This review focuses on recent advances in the use of elegant bio-orthogonal chemistry in conjunction with rec-DNA to affect highly precise, cost-effective immobilisation of enzymes directly from cell lysate.
Engineering
of biological pathways with man-made materials provides
inspiring blueprints for sustainable drug production. (R)-1-[3,5-Bis(trifluoromethyl)phenyl]ethanol [(R)-3,5-BTPE],
as an important artificial chiral intermediate for complicated pharmaceutical
drugs and biologically active molecules, is often synthesized through
a hydrogenation reaction of 3,5-bis(trifluoromethyl)acetophenone (3,5-BTAP),
in which enantioselectivity and sufficient active hydrogen are the
key to restricting the reaction. In this work, a biohybrid photocatalytic
hydrogenation system based on an artificial cross-linked enzymes (CLEs)-TiO2-Cp*Rh(bpy) photoenzyme is developed through a bottom-up engineering
strategy. Here, TiO2 nanotubes in the presence of Cp*Rh(bpy)
are used to transform NADP+ to NADPH during the formation
of chiral alcohol intermediates from the catalytic reduction of a
ketone substrate by alcohol dehydrogenase CLEs. Hydrogen and electrons,
provided by water and photocatalytic systems, respectively, are transferred
to reduce NADP+ to NADPH via [Cp*Rh(bpy)(H2O)]2+. With the resulting NADPH, [(R)-3,5-BTPE]
is synthesized using our efficient CLEs obtained from the cell lysate
by nonstandard amino acid modification. Through this biohybrid photocatalytic
system, the photoenzyme-catalyzed combined reductive synthesis of
[(R)-3,5-BTPE] has a yield of 41.2% after reaction
for 24 h and a very high enantiomeric excess value (>99.99%). In
the
case of reuse, this biohybrid system retained nearly 95% of its initial
catalytic activity for synthesizing the above chiral alcohol. The
excellent reusability of the CLEs and TiO2 nanotubes hybrid
catalytic materials highlights the environmental friendliness of (R)-3,5-BTPE production.
Enzyme proteins are nanometer-sized molecules with a three-dimensional structure that can be manipulated and assembled into highly ordered nanostructures, which allows access to advanced biological materials. Here, genetically-encoded nonstandard amino...
Correction for ‘Controlled chemical assembly of enzymes in cell lysate enabled by genetic-encoded nonstandard amino acids’ by Jing Zhang et al., Mater. Chem. Front., 2022, 6, 182–193, https://doi.org/10.1039/D1QM01285A.
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