heterogeneous and broadly distributed group of enzymes that catalyse the reversible two-electron interconversion of formate and CO 2 (Eq. 1) [94][95][96][97][98][99][100][101]. These enzymes evolved to take part in diverse metabolic pathways, being used by some prokaryotic organism to fix (reduce) CO 2 into formate, while other prokaryotes use FDHs to derive energy, by coupling the formate oxidation (which has a very low reduction potential value, Eº′(CO 2 / HCOO − ) = −0.43 V) to the reduction of several terminal electron acceptors; FDHs are also broadly used by both prokaryotes and eukaryotes in C1 metabolism.…”

“…These enzymes are widespread, being found in bacteria, yeasts, fungi and plants, are all (as far as is known) NAD-dependent and belong to the D-specific dehydrogenases of 2-oxyacids family. The other class-the metal-dependent FDHs class 3 -comprises only prokaryotic enzymes that hold different redox-active centres (Table 1) and whose active site harbours one molybdenum or one tungsten centre (molybdenum-containing FDH (Mo-FDH) or tungsten-containing FDH (W-FDH), respectively) [94][95][96][97][98][99][100][101][110][111][112]. (Fig.…”

“…Depending on the enzyme (on the biochemical pathway where the enzyme is involved in), the physiological redox partner can be membrane Fig. 11 Hydride transfer mechanism proposed for metal-independent NAD-dependent formate dehydrogenases quinols, cytoplasmatic and periplasmatic cytochromes, ferredoxins, NAD(P) or coenzyme F 420 [94][95][96][97][98][99][100][101]. For those enzymes like the dihydrogen-dependent CO 2 reductase (see above), the electrons are directly provided by the co-substrate oxidation (dihydrogen in this case) that occurs in the enzyme second active site.…”

Understanding How the Rate of C–H Bond Cleavage Affects Formate Oxidation Catalysis by a Mo-Dependent Formate Dehydrogenase

“…Metal-dependent formate dehydrogenases (FDHs) are paradigm electrocatalysts for the interconversion of CO 2 and formate, 1 , 2 and play a versatile range of roles in biological systems. 3 The FDHs from several organisms, including Desulfovibrio desulfuricans , 4 Rhodobacter capsulatus , 5 Cupriavidus necator (formerly Ralstonia eutropha ), 6 Escherichia coli , 2 Syntrophobacter fumaroxidans , 1 , 7 Acetobacterium woodi , 8 Methylobacterium extorquens , 9 Rhodobacter aestuarii , 10 and Methanococcus maripaludis , 11 have all been reported to catalyze both formate oxidation and CO 2 reduction in assays using solution electron donors/acceptors, although their relative rates of CO 2 reduction vary widely. The enzymes from S. fumaroxidans , D. vulgaris Hildenborough, and E. coli , which are the W-dependent FDHs Sf FDH1 1 and Dv FDH 12 , 13 and the Mo-dependent Ec FDH-H, 2 respectively, have further been shown to perform thermodynamically reversible (efficient) reduction of CO 2 to formate when immobilized on electrodes.…”