Ueno, T.

Small 2010, 6, 1873-1879, 10.1002/smll.201000772

The synthesis of a robust bio‐nanotube consisting of the β‐helical tubular component proteins of bacteriophage T4 is described. The crystal structure indicates that it has a well‐defined nanoscale length of 10 nm as a result of the head‐to‐head dimerization of β‐helices. Surprisingly, the tube assembly has high thermal stability, high tolerance to organic solvents, and a wide pH‐stability range.

Ueno, T.; Watanabe, Y.

Small 2008, 4, 50-54, 10.1002/smll.200700855

A bionanocup chemical reactor is constructed from a heteroprotein assembly from bacteriophage T4. The preparation of a stable iron(III) porphyrin–bionanocup composite is described. The hydrophobic cup provides a space suitable for the fixation of low‐water‐solubility iron(III) porphyrins. The application of the iron(III) porphyrin–bionanocup composites for the catalysis of sulfoxidation of thioanisoles is demonstrated (see figure).

Mangiatordi, G.F.; Salmain, M.

J. Mol. Catal. B: Enzym. 2015, 122, 314-322, 10.1016/j.molcatb.2015.10.007

Two half-sandwich d6-rhodium(III) complexes of the general formula [(η5-Cp*)Rh(N^N)Cl]Cl where N^N is a phenanthroline or a bispyridine methane derivative carrying a thiol-targeting maleimide or chloroacetamide function were synthesized and characterized. Both complexes were able to catalyse the transfer hydrogenation of 2,2,2-trifluoroacetophenone in aqueous medium using formate or phosphite as hydrogen donor. Covalent anchoring of these complexes to the cysteine endoproteinase papain yielded hybrid metalloproteins with transfer hydrogenase properties. Under optimized conditions of pH, hydrogen donor concentration and catalyst load, conversion of substrate was nearly quantitative within 24 h at 40 °C and the (S)-enantiomer was obtained preferably albeit with a modest enantiomeric excess of 7–10%. Covalent docking simulations complemented the experimental findings suggesting a molecular rationale for the observed low enantioselectivity. The harmonious use of experimental and theoretical approaches represents an unprecedented starting point for driving the rational design of artificial metalloenzymes built up from papain with higher catalytic efficiency.