111. Jeschek M, Reuter R, Heinisch T, Trindler C, Klehr J, Panke S, Ward TR (2016) Directed
evolution of artificial metalloenzymes for in vivo metathesis. Nature 537:661–665. https://
doi.org/10.1038/nature19114
112. Vong K, Eda S, Kadota Y, Nasibullin I, Wakatake T, Yokoshima S, Shirasu K, Tanaka K
(2019) An artificial metalloenzyme biosensor can detect ethylene gas in fruits and
Arabidopsis leaves. Nat Commun 10:5746. https://doi.org/10.1038/s41467-019-13758-2
113. Eda S, Nasibullin I, Vong K, Kudo N, Yoshida M, Kurbangalieva A, Tanaka K (2019)
Biocompatibility and therapeutic potential of glycosylated albumin artificial metalloenzymes. Nat Catal 2:780–792. https://doi.org/10.1038/s41929-019-0317-4
114. Grimm AR, Sauer DF, Polen T, Zhu L, Hayashi T, Okuda J, Schwaneberg U (2018) A
whole cell E. coli display platform for artificial metalloenzymes: poly(phenylacetylene)
production with a rhodium-nitrobindin metalloprotein. ACS Catal 8:2611–2614. https://doi.
org/10.1021/acscatal.7b04369
115. Völker T, Dempwolff F, Graumann PL, Meggers E (2014) Progress towards bioorthogonal
catalysis with organometallic compounds. Angew Chem Int Ed 53:10536–10540. https://doi.
org/10.1002/anie.201404547
116. Cheng Y, Zong L, López-Andarias J, Bartolami E, Okamoto Y, Ward TR, Sakai N, Matile S
(2019) Cell-penetrating dynamic-covalent benzopolysulfane networks. Angew Chem Int Ed
58:9522–9526. https://doi.org/10.1002/anie.201905003
117. Heinisch T, Schwizer F, Garabedian B, Csibra E, Jeschek M, Vallapurackal J, Pinheiro VB,
Marlière P, Panke S, Ward TR (2018) E. coli surface display of streptavidin for directed
evolution of an allylic deallylase. Chem Sci 9:5383–5388. https://doi.org/10.1039/
C8SC00484F
118. Szponarski M, Schwizer F, Ward TR, Gademann K (2018) On-cell catalysis by surface
engineering of live cells with an artificial metalloenzyme. Commun Chem 1:84. https://doi.
org/10.1038/s42004-018-0087-y
119. Zhao J, Rebelein JG, Mallin H, Trindler C, Pellizzoni MM, Ward TR (2018) Genetic
Engineering of an Artificial Metalloenzyme for Transfer Hydrogenation of a
Self-Immolative Substrate in Escherichia coil’s Periplasm. J Am Chem Soc 140:13171–
13175. https://doi.org/10.1021/jacs.8b07189
120. Tsutsumi H, Katsuyama Y, Izumikawa M, Takagi M, Fujie M, Satoh N, Shin-ya K,
Ohnishi Y (2018) Unprecedented cyclization catalyzed by a cytochrome P450 in benzastatin
biosynthesis. J Am Chem Soc 140:6631–6639. https://doi.org/10.1021/jacs.8b02769
121. Breslow R, Gellman SH (1982) Tosylamidation of cyclohexane by a cytochrome P-450
model. J Chem Soc Chem Commun 1400–1401. https://doi.org/10.1039/c39820001400
122. Breslow R, Gellman SH (1983) Intramolecular nitrene carbon-hydrogen insertions mediated
by transition-metal complexes as nitrogen analogs of cytochrome P-450 reactions. J Am
Chem Soc 105:6728–6729. https://doi.org/10.1021/ja00360a039
123. Svastits EW, Dawson JH, Breslow R, Gellman SH (1985) Functionalized nitrogen atom
transfer catalyzed by cytochrome P-450. J Am Chem Soc 107:6427–6428. https://doi.org/10.
1021/ja00308a064
124. Mansuy D, Mahy J-P, Dureault A, Bedi G, Battioni P (1984) Iron- and manganese-porphyrin
catalysed aziridination of alkenes by tosyl- and acyl-iminoiodobenzene. J Chem Soc Chem
Commun 1161–1163. https://doi.org/10.1039/c39840001161
125. Singh R, Kolev JN, Sutera PA, Fasan R (2015) Enzymatic C(sp
3
)-H amination:
P450-catalyzed conversion of carbonazidates into oxazolidinones. ACS Catal 5:1685–
1691. https://doi.org/10.1021/cs5018612
126. Singh R, Bordeaux M, Fasan R (2014) P450-catalyzed intramolecular sp 3 C–H amination
with arylsulfonyl azide substrates. ACS Catal 4:546–552. https://doi.org/10.1021/cs400893n
127. Dydio P, Key HM, Hayashi H, Clark DS, Hartwig JF (2017) Chemoselective, enzymatic C–
H bond amination catalyzed by a cytochrome P450 containing an Ir(Me)-PIX cofactor. J Am
Chem Soc 139:1750–1753. https://doi.org/10.1021/jacs.6b11410
408
J.-P. Mahy et al.
evolution of artificial metalloenzymes for in vivo metathesis. Nature 537:661–665. https://
doi.org/10.1038/nature19114
112. Vong K, Eda S, Kadota Y, Nasibullin I, Wakatake T, Yokoshima S, Shirasu K, Tanaka K
(2019) An artificial metalloenzyme biosensor can detect ethylene gas in fruits and
Arabidopsis leaves. Nat Commun 10:5746. https://doi.org/10.1038/s41467-019-13758-2
113. Eda S, Nasibullin I, Vong K, Kudo N, Yoshida M, Kurbangalieva A, Tanaka K (2019)
Biocompatibility and therapeutic potential of glycosylated albumin artificial metalloenzymes. Nat Catal 2:780–792. https://doi.org/10.1038/s41929-019-0317-4
114. Grimm AR, Sauer DF, Polen T, Zhu L, Hayashi T, Okuda J, Schwaneberg U (2018) A
whole cell E. coli display platform for artificial metalloenzymes: poly(phenylacetylene)
production with a rhodium-nitrobindin metalloprotein. ACS Catal 8:2611–2614. https://doi.
org/10.1021/acscatal.7b04369
115. Völker T, Dempwolff F, Graumann PL, Meggers E (2014) Progress towards bioorthogonal
catalysis with organometallic compounds. Angew Chem Int Ed 53:10536–10540. https://doi.
org/10.1002/anie.201404547
116. Cheng Y, Zong L, López-Andarias J, Bartolami E, Okamoto Y, Ward TR, Sakai N, Matile S
(2019) Cell-penetrating dynamic-covalent benzopolysulfane networks. Angew Chem Int Ed
58:9522–9526. https://doi.org/10.1002/anie.201905003
117. Heinisch T, Schwizer F, Garabedian B, Csibra E, Jeschek M, Vallapurackal J, Pinheiro VB,
Marlière P, Panke S, Ward TR (2018) E. coli surface display of streptavidin for directed
evolution of an allylic deallylase. Chem Sci 9:5383–5388. https://doi.org/10.1039/
C8SC00484F
118. Szponarski M, Schwizer F, Ward TR, Gademann K (2018) On-cell catalysis by surface
engineering of live cells with an artificial metalloenzyme. Commun Chem 1:84. https://doi.
org/10.1038/s42004-018-0087-y
119. Zhao J, Rebelein JG, Mallin H, Trindler C, Pellizzoni MM, Ward TR (2018) Genetic
Engineering of an Artificial Metalloenzyme for Transfer Hydrogenation of a
Self-Immolative Substrate in Escherichia coil’s Periplasm. J Am Chem Soc 140:13171–
13175. https://doi.org/10.1021/jacs.8b07189
120. Tsutsumi H, Katsuyama Y, Izumikawa M, Takagi M, Fujie M, Satoh N, Shin-ya K,
Ohnishi Y (2018) Unprecedented cyclization catalyzed by a cytochrome P450 in benzastatin
biosynthesis. J Am Chem Soc 140:6631–6639. https://doi.org/10.1021/jacs.8b02769
121. Breslow R, Gellman SH (1982) Tosylamidation of cyclohexane by a cytochrome P-450
model. J Chem Soc Chem Commun 1400–1401. https://doi.org/10.1039/c39820001400
122. Breslow R, Gellman SH (1983) Intramolecular nitrene carbon-hydrogen insertions mediated
by transition-metal complexes as nitrogen analogs of cytochrome P-450 reactions. J Am
Chem Soc 105:6728–6729. https://doi.org/10.1021/ja00360a039
123. Svastits EW, Dawson JH, Breslow R, Gellman SH (1985) Functionalized nitrogen atom
transfer catalyzed by cytochrome P-450. J Am Chem Soc 107:6427–6428. https://doi.org/10.
1021/ja00308a064
124. Mansuy D, Mahy J-P, Dureault A, Bedi G, Battioni P (1984) Iron- and manganese-porphyrin
catalysed aziridination of alkenes by tosyl- and acyl-iminoiodobenzene. J Chem Soc Chem
Commun 1161–1163. https://doi.org/10.1039/c39840001161
125. Singh R, Kolev JN, Sutera PA, Fasan R (2015) Enzymatic C(sp
3
)-H amination:
P450-catalyzed conversion of carbonazidates into oxazolidinones. ACS Catal 5:1685–
1691. https://doi.org/10.1021/cs5018612
126. Singh R, Bordeaux M, Fasan R (2014) P450-catalyzed intramolecular sp 3 C–H amination
with arylsulfonyl azide substrates. ACS Catal 4:546–552. https://doi.org/10.1021/cs400893n
127. Dydio P, Key HM, Hayashi H, Clark DS, Hartwig JF (2017) Chemoselective, enzymatic C–
H bond amination catalyzed by a cytochrome P450 containing an Ir(Me)-PIX cofactor. J Am
Chem Soc 139:1750–1753. https://doi.org/10.1021/jacs.6b11410
408
J.-P. Mahy et al.