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Showing 1–7 of 7 results
Advanced filters: Author: Bastian Vogeli Clear advanced filters

  • Cost-effective, environmentally sustainable and energy-efficient ways to address rising atmospheric CO2 levels are urgently needed. Here the authors combine electrochemical reduction of CO2 to formate with biosynthetic conversion of formate to the universal building block acetyl-CoA using a synthetic metabolic pathway called ReForm.

    • Grant M. Landwehr
    • Bastian Vogeli
    • Michael C. Jewett
    Research
    Nature Chemical Engineering
    Volume: 3, P: 57-69

  • Structural and biochemical analysis of propionyl-CoA synthase reveals that it forms a reaction chamber containing three active sites, which sequesters the reactive intermediate acrylyl-CoA during the conversion of 3-hydroxypropionate to propionyl-CoA.

    • Iria Bernhardsgrütter
    • Bastian Vögeli
    • Tobias J. Erb
    Research
    Nature Chemical Biology
    Volume: 14, P: 1127-1132

  • An attractive route for carbon-negative synthesis of biochemical products is the reverse β-oxidation pathway coupled to the Wood-Ljungdahl pathway. Here the authors use a high-throughput in vitro prototyping workflow to screen 762 unique pathway combinations using cell-free extracts tailored for r-BOX to identify enzyme sets for enhanced product selectivity.

    • Bastian Vögeli
    • Luca Schulz
    • Michael C. Jewett
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-10

  • Antibody discovery is bottlenecked by the individual expression and evaluation of antigen specific hits. Here, the authors build an antibody screening workflow leveraging cell-free protein synthesis that enables expression and evaluation of hundreds of antibody fragments in less than 24 h.

    • Andrew C. Hunt
    • Bastian Vögeli
    • Michael C. Jewett
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-14

  • Current efforts to establish synthetic carbon fixation in model heterotrophs rely on expression of heterologous enzymes. Here, the authors explore the presence and activity of a latent CO2-assimilation pathway in E. coli based only on endogenous enzymes and a reversible decarboxylase.

    • Ari Satanowski
    • Beau Dronsella
    • Arren Bar-Even
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-14

  • The use of a presumed chemical intermediate in the mechanism of enoyl thioester reductase enables the identification of the long-sought proton donor and the rational redesign of enzyme stereoselectivity.

    • Raoul G Rosenthal
    • Bastian Vögeli
    • Tobias J Erb
    Research
    Nature Chemical Biology
    Volume: 11, P: 398-400

  • A conserved threonine in medium-chain dehydrogenases/reductases is essential to suppress the formation of an inhibitory side product, which suggests that it functions to destabilize competing transition states rather than to promote positive catalysis.

    • Raoul G Rosenthal
    • Bastian Vögeli
    • Tobias J Erb
    Research
    Nature Chemical Biology
    Volume: 13, P: 745-749