Reduction of CO₂ Accompanying ATP Synthesis in Polydopamine Microreactors Covered by Lipid Bilayers with ATPase

Global energy and environmental crises have stimulated increased efforts toward converting CO₂ into valuable chemicals or energy substance. Inspired by natural chloroplasts and mitochondria, we build an innovative polydopamine-armored multiple enzyme microreactor for co-immobilizing glyceraldehyde-3-phosphate dehydrogenase (GAPDH), 3-phosphoglyceric phosphokinase (PGK), formate dehydrogenase (FDH), and ATPase-incorporating proteoliposome, providing spatially confined microenvironments akin to natural systems. Within this microreactor, GAPDH and PGK catalyze the conversion of glyceraldehyde 3-phosphate to 3-phosphoglyceric acid, reducing β-nicotinamide adenine dinucleotide (NAD⁺) to NADH and generating a proton influx that drives ATP synthesis. The microreactor possesses strong affinity for CO₂, combined with FDH, facilitates the reduction of CO₂ to formic acid, oxidizing NADH back to NAD⁺ and enabling the recycling of the NAD⁺/NADH redox couple. This process further boosts ATP production by contributing additional protons. Such microreactor adeptly orchestrates the chloroplast's enzymes to fix CO₂ and the mitochondrion's enzymes to synthesize ATP into a unified artificial biomimetic system, effectively replicating the glycolysis process to simultaneously achieve CO₂ fixation, NADH regeneration, and ATP synthesis. This strategy not only holds great potential to inspire significant design innovations for more efficient ATP synthesis from low-value substances but also greatly expands the application scenarios for biomolecular motors.