Hydrogen-Producing Catalysts Based on Ferredoxin Scaffolds

Abstract

Current attempts to transform our fossil fuel-based society into a sustainable one involve learning from and employing the biochemistry of nature. The process of photosynthesis is exemplary for utilizing sunlight as a regenerative energy source. Enzymes like hydrogenases, which reduce protons to molecular hydrogen (H2) under ambient conditions, are model biocatalysts for generating sustainable, clean fuels. In green algae, photosynthesis and hydrogenases are coupled through ferredoxin, a small electron transfer protein. Here, it is shown that several plant-type ferredoxins can interact with a chemically synthesized active site cofactor analog of [FeFe]-hydrogenases in a way that allows comparably high H2 evolution rates. UV–vis and Fourier-transform infrared spectroscopy indicate that the natural [2Fe-2S] clusters of the ferredoxin hosts must be absent for a functional interaction of polypeptide and cofactor mimic and that the apo-ferredoxins shield the H2-producing cofactor from the solvent. The hybrid proteins exhibited higher O2 tolerance than natural [FeFe]-hydrogenases and generated H2 in light-dependent cascades based on photosystem I or the chemical photosensitizer proflavine. These features and the combination of natural hosts and cofactors might contribute to establishing sustainable light-dependent H2 production systems.