Fig. 1: Functional reconstitution of a metal-dependent formate dehydrogenase from C. necator in E. coli.

a Schematic diagram of FDH proteins and genes used in this study highlighting the structural complexity of cnFDH and cofactors required for functionality. b Schematic diagram of the metabolism of E. coli ∆lpd showing reactions disrupted by the deletion of lpd (red cross) and the flux of carbon through the non-oxidative glyoxylate shunt (green). c Growth curves showing the rescue of the ∆lpd strain in a minimal medium containing 20 mM acetate and 60 mM formate (n = 4). Only the induction level that minimized the doubling time for each condition (0.5 mM IPTG for pBbS1k_psFDH and 0.05 mM IPTG for pBbS1k_cnFDH) is shown here for clarity (additional induction conditions are shown in Supplementary Fig. 1). d Extracted doubling times from the growth curves displayed in c showing a significant (p = 0.004) decrease in doubling time of ∆lpd with rescue by cnFDH (n = 4). Statistical analysis was performed using a two-tailed t-test. e Proteome allocation to FDH protein subunits in each condition shown in c and d. psFDH accounted for roughly 100 times more of the proteome than the cnFDH complex, likely imparting a burden which could explain the difference in doubling time (n = 4). Individual data points are shown as the sum of all FDH subunits within each biological sample. Data represent the mean ± s.d. of biological replicates. Source data are provided as a Source Data file.