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56:13618–13622. https://doi.org/10.1002/anie.201704524
160. Deuss PJ, Popa G, Slawin AMZ, Laan W, Kamer PCJ (2013) Artificial copper enzymes for
asymmetric Diels-Alder reactions. Chem Cat Chem 5:1184–1191. https://doi.org/10.1002/
cctc.201200671
161. Bos J, Fusetti F, Driessen AJM, Roelfes G (2012) Enantioselective artificial metalloenzymes
by creation of a novel active site at the protein dimer interface. Angew Chem Int Ed
51:7472–7475. https://doi.org/10.1002/anie.201202070
410
J.-P. Mahy et al.
An artificial metalloenzyme with the kinetics of native enzymes. Science 354:102–106.
https://doi.org/10.1126/science.aah4427
146. Natoli SN, Hartwig JF (2019) Noble–metal substitution in hemoproteins: an emerging
strategy for abiological catalysis. Acc Chem Res 52:326–335. https://doi.org/10.1021/acs.
accounts.8b00586
147. Zhang J, Huang X, Zhang RK, Arnold FH (2019) Enantiodivergent a-amino C–H
fluoroalkylation catalyzed by engineered cytochrome P450s. J Am Chem Soc 141:9798–
9802. https://doi.org/10.1021/jacs.9b04344
148. Otto S, Bertoncin F, Engberts JBFN (1996) Lewis Acid Catalysis of a Diels − Alder
Reaction in Water. J Am Chem Soc 118:7702–7707. https://doi.org/10.1021/ja960318k
149. Otto S, Engberts JBFN (1999) A systematic study of ligand effects on a lewis-acid-catalyzed
Diels–Alder reaction in water: water-enhanced enantioselectivity. J Am Chem Soc
121:6798–6806. https://doi.org/10.1021/ja984273u
150. Mubofu EB, Engberts JBFN (2004) Specific acid catalysis and Lewis acid catalysis of
Diels–Alder reactions in aqueous media. J Phys Org Chem 17:180–186. https://doi.org/10.
1002/poc.711
151. Reetz MT, Jiao N (2006) Copper-phthalocyanine conjugates of serum albumins as
enantioselective catalysts in Diels–Alder reactions. Angew Chem Int Ed 45:2416–2419.
https://doi.org/10.1002/anie.200504561
152. Reetz MT (2012) Artificial Metalloenzymes as Catalysts in Stereoselective Diels-Alder
Reactions. Chem Rec 12:391–406. https://doi.org/10.1002/tcr.201100043
153. Roelfes G, Boersma AJ, Feringa BL (2006) Highly enantioselective DNA-based catalysis.
Chem Commun 635–637. https://doi.org/10.1039/b516552k
154. Filice M, Romero O, Gutiérrez-Fernández J, de las Rivas B, Hermoso JA, Palomo JM (2015)
Synthesis of a heterogeneous artificial metallolipase with chimeric catalytic activity. Chem
Commun 51:9324–9327. https://doi.org/10.1039/C5CC02450A
155. Ghattas W, Cotchico-Alonso L, Maréchal J-D, Urvoas A, Rousseau M, Mahy J-P, Ricoux R
(2016) Artificial metalloenzymes with the neocarzinostatin scaffold: toward a biocatalyst for
the Diels-Alder reaction. ChemBioChem 17:433–440. https://doi.org/10.1002/cbic.
201500445
156. Talbi B, Haquette P, Martel A, de Montigny F, Fosse C, Cordier S, Roisnel T, Jaouen G,
Salmain M (2010) (η6-Arene) ruthenium(II) complexes and metallo-papain hybrid as Lewis
acid catalysts of Diels-Alder reaction in water. Dalton Trans 39:5605–5607. https://doi.org/
10.1039/c001630f
157. Di Meo T, Ghattas W, Herrero C, Velours C, Minard P, Mahy J-P J-P, Ricoux R, Urvoas A
(2017) aRep A3: a versatile artificial scaffold for metalloenzyme design. Chem Eur J
23:10156–10166. https://doi.org/10.1002/chem.201701518
158. Di Meo T, Kariyawasam K, Ghattas W, Valerio-Lepiniec M, Sciortino G, Maréchal J-D,
Minard P, Mahy J-P, Urvoas A, Ricoux R (2019) functionalized artificial bidomain proteins
based on an a-solenoid protein repeat scaffold: a new class of artificial Diels-Alderases. ACS
Omega 4:4437–4447. https://doi.org/10.1021/acsomega.8b03448
159. Himiyama T, Taniguchi N, Kato S, Onoda A, Hayashi T (2017) A pyrene-linked cavity
within a b-barrel protein promotes an asymmetric Diels-Alder reaction. Angew Chem Int Ed
56:13618–13622. https://doi.org/10.1002/anie.201704524
160. Deuss PJ, Popa G, Slawin AMZ, Laan W, Kamer PCJ (2013) Artificial copper enzymes for
asymmetric Diels-Alder reactions. Chem Cat Chem 5:1184–1191. https://doi.org/10.1002/
cctc.201200671
161. Bos J, Fusetti F, Driessen AJM, Roelfes G (2012) Enantioselective artificial metalloenzymes
by creation of a novel active site at the protein dimer interface. Angew Chem Int Ed
51:7472–7475. https://doi.org/10.1002/anie.201202070
410
J.-P. Mahy et al.