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The use of CO2 as a chemical building block is of considerable interest. To achieve carbon fixation at ambient conditions, (de)carboxylase enzymes offer an attractive route but frequently require elevated [CO2] levels to yield the acid product. However, it has recently been shown that the coupling of a UbiD-type decarboxylase with carboxylic acid reductase yields the corresponding aldehyde product at near ambient [CO2]. Here, we show this approach can be expanded to different UbiD and CAR enzymes to yield alternative products, in this case, the production of pyrrole-2-carbaldehyde from pyrrole, using Pseudomonas aeruginosa HudA/PA0254 in combination with Segniliparus rotundus CAR. This confirms the varied substrate range of the respective UbiD and CAR enzymes can be harnessed in distinct combinations to support production of a wide range of aldehydes via enzymatic CO2 fixation.