Catalysis at the Interface- Elucidation of the Activation Process and Coupling of Catalysis and Compartmentalization of the Peripheral Membrane Protein Pyruvate Oxidase from Escherichia coli

TL;DRAbstract

The thiamine- and flavin-dependent peripheral membrane protein pyruvate oxidase from E. coli (EcPOX) catalyzes the oxidative decarboxylation of the central metabolite pyruvate to CO2 and acetate with a concomitant electron transfer step to ubiquinone 8 (Q8), a membrane-bound mobile carrier of the respiratory chain. Association of EcPOX to the lipid bilayer is conferred by the last 23 amino acids of the C-terminal part which form an amphipathic helix in the presence of membranes. Binding to the lipid bilayer is not only mandatory for feeding the reducing equivalents into the electron transport chain, but also leads to enhancement of the catalytic activity of the enzyme. In this thesis the activation and membrane binding mechanism of EcPOX was investigated. EcPOX was used as well-suited model system to analyze the impact of multiple amino acids on an enzymes activation mechanism and eventual bilayer association. Intensive kinetic and thermodynamic studies were performed in combination wi

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