Ferric hydroxamate uptake protein component A (FhuA) is a monomeric β-barrel protein from the outer membrane of Escherichia coli,¹  and was the second pure protein isolated from the E. coli cell envelope.²  FhuA has attracted great attention since the beginning of phage genetics and molecular biology. FhuA-containing proteoliposomes were used to study the mechanism of phage infection.³  With the crystal structures of FhuA solved,^4–6  its function and properties characterized and the FhuA channel re-engineered, interest in the applications of FhuA expanded to its use as a nanopore integrated in liposome/polymersome membranes for the translocation of compounds in/out of liposomes and polymersomes.^7–9  Various redesigned FhuA variants were investigated, including deletions of the large extracellular loops, deletion of the cork domain, elongation of the hydrophobic membrane region and enlargement of its diameter.^10–12  Molecular understanding of sterically controlled compound release from the FhuA channel provided structural information to achieve triggerable compound release through the FhuA channel.^13,14  Because of its remarkable resistance towards organic solvents, high temperatures and alkaline pH¹⁵  and its robustness in genetic modification, FhuA has become an attractive scaffold for hybrid catalysts (artificial metalloenzymes) to accommodate metal/organic catalysts for improving enantioselectivity.¹⁶  The amino acid side-chain in the interior of the FhuA channel provides a chirally defined second coordination sphere and improves the enantioselectivity of hybrid catalysts. By substituting the amino acid residues surrounding the catalyst complex in the interior of the FhuA channel, one can also optimize the accessibility of the coupling site and the enantioselectivity of the hybrid catalyst.