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The electrolysis of dilute CO2 streams suffers from low concentrations of dissolved substrate and its rapid depletion at the electrolyte‐electrocatalyst interface. These limitations require first energy‐intensive CO2 capture and concentration, before electrolyzers can achieve acceptable performances. For direct electrocatalytic CO2 reduction from low‐concentration sources, we introduce a strategy that mimics the carboxysome in cyanobacteria by utilizing microcompartments with nanoconfined enzymes in a porous electrode. A carbonic anhydrase accelerates CO2 hydration kinetics and minimizes substrate depletion by making all dissolved carbon available for utilization, while a highly efficient formate dehydrogenase reduces CO2 cleanly to formate; down to even atmospheric concentrations of CO2. This bio‐inspired concept demonstrates that the carboxysome provides a viable blueprint for the reduction of low‐concentration CO2 streams to chemicals by using all forms of dissolved carbon. [ABSTRACT FROM AUTHOR]

Only two enzymes are capable of directly reducing CO2: CO dehydrogenase, which produces CO at a [NiFe4S4] active site, and formate dehydrogenase, which produces formate at a mononuclear W or Mo active site. Both metalloenzymes are very rapid, energy‐efficient and specific in terms of product. They have been connected to electrodes with two different objectives. A series of studies used protein film electrochemistry to learn about different aspects of the mechanism of these enzymes (reactivity with substrates, inhibitors...). Another series focused on taking advantage of the catalytic performance of these enzymes to build biotechnological devices, from CO2‐reducing electrodes to full photochemical devices performing artificial photosynthesis. Here, we review all these works. [ABSTRACT FROM AUTHOR]