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Gebbink RJMK (2011) Covalent anchoring of a racemization catalyst to CALB-beads:
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org/10.1016/j.tetlet.2011.01.106
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107. Engström K, Johnston EV, Verho O, Gustafson KPJ, Shakeri M, Tai C-W, Bäckvall J-E
(2013) Co-immobilization of an enzyme and a metal into the compartments of mesoporous
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Häussinger D, Hollmann F, Turner NJ, Ward TR (2012) Synthetic cascades are enabled by
combining biocatalysts with artificial metalloenzymes. Nat Chem 5:93–99. https://doi.org/
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109. Okamoto Y, Köhler V, Ward TR (2016) An NAD(P)H-dependent artificial transfer
hydrogenase for multienzymatic cascades. J Am Chem Soc 138:5781–5784. https://doi.org/
10.1021/jacs.6b02470
110. Morra S, Pordea A (2018) Biocatalyst–artificial metalloenzyme cascade based on alcohol
dehydrogenase. Chem Sci 9:7447–7454. https://doi.org/10.1039/C8SC02371A
Current Applications of Artificial Metalloenzymes …
407
monomeric and dendritic Ru-based metathesis catalysts. J Am Chem Soc 122:8168–8179.
https://doi.org/10.1021/ja001179g
96. Jordan JP, Grubbs RH (2007) Small-molecule N-heterocyclic-carbene-containing
olefin-metathesis catalysts for use in water. Angew Chem Int Ed 46:5152–5155. https://
doi.org/10.1002/anie.200701258
97. Sauer DF, Bocola M, Broglia C, Arlt M, Zhu L-L, Brocker M, Schwaneberg U, Okuda J
(2015) Hybrid ruthenium ROMP catalysts based on an engineered variant of b-barrel protein
FhuA DCVFtev: effect of spacer length. Chem Asian J 10:177–182. https://doi.org/10.1002/
asia.201403005
98. Sauer DF, Himiyama T, Tachikawa K, Fukumoto K, Onoda A, Mizohata E, Inoue T,
Bocola M, Schwaneberg U, Hayashi T, Okuda J (2015) A highly active biohybrid catalyst
for olefin metathesis in water: impact of a hydrophobic cavity in a beta-barrel protein. ACS
Catal 5:7519–7522. https://doi.org/10.1021/acscatal.5b01792
99. Grimm AR, Sauer DF, Davari MD, Zhu L, Bocola M, Kato S, Onoda A, Hayashi T,
Okuda J, Schwaneberg U (2018) Cavity size engineering of a beta-barrel protein generates
efficient biohybrid catalysts for olefin metathesis. ACS Catal 8:3358–3364. https://doi.org/
10.1021/acscatal.7b03652
100. Ricca E, Brucher B, Schrittwieser JH (2011) Multi-enzymatic cascade reactions: overview
and perspectives. Adv Synth Catal 353:2239–2262. https://doi.org/10.1002/adsc.201100256
101. O’Reilly E, Turner NJ (2015) Enzymatic cascades for the regio- and stereoselective
synthesis of chiral amines. Perspect Sci 4:55–61. https://doi.org/10.1016/j.pisc.2014.12.009
102. Betanzos-Lara S, Liu Z, Habtemariam A, Pizarro AM, Qamar B, Sadler PJ (2012)
Organometallic Ruthenium and Iridium transfer-hydrogenation catalysts using coenzyme
NADH as a cofactor. Angew Chem Int Ed 51:3897–3900. https://doi.org/10.1002/anie.
201108175
103. Wingstrand E, Laurell A, Fransson L, Hult K, Moberg C (2009) Minor enantiomer
recycling: metal catalyst, organocatalyst and biocatalyst working in concert. Chem Eur J
15:12107–12113. https://doi.org/10.1002/chem.200901338
104. Simons C, Hanefeld U, Arends IWCE, Maschmeyer T, Sheldon RA (2006) Towards
catalytic cascade reactions: asymmetric synthesis using combined chemo-enzymatic
catalysts. Top Catal 40:35–44. https://doi.org/10.1007/s11244-006-0106-6
105. Wieczorek B, Träff A, Krumlinde P, Dijkstra HP, Egmond MR, van Koten G, Bäckvall J-E,
Gebbink RJMK (2011) Covalent anchoring of a racemization catalyst to CALB-beads:
towards dual immobilization of DKR catalysts. Tetrahedron Lett 52:1601–1604. https://doi.
org/10.1016/j.tetlet.2011.01.106
106. Worsdorfer B, Woycechowsky KJ, Hilvert D (2011) Directed evolution of a protein
container. Science 331:589–592. https://doi.org/10.1126/science.1199081
107. Engström K, Johnston EV, Verho O, Gustafson KPJ, Shakeri M, Tai C-W, Bäckvall J-E
(2013) Co-immobilization of an enzyme and a metal into the compartments of mesoporous
silica for cooperative tandem catalysis: an artificial metalloenzyme. Angew Chem Int Ed
52:14006–14010. https://doi.org/10.1002/anie.201306487
108. Köhler V, Wilson YM, Dürrenberger M, Ghislieri D, Churakova E, Quinto T, Knörr L,
Häussinger D, Hollmann F, Turner NJ, Ward TR (2012) Synthetic cascades are enabled by
combining biocatalysts with artificial metalloenzymes. Nat Chem 5:93–99. https://doi.org/
10.1038/nchem.1498
109. Okamoto Y, Köhler V, Ward TR (2016) An NAD(P)H-dependent artificial transfer
hydrogenase for multienzymatic cascades. J Am Chem Soc 138:5781–5784. https://doi.org/
10.1021/jacs.6b02470
110. Morra S, Pordea A (2018) Biocatalyst–artificial metalloenzyme cascade based on alcohol
dehydrogenase. Chem Sci 9:7447–7454. https://doi.org/10.1039/C8SC02371A
Current Applications of Artificial Metalloenzymes …
407