Rimoldi, I.

New J. Chem., 2018, 10.1039/C8NJ04558E

Diamine ligands I–IV coordinated to an iridium metal complex with the biotin moiety anchored to the Cp* ring were investigated. This strategy, in contrast to the traditional biotin–streptavidin technology that uses a biotinylated ligand in the artificial imine reductase, is practical for envisaging how the enantiodiscrimination by different Streptavidin (Sav) mutants could influence the chiral environment of the metal cofactor. Only in the case of (R)-CAMPY IV did the chirality at the metal centre and the second coordination sphere environment, which was dictated by the host protein, operate in a synergistic way, producing better enantioselectivity at a S112M Sav catalyst/catalyst ratio of 1.0 : 2.5. Under these optimized conditions, the artificial imine reductase afforded a good enantiomeric excess (83%) in the asymmetric transfer hydrogenation of 6,7-dimethoxy-1-methyl-3,4-dihydroisoquinoline.

Ward, T. R.

J. Am. Chem. Soc., 2013, 10.1021/ja309974s

Artificial metalloenzymes result from anchoring an active catalyst within a protein environment. Toward this goal, various localization strategies have been pursued: covalent, supramolecular, or dative anchoring. Herein we show that introduction of a suitably positioned histidine residue contributes to firmly anchor, via a dative bond, a biotinylated rhodium piano stool complex within streptavidin. The in silico design of the artificial metalloenzyme was confirmed by X-ray crystallography. The resulting artificial metalloenzyme displays significantly improved catalytic performance, both in terms of activity and selectivity in the transfer hydrogenation of imines. Depending on the position of the histidine residue, both enantiomers of the salsolidine product can be obtained.

Ward, T. R.

ChemCatChem, 2014, 10.1002/cctc.201300995

Ward, T. R.

J. Am. Chem. Soc., 2016, 10.1021/jacs.6b02470

Ward, T. R.

J. Organomet. Chem., 2005, 10.1016/j.jorganchem.2005.02.001

Salmain, M.

Appl. Organomet. Chem., 2013, 10.1002/aoc.2929

Hayashi, T

Chem. Commun., 2012, 10.1039/C2CC35165J

Our group recently prepared a hybrid catalyst containing a rhodium complex, Rh(Cp)(cod), with a maleimide moiety at the peripheral position of the Cp ligand. This compound was then inserted into a β-barrel protein scaffold of a mutant of aponitrobindin (Q96C) via a covalent linkage. The hybrid protein is found to act as a polymerization catalyst and preferentially yields trans-poly(phenylacetylene) (PPA), although the rhodium complex without the protein scaffold normally produces cis PPA.

Salmain, M.

Dalton Trans., 2014, 10.1039/c3dt53253d

Ward, T. R.

Org. Biomol. Chem., 2015, 10.1039/c4ob02071e

Ward, T. R.

J. Am. Chem. Soc., 2006, 10.1021/ja061580o

Ward, T. R.

Angew. Chem., Int. Ed., 2011, 10.1002/anie.201007820

McNaughton, B. R.; Rovis, T.

J. Am. Chem. Soc., 2019, 10.1021/jacs.9b01596

Rovis, T.; Ward, T. R.

Science, 2012, 10.1126/science.1226132

Salmain, M.

Org. Biomol. Chem., 2011, 10.1039/c1ob05482a

Ward, T. R.; Woolfson, D. N.

ACS Catal., 2018, 10.1021/acscatal.7b03773

Maréchal, J.-D.

ACS Catal., 2014, 10.1021/cs400921n

Ward, T. R.

Angew. Chem., Int. Ed., 2017, 10.1002/anie.201702181

Maréchal, J.-D.; Ward, T. R.

Angew. Chem., Int. Ed., 2018, 10.1002/anie.201711016

Ward, T. R.

ACS Catal., 2016, 10.1021/acscatal.6b00258

Salmain, M.

Chem. Commun., 2012, 10.1039/c2cc36980j

Rimoldi, I.

ChemCatChem, 2016, 10.1002/cctc.201600116

Ward, T. R.

ChemCatChem, 2014, 10.1002/cctc.201300825

Ward, T. R.

Dalton Trans., 2018, 10.1039/C8DT02224K

Ward, T. R.

ChemCatChem, 2013, 10.1002/cctc.201200834

Ward, T. R.

J. Am. Chem. Soc., 2018, 10.1021/jacs.8b07189

Ward, T. R.

ACS Catal., 2013, 10.1021/cs400428r

Jaussi, R.

Protein Expression Purif., 2014, 10.1016/j.pep.2013.10.015

Ward, T. R.

Chem. Sci., 2013, 10.1039/c3sc51065d

Shahgaldian, P.; Ward, T. R.

Chem. Commun., 2016, 10.1039/c6cc04604e

Ueno, T.

Chem. Commun., 2016, 10.1039/C6CC00679E