80. Duerrenberger M, Heinisch T, Wilson YM, Rossel T, Nogueira E, Knoerr L, Mutschler A,
Kersten K, Zimbron MJ, Pierron J, Schirmer T, Ward TR (2011) Artificial transfer
hydrogenases for the enantioselective reduction of cyclic imines. Angew Chem-Int Ed
50:3026–3029. https://doi.org/10.1002/anie.201007820
81. Muñoz Robles V, Dürrenberger M, Heinisch T, Lledós A, Schirmer T, Ward TR, Maréchal
J-D (2014) Structural, kinetic, and docking studies of artificial imine reductases based on
biotin-streptavidin technology: an induced lock-and-key hypothesis. J Am Chem Soc
136:15676–15683. https://doi.org/10.1021/ja508258t
82. Schwizer F, Koehler V, Duerrenberger M, Knoerr L, Ward TR (2013) Genetic optimization
of the catalytic efficiency of artificial imine reductases based on biotin-streptavidin
technology. ACS Catal 3:1752–1755. https://doi.org/10.1021/cs400428r
83. Zimbron JM, Heinisch T, Schmid M, Hamels D, Nogueira ES, Schirmer T, Ward TR (2013)
A dual anchoring strategy for the localization and activation of artificial metalloenzymes
based on the biotin-streptavidin technology. J Am Chem Soc 135:5384–5388. https://doi.
org/10.1021/ja309974s
84. Hestericova M, Heinisch T, Alonso-Cotchico L, Marechal J-D, Vidossich P, Ward TR
(2018) Directed evolution of an artificial imine reductase. Angew Chem-Int Ed 57:1863–
1868. https://doi.org/10.1002/anie.201711016
85. Wilson YM, Duerrenberger M, Nogueira ES, Ward TR (2014) Neutralizing the detrimental
effect of glutathione on precious metal catalysts. J Am Chem Soc 136:8928–8932. https://
doi.org/10.1021/ja500613n
86. Wu S, Zhou Y, Rebelein JG, Kuhn M, Mallin H, Zhao J, Igareta NV, Ward TR (2019)
Breaking symmetry: engineering single-chain dimeric streptavidin as host for artificial
metalloenzymes. J Am Chem Soc 141:15869–15878. https://doi.org/10.1021/jacs.9b06923
87. Monnard FW, Nogueira ES, Heinisch T, Schirmer T, Ward TR (2013) Human carbonic
anhydrase II as host protein for the creation of artificial metalloenzymes: the asymmetric
transfer hydrogenation of imines. Chem Sci 4:3269–3274. https://doi.org/10.1039/
c3sc51065d
88. Heinisch T, Pellizzoni M, Duerrenberger M, Tinberg CE, Koehler V, Klehr J,
Haeussinger D, Baker D, Wardt TR (2015) Improving the catalytic performance of an
artificial metalloenzyme by computational design. J Am Chem Soc 137:10414–10419.
https://doi.org/10.1021/jacs.5b06622
89. Tang BZ, Poon WH, Leung SM, Leung WH, Peng H (1997) Synthesis of stereoregular poly
(phenylacetylene)s by organorhodium complexes in aqueous media. Macromolecules
30:2209–2212. https://doi.org/10.1021/ma961573s
90. Abe S, Hirata K, Ueno T, Morino K, Shimizu N, Yamamoto M, Takata M, Yashima E,
Watanabe Y (2009) Polymerization of phenylacetylene by rhodium complexes within a
discrete space of apo-ferritin. J Am Chem Soc 131:6958–6960. https://doi.org/10.1021/
ja901234j
91. Ke Z, Abe S, Ueno T, Morokuma K (2012) Catalytic mechanism in artificial metalloenzyme:
QM/mm study of phenylacetylene polymerization by rhodium complex encapsulated in
apo-ferritin. J Am Chem Soc 134:15418–15429. https://doi.org/10.1021/ja305453w
92. Onoda A, Fukumoto K, Arlt M, Bocola M, Schwaneberg U, Hayashi T (2012) A rhodium
complex-linked beta-barrel protein as a hybrid biocatalyst for phenylacetylene polymerization. Chem Commun 48:9756–9758. https://doi.org/10.1039/c2cc35165j
93. Kinzel J, Sauer DF, Bocola M, Arlt M, Garakani TM, Thiel A, Beckerle K, Polen T,
Okuda J, Schwaneberg U (2017) 2-Methyl-2,4-pentanediol (MPD) boosts as
detergent-substitute the performance of ß-barrel hybrid catalyst for phenylacetylene
polymerization. Beilstein J Org Chem 13:1498–1506. https://doi.org/10.3762/bjoc.13.148
94. Philippart F, Arlt M, Gotzen S, Tenne S-J, Bocola M, Chen H-H, Zhu L, Schwaneberg U,
Okuda J (2013) A hybrid ring-opening metathesis polymerization catalyst based on an
engineered variant of the b-barrel protein FhuA. Chem Eur J 19:13865–13871. https://doi.
org/10.1002/chem.201301515
406
J.-P. Mahy et al.
Kersten K, Zimbron MJ, Pierron J, Schirmer T, Ward TR (2011) Artificial transfer
hydrogenases for the enantioselective reduction of cyclic imines. Angew Chem-Int Ed
50:3026–3029. https://doi.org/10.1002/anie.201007820
81. Muñoz Robles V, Dürrenberger M, Heinisch T, Lledós A, Schirmer T, Ward TR, Maréchal
J-D (2014) Structural, kinetic, and docking studies of artificial imine reductases based on
biotin-streptavidin technology: an induced lock-and-key hypothesis. J Am Chem Soc
136:15676–15683. https://doi.org/10.1021/ja508258t
82. Schwizer F, Koehler V, Duerrenberger M, Knoerr L, Ward TR (2013) Genetic optimization
of the catalytic efficiency of artificial imine reductases based on biotin-streptavidin
technology. ACS Catal 3:1752–1755. https://doi.org/10.1021/cs400428r
83. Zimbron JM, Heinisch T, Schmid M, Hamels D, Nogueira ES, Schirmer T, Ward TR (2013)
A dual anchoring strategy for the localization and activation of artificial metalloenzymes
based on the biotin-streptavidin technology. J Am Chem Soc 135:5384–5388. https://doi.
org/10.1021/ja309974s
84. Hestericova M, Heinisch T, Alonso-Cotchico L, Marechal J-D, Vidossich P, Ward TR
(2018) Directed evolution of an artificial imine reductase. Angew Chem-Int Ed 57:1863–
1868. https://doi.org/10.1002/anie.201711016
85. Wilson YM, Duerrenberger M, Nogueira ES, Ward TR (2014) Neutralizing the detrimental
effect of glutathione on precious metal catalysts. J Am Chem Soc 136:8928–8932. https://
doi.org/10.1021/ja500613n
86. Wu S, Zhou Y, Rebelein JG, Kuhn M, Mallin H, Zhao J, Igareta NV, Ward TR (2019)
Breaking symmetry: engineering single-chain dimeric streptavidin as host for artificial
metalloenzymes. J Am Chem Soc 141:15869–15878. https://doi.org/10.1021/jacs.9b06923
87. Monnard FW, Nogueira ES, Heinisch T, Schirmer T, Ward TR (2013) Human carbonic
anhydrase II as host protein for the creation of artificial metalloenzymes: the asymmetric
transfer hydrogenation of imines. Chem Sci 4:3269–3274. https://doi.org/10.1039/
c3sc51065d
88. Heinisch T, Pellizzoni M, Duerrenberger M, Tinberg CE, Koehler V, Klehr J,
Haeussinger D, Baker D, Wardt TR (2015) Improving the catalytic performance of an
artificial metalloenzyme by computational design. J Am Chem Soc 137:10414–10419.
https://doi.org/10.1021/jacs.5b06622
89. Tang BZ, Poon WH, Leung SM, Leung WH, Peng H (1997) Synthesis of stereoregular poly
(phenylacetylene)s by organorhodium complexes in aqueous media. Macromolecules
30:2209–2212. https://doi.org/10.1021/ma961573s
90. Abe S, Hirata K, Ueno T, Morino K, Shimizu N, Yamamoto M, Takata M, Yashima E,
Watanabe Y (2009) Polymerization of phenylacetylene by rhodium complexes within a
discrete space of apo-ferritin. J Am Chem Soc 131:6958–6960. https://doi.org/10.1021/
ja901234j
91. Ke Z, Abe S, Ueno T, Morokuma K (2012) Catalytic mechanism in artificial metalloenzyme:
QM/mm study of phenylacetylene polymerization by rhodium complex encapsulated in
apo-ferritin. J Am Chem Soc 134:15418–15429. https://doi.org/10.1021/ja305453w
92. Onoda A, Fukumoto K, Arlt M, Bocola M, Schwaneberg U, Hayashi T (2012) A rhodium
complex-linked beta-barrel protein as a hybrid biocatalyst for phenylacetylene polymerization. Chem Commun 48:9756–9758. https://doi.org/10.1039/c2cc35165j
93. Kinzel J, Sauer DF, Bocola M, Arlt M, Garakani TM, Thiel A, Beckerle K, Polen T,
Okuda J, Schwaneberg U (2017) 2-Methyl-2,4-pentanediol (MPD) boosts as
detergent-substitute the performance of ß-barrel hybrid catalyst for phenylacetylene
polymerization. Beilstein J Org Chem 13:1498–1506. https://doi.org/10.3762/bjoc.13.148
94. Philippart F, Arlt M, Gotzen S, Tenne S-J, Bocola M, Chen H-H, Zhu L, Schwaneberg U,
Okuda J (2013) A hybrid ring-opening metathesis polymerization catalyst based on an
engineered variant of the b-barrel protein FhuA. Chem Eur J 19:13865–13871. https://doi.
org/10.1002/chem.201301515
406
J.-P. Mahy et al.