TON. Apart from the simple applications described above, ArMs have also been
used for the development of cascade reactions by association with natural enzymes
for dynamic kinetic resolution of amines or for the stereoselective synthesis of
L-pipecolic acid. Finally, the capacity of ArMs to catalyze abiotic reactions in
biological medium opens new opportunities to improve the toolbox of bioorthogonal chemistry applications. This prompted the scientific community to develop
catalytic hybrid systems operating in vivo and some exciting constructs have been
obtained for olefin metathesis, polymerization of phenylacetylene, uncaging by
deallylation, C–N and C–C bond formation, as well as Diels–Alder reactions. There
is no doubt that artificial metalloenzymes have a bright future ahead as sustainable
and environmentally friendly catalysts.
References
1. Degtyarenko K (2005) Metalloproteins. Encycl Genet Genom Prot Bioinf g306204. https://
doi.org/10.1002/047001153X.g306204
2. Valdez CE, Smith QA, Nechay MR, Alexandrova AN (2014) Mysteries of metals in
metalloenzymes. Acc Chem Res 47:3110–3117. https://doi.org/10.1021/ar500227u
3. Que L, Tolman WB (2008) Biologically inspired oxidation catalysis. Nature 455:333–340.
https://doi.org/10.1038/nature07371
4. Liu J-Y, Li X-F, Li Y-Z, Chang W-B, Huang A-J (2002) Oxidation of styrene by various
oxidants with different kinds of metalloporphyrins. J Mol Catal Chem 187:163–167. https://
doi.org/10.1016/S1381-1169(02)00137-1
5. Meunier B (1992) Metalloporphyrins as versatile catalysts for oxidation reactions and
oxidative DNA cleavage. Chem Rev 92:1411–1456. https://doi.org/10.1021/cr00014a008
6. de Araujo Tôrres MG, da Silva VS, Idemori YM, DeFreitas-Silva G (2017) Manganese
porphyrins as efficient catalysts in solvent-free cyclohexane oxidation. Arab J Chem
S1878535217302423. https://doi.org/10.1016/j.arabjc.2017.12.007
7. Barona-Castaño J, Carmona-Vargas C, Brocksom T, de Oliveira K (2016) Porphyrins as
catalysts in scalable organic reactions. Molecules 21:310. https://doi.org/10.3390/
molecules21030310
8. 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
9. Mahy J-P, Ghattas W, Di Méo T, Ricoux R (2018) Artificial metalloenzymes (Chap. 3). In:
Williams G, Hall M (eds) Catalysis Series. Royal Society of Chemistry, Cambridge, pp 53–87
10. Mahy J-P, Raffy Q, Allard M, Ricoux R (2009) Various strategies for obtaining artificial
hemoproteins: From “hemoabzymes” to “hemozymes”. Biochimie 91:1321–1323. https://
doi.org/10.1016/j.biochi.2009.03.002
11. Mahy J-P, Maréchal J-D, Ricoux R (2014) Various strategies for obtaining oxidative
artificial hemoproteins with a catalytic oxidative activity: from “Hemoabzymes” to
“Hemozymes”? J Porphyr Phthalocyanines 18:1063–1092. https://doi.org/10.1142/
S1088424614500813
12. Ricoux R, Dubuc R, Dupont C, Marechal J-D, Martin A, Sellier M, Mahy J-P (2008)
Hemozymes peroxidase activity of artificial hemoproteins constructed from the streptomyces
lividans Xylanase A and Iron(III)-carboxy-substituted porphyrins. Bioconjug Chem 19:899–
910. https://doi.org/10.1021/bc700435a
Current Applications of Artificial Metalloenzymes …
401
used for the development of cascade reactions by association with natural enzymes
for dynamic kinetic resolution of amines or for the stereoselective synthesis of
L-pipecolic acid. Finally, the capacity of ArMs to catalyze abiotic reactions in
biological medium opens new opportunities to improve the toolbox of bioorthogonal chemistry applications. This prompted the scientific community to develop
catalytic hybrid systems operating in vivo and some exciting constructs have been
obtained for olefin metathesis, polymerization of phenylacetylene, uncaging by
deallylation, C–N and C–C bond formation, as well as Diels–Alder reactions. There
is no doubt that artificial metalloenzymes have a bright future ahead as sustainable
and environmentally friendly catalysts.
References
1. Degtyarenko K (2005) Metalloproteins. Encycl Genet Genom Prot Bioinf g306204. https://
doi.org/10.1002/047001153X.g306204
2. Valdez CE, Smith QA, Nechay MR, Alexandrova AN (2014) Mysteries of metals in
metalloenzymes. Acc Chem Res 47:3110–3117. https://doi.org/10.1021/ar500227u
3. Que L, Tolman WB (2008) Biologically inspired oxidation catalysis. Nature 455:333–340.
https://doi.org/10.1038/nature07371
4. Liu J-Y, Li X-F, Li Y-Z, Chang W-B, Huang A-J (2002) Oxidation of styrene by various
oxidants with different kinds of metalloporphyrins. J Mol Catal Chem 187:163–167. https://
doi.org/10.1016/S1381-1169(02)00137-1
5. Meunier B (1992) Metalloporphyrins as versatile catalysts for oxidation reactions and
oxidative DNA cleavage. Chem Rev 92:1411–1456. https://doi.org/10.1021/cr00014a008
6. de Araujo Tôrres MG, da Silva VS, Idemori YM, DeFreitas-Silva G (2017) Manganese
porphyrins as efficient catalysts in solvent-free cyclohexane oxidation. Arab J Chem
S1878535217302423. https://doi.org/10.1016/j.arabjc.2017.12.007
7. Barona-Castaño J, Carmona-Vargas C, Brocksom T, de Oliveira K (2016) Porphyrins as
catalysts in scalable organic reactions. Molecules 21:310. https://doi.org/10.3390/
molecules21030310
8. 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
9. Mahy J-P, Ghattas W, Di Méo T, Ricoux R (2018) Artificial metalloenzymes (Chap. 3). In:
Williams G, Hall M (eds) Catalysis Series. Royal Society of Chemistry, Cambridge, pp 53–87
10. Mahy J-P, Raffy Q, Allard M, Ricoux R (2009) Various strategies for obtaining artificial
hemoproteins: From “hemoabzymes” to “hemozymes”. Biochimie 91:1321–1323. https://
doi.org/10.1016/j.biochi.2009.03.002
11. Mahy J-P, Maréchal J-D, Ricoux R (2014) Various strategies for obtaining oxidative
artificial hemoproteins with a catalytic oxidative activity: from “Hemoabzymes” to
“Hemozymes”? J Porphyr Phthalocyanines 18:1063–1092. https://doi.org/10.1142/
S1088424614500813
12. Ricoux R, Dubuc R, Dupont C, Marechal J-D, Martin A, Sellier M, Mahy J-P (2008)
Hemozymes peroxidase activity of artificial hemoproteins constructed from the streptomyces
lividans Xylanase A and Iron(III)-carboxy-substituted porphyrins. Bioconjug Chem 19:899–
910. https://doi.org/10.1021/bc700435a
Current Applications of Artificial Metalloenzymes …
401