63. Alcala-Torano R, Sommer DJ, Bahrami Dizicheh Z, Ghirlanda G (2016) Chapter seventeen
—design strategies for redox active metalloenzymes: applications in hydrogen production.
In: Pecoraro VL (ed) Methods in enzymology. Academic Press, pp 389–416
64. Sano Y, Onoda A, Hayashi T (2011) A hydrogenase model system based on the sequence of
cytochrome c: photochemical hydrogen evolution in aqueous media. Chem Commun
47:8229. https://doi.org/10.1039/c1cc11157d
65. Sano Y, Onoda A, Hayashi T (2012) Photocatalytic hydrogen evolution by a diiron
hydrogenase model based on a peptide fragment of cytochrome c556 with an attached diiron
carbonyl cluster and an attached ruthenium photosensitizer. J Inorg Chem 108:159–162.
https://doi.org/10.1016/j.jinorgbio.2011.07.010
66. Onoda A, Kihara Y, Fukumoto K, Sano Y, Hayashi T (2014) Photoinduced hydrogen
evolution catalyzed by a synthetic diiron dithiolate complex embedded within a protein
matrix. ACS Catal 4:2645–2648. https://doi.org/10.1021/cs500392e
67. Chen W, Li S, Li X, Zhang C, Hu X, Zhu F, Shen G, Feng F (2019) Iron sulfur clusters in
protein nanocages for photocatalytic hydrogen generation in acidic aqueous solutions. Chem
Sci 10:2179–2185. https://doi.org/10.1039/C8SC05293J
68. Hu X, Chen W, Li S, Sun J, Du K, Xia Q, Feng F (2019) Diiron dithiolate complex induced
helical structure of histone and application in photochemical hydrogen generation. ACS
Appl Mater Interfaces 11:19691–19699. https://doi.org/10.1021/acsami.9b01866
69. Sommer DJ, Vaughn MD, Ghirlanda G (2014) Protein secondary-shell interactions enhance
the photoinduced hydrogen production of cobalt protoporphyrin IX. Chem Commun
50:15852–15855. https://doi.org/10.1039/C4CC06700B
70. Sommer DJ, Vaughn MD, Clark BC, Tomlin J, Roy A, Ghirlanda G (2016) Reengineering
cyt b562 for hydrogen production: a facile route to artificial hydrogenases. Biochim Biophys
Acta BBA—Bioenerg 1857:598–603. https://doi.org/10.1016/j.bbabio.2015.09.001
71. Artz J, Müller TE, Thenert K, Kleinekorte J, Meys R, Sternberg A, Bardow A, Leitner W
(2018) Sustainable conversion of carbon dioxide: an integrated review of catalysis and life
cycle assessment. Chem Rev 118:434–504. https://doi.org/10.1021/acs.chemrev.7b00435
72. Shi J, Jiang Y, Jiang Z, Wang X, Wang X, Zhang S, Han P, Yang C (2015) Enzymatic
conversion of carbon dioxide. Chem Soc Rev 44:5981–6000. https://doi.org/10.1039/
C5CS00182J
73. Schneider CR, Shafaat HS (2016) An internal electron reservoir enhances catalytic CO 2
reduction by a semisynthetic enzyme. Chem Commun 52:9889–9892. https://doi.org/10.
1039/C6CC03901D
74. Schneider CR, Manesis AC, Stevenson MJ, Shafaat HS (2018) A photoactive semisynthetic
metalloenzyme exhibits complete selectivity for CO 2 reduction in water. Chem Commun
54:4681–4684. https://doi.org/10.1039/C8CC01297K
75. Amao Y (2018) Formate dehydrogenase for CO 2 utilization and its application. J CO2 Util
26:623–641. https://doi.org/10.1016/j.jcou.2018.06.022
76. Laureanti JA, Buchko GW, Katipamula S, Su Q, Linehan JC, Zadvornyy OA, Peters JW,
O’Hagan M (2019) Protein scaffold activates catalytic co 2 hydrogenation by a rhodium bis
(diphosphine) complex. ACS Catal 9:620–625. https://doi.org/10.1021/acscatal.8b02615
77. Gamenara D, Domínguez de María P (2014) Enantioselective imine reduction catalyzed by
imine reductases and artificial metalloenzymes. Org Biomol Chem 12:2989–2992. https://
doi.org/10.1039/C3OB42205D
78. Bembenek ME, Abell CW, Chrisey LA, Rozwadowska MD, Gessner W, Brossi A (1990)
Inhibition of monoamine oxidases A and B by simple isoquinoline alkaloids: racemic and
optically active 1,2,3,4-tetrahydro-, 3,4-dihydro-, and fully aromatic isoquinolines. J Med
Chem 33:147–152. https://doi.org/10.1021/jm00163a025
79. Tundis R, Menichini F, Conforti F, Loizzo MR, Bonesi M, Statti G, Menichini F (2009) A
potential role of alkaloid extracts from Salsola species (Chenopodiaceae) in the treatment of
Alzheimer’s disease. J Enzyme Inhib Med Chem 24:818–824. https://doi.org/10.1080/
14756360802399662
Current Applications of Artificial Metalloenzymes …
405
—design strategies for redox active metalloenzymes: applications in hydrogen production.
In: Pecoraro VL (ed) Methods in enzymology. Academic Press, pp 389–416
64. Sano Y, Onoda A, Hayashi T (2011) A hydrogenase model system based on the sequence of
cytochrome c: photochemical hydrogen evolution in aqueous media. Chem Commun
47:8229. https://doi.org/10.1039/c1cc11157d
65. Sano Y, Onoda A, Hayashi T (2012) Photocatalytic hydrogen evolution by a diiron
hydrogenase model based on a peptide fragment of cytochrome c556 with an attached diiron
carbonyl cluster and an attached ruthenium photosensitizer. J Inorg Chem 108:159–162.
https://doi.org/10.1016/j.jinorgbio.2011.07.010
66. Onoda A, Kihara Y, Fukumoto K, Sano Y, Hayashi T (2014) Photoinduced hydrogen
evolution catalyzed by a synthetic diiron dithiolate complex embedded within a protein
matrix. ACS Catal 4:2645–2648. https://doi.org/10.1021/cs500392e
67. Chen W, Li S, Li X, Zhang C, Hu X, Zhu F, Shen G, Feng F (2019) Iron sulfur clusters in
protein nanocages for photocatalytic hydrogen generation in acidic aqueous solutions. Chem
Sci 10:2179–2185. https://doi.org/10.1039/C8SC05293J
68. Hu X, Chen W, Li S, Sun J, Du K, Xia Q, Feng F (2019) Diiron dithiolate complex induced
helical structure of histone and application in photochemical hydrogen generation. ACS
Appl Mater Interfaces 11:19691–19699. https://doi.org/10.1021/acsami.9b01866
69. Sommer DJ, Vaughn MD, Ghirlanda G (2014) Protein secondary-shell interactions enhance
the photoinduced hydrogen production of cobalt protoporphyrin IX. Chem Commun
50:15852–15855. https://doi.org/10.1039/C4CC06700B
70. Sommer DJ, Vaughn MD, Clark BC, Tomlin J, Roy A, Ghirlanda G (2016) Reengineering
cyt b562 for hydrogen production: a facile route to artificial hydrogenases. Biochim Biophys
Acta BBA—Bioenerg 1857:598–603. https://doi.org/10.1016/j.bbabio.2015.09.001
71. Artz J, Müller TE, Thenert K, Kleinekorte J, Meys R, Sternberg A, Bardow A, Leitner W
(2018) Sustainable conversion of carbon dioxide: an integrated review of catalysis and life
cycle assessment. Chem Rev 118:434–504. https://doi.org/10.1021/acs.chemrev.7b00435
72. Shi J, Jiang Y, Jiang Z, Wang X, Wang X, Zhang S, Han P, Yang C (2015) Enzymatic
conversion of carbon dioxide. Chem Soc Rev 44:5981–6000. https://doi.org/10.1039/
C5CS00182J
73. Schneider CR, Shafaat HS (2016) An internal electron reservoir enhances catalytic CO 2
reduction by a semisynthetic enzyme. Chem Commun 52:9889–9892. https://doi.org/10.
1039/C6CC03901D
74. Schneider CR, Manesis AC, Stevenson MJ, Shafaat HS (2018) A photoactive semisynthetic
metalloenzyme exhibits complete selectivity for CO 2 reduction in water. Chem Commun
54:4681–4684. https://doi.org/10.1039/C8CC01297K
75. Amao Y (2018) Formate dehydrogenase for CO 2 utilization and its application. J CO2 Util
26:623–641. https://doi.org/10.1016/j.jcou.2018.06.022
76. Laureanti JA, Buchko GW, Katipamula S, Su Q, Linehan JC, Zadvornyy OA, Peters JW,
O’Hagan M (2019) Protein scaffold activates catalytic co 2 hydrogenation by a rhodium bis
(diphosphine) complex. ACS Catal 9:620–625. https://doi.org/10.1021/acscatal.8b02615
77. Gamenara D, Domínguez de María P (2014) Enantioselective imine reduction catalyzed by
imine reductases and artificial metalloenzymes. Org Biomol Chem 12:2989–2992. https://
doi.org/10.1039/C3OB42205D
78. Bembenek ME, Abell CW, Chrisey LA, Rozwadowska MD, Gessner W, Brossi A (1990)
Inhibition of monoamine oxidases A and B by simple isoquinoline alkaloids: racemic and
optically active 1,2,3,4-tetrahydro-, 3,4-dihydro-, and fully aromatic isoquinolines. J Med
Chem 33:147–152. https://doi.org/10.1021/jm00163a025
79. Tundis R, Menichini F, Conforti F, Loizzo MR, Bonesi M, Statti G, Menichini F (2009) A
potential role of alkaloid extracts from Salsola species (Chenopodiaceae) in the treatment of
Alzheimer’s disease. J Enzyme Inhib Med Chem 24:818–824. https://doi.org/10.1080/
14756360802399662
Current Applications of Artificial Metalloenzymes …
405