A tiny 20-link protein chain allows bacteria to produce hydrogen fuel even in the presence of toxic oxygen.
Creating biohydrogen is usually impossible in normal air because oxygen immediately shuts down the necessary enzymes. This synthetic peptide self-assembles into a protective cage that shields the electron-transfer chain from the surrounding environment. It allows E. coli to keep churning out fuel in conditions that would normally kill the process. The shell-free design is much simpler than traditional methods and does not require complex genetic engineering of the entire cell. This breakthrough could finally make biological hydrogen a viable, low-cost source of clean energy.
Shell-free peptide-driven nanocompartmentation of an electron-transfer chain boosts oxygen-tolerant biohydrogen production
SSRN · 6710686
Oxygen sensitivity of hydrogenases remains a principal barrier to aerobic biohydrogen. In this study, we exploit a 20-residue metabolosome peptide (PduP20) that self-assembles into a polar α-helical nanodomain, quantitatively sequestering an electron-transfer chain (HydA–Fd–FNR) for robust hydrogen-production in Escherichia coli without proteinaceous shells. The aggregated system exhibits markedly improved hydrogen production and oxygen tolerance compared with a conventional free hydrogenase sys