frontiers will certainly emerge, which are not apparent for us now with our current
knowledge. Regardless, it will be very exciting to follow this research at the
intersection of nanotechnology and biology and to see where it takes us in
the upcoming decades.
References
1. San BH, Gusthart J, Lee SS, Kim KK (2018) Metal–enzyme hybrid catalysts in
cascade and multicomponent processes. In: Montserrat D, Bäckvall JE, Pàmies O (eds)
Artificial metalloenzymes and metalloDNAzymes in catalysis: from design to applications.
Wiley-VCH, Weinheim, pp 321–351. https://doi.org/10.1002/9783527804085.ch11
2. Chen M, Zeng G, Xu P, Lai C, Tang L (2017) How do enzymes ‘meet’ nanoparticles
and nanomaterials? Trends Biochem Sci 42:914–930. https://doi.org/10.1016/j.tibs.2017.08.
008
3. Pàmies O, Diéguez M, Bäckvall JE (2015) Artificial metalloenzymes in asymmetric catalysis:
key developments and future directions. Adv Synth Catal 357:1567–1586. https://doi.org/10.
1002/adsc.201500290
4. Macaskie LE, Mkiheenko IP, Omajai JB, Stephen AJ, Wood J (2017) Metallic
bionanocatalysts: potential applications as green catalysts and energy materials. Microb
Biotechnol 10:1171–1180
5. Pinyou P, Blay V, Muresan LM, Noguer T (2019) Enzyme-modified electrodes for biosensors
and biofuel cells. Mater Horiz 6:1336–1358. https://doi.org/10.1039/c9mh00013e
6. Kärkäs MD, Verho O, Åkermark B (2018) Metalloenzyme-inspired systems for
alternative energy harvest. In: Montserrat D, Bäckvall JE, Pàmies O (eds) Artificial
metalloenzymes and metalloDNAzymes in catalysis: from design to applications. WileyVCH, Weinheim, pp 353–381. https://doi.org/10.1002/9783527804085.ch12
7. Lloyd JR, Byrne JM, Coker VS (2011) Biotechnological synthesis of functional
nanomaterials. Curr Opin Biotechnol 22:509–515. https://doi.org/10.1016/j.copbio.2011.06.
008
8. Bruggink A, Schoevaart R, Kieboom T (2003) Concepts of nature in organic synthesis:
cascade catalysis and multistep conversions in concert. Org Process Res Dev 7:622–640.
https://doi.org/10.1021/op0340311
9. Liu J, Chakraborty S, Hosseinzadeh P, Yu Y, Tian S, Petrik I, Bhagi A, Lu Y (2014)
Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers. Chem Rev
114:4366–4469. https://doi.org/10.1021/cr400479b
10. Hoffman BM, Lukoyanov D, Dean DR, Seefeldt LC (2013) Nitrogenase: a draft mechanism.
Acc Chem Res 46:587–595. https://doi.org/10.1021/ar300267m
11. Barber J (2006) Photosystem II: an enzyme of global significance. Biochem Soc Trans
34:619–631. https://doi.org/10.1042/BST0340619
12. Köhler V, Turner NJ (2015) Artificial concurrent catalytic processes involving enzymes.
Chem Commun 51:450–464. https://doi.org/10.1039/C4CC07277D
13. Schwizer F, Okamoto Y, Heinisch T, Gu Y, Pellizzoni MM, Lebrun V, Reuter R, Köhler V,
Lewis JC, Ward TR (2018) Artificial metalloenzymes: reaction scope and optimization
strategies. Chem Rev 118:142–231. https://doi.org/10.1021/acs.chemrev.7b00014
14. Verho O, Bäckvall JE (2015) Chemoenzymatic dynamic kinetic resolution: a powerful
tool for the preparation for the preparation of enantiomerically pure alcohols and amines.
J Am Chem Soc 137:3996–4009. https://doi.org/10.1021/jacs.5b01031
15. Marcos R, Martín-Matute B (2012) Combined enzyme and transition-metal catalysis for
dynamic kinetic resolution. Isr J Chem 52:639–652. https://doi.org/10.1002/ijch.201200012
270
O. Verho and J.-E. Bäckvall
knowledge. Regardless, it will be very exciting to follow this research at the
intersection of nanotechnology and biology and to see where it takes us in
the upcoming decades.
References
1. San BH, Gusthart J, Lee SS, Kim KK (2018) Metal–enzyme hybrid catalysts in
cascade and multicomponent processes. In: Montserrat D, Bäckvall JE, Pàmies O (eds)
Artificial metalloenzymes and metalloDNAzymes in catalysis: from design to applications.
Wiley-VCH, Weinheim, pp 321–351. https://doi.org/10.1002/9783527804085.ch11
2. Chen M, Zeng G, Xu P, Lai C, Tang L (2017) How do enzymes ‘meet’ nanoparticles
and nanomaterials? Trends Biochem Sci 42:914–930. https://doi.org/10.1016/j.tibs.2017.08.
008
3. Pàmies O, Diéguez M, Bäckvall JE (2015) Artificial metalloenzymes in asymmetric catalysis:
key developments and future directions. Adv Synth Catal 357:1567–1586. https://doi.org/10.
1002/adsc.201500290
4. Macaskie LE, Mkiheenko IP, Omajai JB, Stephen AJ, Wood J (2017) Metallic
bionanocatalysts: potential applications as green catalysts and energy materials. Microb
Biotechnol 10:1171–1180
5. Pinyou P, Blay V, Muresan LM, Noguer T (2019) Enzyme-modified electrodes for biosensors
and biofuel cells. Mater Horiz 6:1336–1358. https://doi.org/10.1039/c9mh00013e
6. Kärkäs MD, Verho O, Åkermark B (2018) Metalloenzyme-inspired systems for
alternative energy harvest. In: Montserrat D, Bäckvall JE, Pàmies O (eds) Artificial
metalloenzymes and metalloDNAzymes in catalysis: from design to applications. WileyVCH, Weinheim, pp 353–381. https://doi.org/10.1002/9783527804085.ch12
7. Lloyd JR, Byrne JM, Coker VS (2011) Biotechnological synthesis of functional
nanomaterials. Curr Opin Biotechnol 22:509–515. https://doi.org/10.1016/j.copbio.2011.06.
008
8. Bruggink A, Schoevaart R, Kieboom T (2003) Concepts of nature in organic synthesis:
cascade catalysis and multistep conversions in concert. Org Process Res Dev 7:622–640.
https://doi.org/10.1021/op0340311
9. Liu J, Chakraborty S, Hosseinzadeh P, Yu Y, Tian S, Petrik I, Bhagi A, Lu Y (2014)
Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers. Chem Rev
114:4366–4469. https://doi.org/10.1021/cr400479b
10. Hoffman BM, Lukoyanov D, Dean DR, Seefeldt LC (2013) Nitrogenase: a draft mechanism.
Acc Chem Res 46:587–595. https://doi.org/10.1021/ar300267m
11. Barber J (2006) Photosystem II: an enzyme of global significance. Biochem Soc Trans
34:619–631. https://doi.org/10.1042/BST0340619
12. Köhler V, Turner NJ (2015) Artificial concurrent catalytic processes involving enzymes.
Chem Commun 51:450–464. https://doi.org/10.1039/C4CC07277D
13. Schwizer F, Okamoto Y, Heinisch T, Gu Y, Pellizzoni MM, Lebrun V, Reuter R, Köhler V,
Lewis JC, Ward TR (2018) Artificial metalloenzymes: reaction scope and optimization
strategies. Chem Rev 118:142–231. https://doi.org/10.1021/acs.chemrev.7b00014
14. Verho O, Bäckvall JE (2015) Chemoenzymatic dynamic kinetic resolution: a powerful
tool for the preparation for the preparation of enantiomerically pure alcohols and amines.
J Am Chem Soc 137:3996–4009. https://doi.org/10.1021/jacs.5b01031
15. Marcos R, Martín-Matute B (2012) Combined enzyme and transition-metal catalysis for
dynamic kinetic resolution. Isr J Chem 52:639–652. https://doi.org/10.1002/ijch.201200012
270
O. Verho and J.-E. Bäckvall