Reduction of CO ₂ Accompanying ATP Synthesis in Polydopamine Microreactors Covered by Lipid Bilayers with ATPase

Abstract

Abstract Global energy and environmental crises have stimulated increased efforts toward converting CO 2 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 CO 2 , combined with FDH, facilitates the reduction of CO 2 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 CO 2 and the mitochondrion's enzymes to synthesize ATP into a unified artificial biomimetic system, effectively replicating the glycolysis process to simultaneously achieve CO 2 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.