31. Mahammed A, Gross Z (2005) Albumin-conjugated corrole metal complexes: extremely
simple yet very efficient biomimetic oxidation systems. J Am Chem Soc 127:2883–2887.
https://doi.org/10.1021/ja045372c
32. Herrero C, Quaranta A, Ricoux R, Trehoux A, Mahammed A, Gross Z, Banse F, Mahy J-P
(2016) Oxidation catalysis via visible-light water activation of a [Ru(bpy) 3 ]
2+ chromophore
BSA–metallocorrole couple. Dalton Trans 45:706–710. https://doi.org/10.1039/C5DT04158A
33. Rousselot-Pailley P, Bochot C, Marchi-Delapierre C, Jorge-Robin A, Martin L,
Fontecilla-Camps JC, Cavazza C, Ménage S (2009) The protein environment drives
selectivity for sulfide oxidation by an artificial metalloenzyme. ChemBioChem 10:545–552.
https://doi.org/10.1002/cbic.200800595
34. Tang J, Huang F, Wei Y, Bian H, Zhang W, Liang H (2016) Bovine serum albumin–cobalt
(II) Schiff base complex hybrid: an efficient artificial metalloenzyme for enantioselective
sulfoxidation using hydrogen peroxide. Dalton Trans 45:8061–8072. https://doi.org/10.
1039/C5DT04507J
35. Hunter CL, Lloyd E, Eltis LD, Rafferty SP, Lee H, Smith M, Mauk AG (1997) Role of the
heme propionates in the interaction of heme with apomyoglobin and apocytochrome b 5 .
Biochemistry 36:1010–1017. https://doi.org/10.1021/bi961385u
36. Hayashi T, Hisaeda Y (2002) New functionalization of myoglobin by chemical modification
of heme-propionates. Acc Chem Res 35:35–43. https://doi.org/10.1021/ar000087t
37. Ueno T, Koshiyama T, Abe S, Yokoi N, Ohashi M, Nakajima H, Watanabe Y (2007) Design
of artificial metalloenzymes using non-covalent insertion of a metal complex into a protein
scaffold. J Organomet Chem 692:142–147. https://doi.org/10.1016/j.jorganchem.2006.08.
043
38. Ueno T, Koshiyama T, Ohashi M, Kondo K, Kono M, Suzuki A, Yamane T, Watanabe Y
(2005) Coordinated design of cofactor and active site structures in development of new
protein catalysts. J Am Chem Soc 127:6556–6562. https://doi.org/10.1021/ja045995q
39. Ohashi M, Koshiyama T, Ueno T, Yanase M, Fujii H, Watanabe Y (2003) Preparation of
artificial metalloenzymes by insertion of chromium(III) Schiff base complexes into
apomyoglobin Mutants. Angew Chem Int Ed 42:1005–1008. https://doi.org/10.1002/anie.
200390256
40. Carey JR, Ma SK, Pfister TD, Garner DK, Kim HK, Abramite JA, Wang Z, Guo Z, Lu Y
(2004) A site-selective dual anchoring strategy for artificial metalloprotein design. J Am
Chem Soc 126:10812–10813. https://doi.org/10.1021/ja046908x
41. Zhang J-L, Garner DK, Liang L, Chen Q, Lu Y (2008) Protein scaffold of a designed
metalloenzyme enhances the chemoselectivity in sulfoxidation of thioanisole. Chem
Commun 1665. https://doi.org/10.1039/b718915j
42. Hayashi T, Murata D, Makino M, Sugimoto H, Matsuo T, Sato H, Shiro Y, Hisaeda Y
(2006) Crystal structure and peroxidase activity of myoglobin reconstituted with iron
porphycene. Inorg Chem 45:10530–10536. https://doi.org/10.1021/ic061130x
43. Ducros V, Charnock SJ, Derewenda U, Derewenda ZS, Dauter Z, Dupont C, Shareck F,
Morosoli R, Kluepfel D, Davies GJ (2000) Substrate specificity in glycoside hydrolase
family 10: structural and kinetic analysis of the Streptomyces Lividans Xylanase 10A. J Biol
Chem 275:23020–23026. https://doi.org/10.1074/jbc.275.30.23020
44. Komatsu T, Ishihara S, Tsuchida E, Nishide H, Morokuma C, Nakamura S (2005)
Heat-resistant oxygen-carrying hemoproteins consist of recombinant xylanases and synthetic
iron(II) porphyrin. Biomacromol 6:1489–1494. https://doi.org/10.1021/bm049255l
45. Ricoux R, Allard M, Dubuc R, Dupont C, Maréchal J-D, Mahy J-P (2009) Selective
oxidation of aromatic sulfide catalyzed by an artificial metalloenzyme: new activity of
hemozymes. Org Biomol Chem 7:3208–3211. https://doi.org/10.1039/b907534h
46. Allard M, Dupont C, Muñoz Robles V, Doucet N, Lledós A, Maréchal J-D, Urvoas A, Mahy
J-P, Ricoux R (2012) Incorporation of manganese complexes into xylanase: new artificial
metalloenzymes for enantioselective epoxidation. ChemBioChem 13:240–251. https://doi.
org/10.1002/cbic.201100659
Current Applications of Artificial Metalloenzymes …
403
simple yet very efficient biomimetic oxidation systems. J Am Chem Soc 127:2883–2887.
https://doi.org/10.1021/ja045372c
32. Herrero C, Quaranta A, Ricoux R, Trehoux A, Mahammed A, Gross Z, Banse F, Mahy J-P
(2016) Oxidation catalysis via visible-light water activation of a [Ru(bpy) 3 ]
2+ chromophore
BSA–metallocorrole couple. Dalton Trans 45:706–710. https://doi.org/10.1039/C5DT04158A
33. Rousselot-Pailley P, Bochot C, Marchi-Delapierre C, Jorge-Robin A, Martin L,
Fontecilla-Camps JC, Cavazza C, Ménage S (2009) The protein environment drives
selectivity for sulfide oxidation by an artificial metalloenzyme. ChemBioChem 10:545–552.
https://doi.org/10.1002/cbic.200800595
34. Tang J, Huang F, Wei Y, Bian H, Zhang W, Liang H (2016) Bovine serum albumin–cobalt
(II) Schiff base complex hybrid: an efficient artificial metalloenzyme for enantioselective
sulfoxidation using hydrogen peroxide. Dalton Trans 45:8061–8072. https://doi.org/10.
1039/C5DT04507J
35. Hunter CL, Lloyd E, Eltis LD, Rafferty SP, Lee H, Smith M, Mauk AG (1997) Role of the
heme propionates in the interaction of heme with apomyoglobin and apocytochrome b 5 .
Biochemistry 36:1010–1017. https://doi.org/10.1021/bi961385u
36. Hayashi T, Hisaeda Y (2002) New functionalization of myoglobin by chemical modification
of heme-propionates. Acc Chem Res 35:35–43. https://doi.org/10.1021/ar000087t
37. Ueno T, Koshiyama T, Abe S, Yokoi N, Ohashi M, Nakajima H, Watanabe Y (2007) Design
of artificial metalloenzymes using non-covalent insertion of a metal complex into a protein
scaffold. J Organomet Chem 692:142–147. https://doi.org/10.1016/j.jorganchem.2006.08.
043
38. Ueno T, Koshiyama T, Ohashi M, Kondo K, Kono M, Suzuki A, Yamane T, Watanabe Y
(2005) Coordinated design of cofactor and active site structures in development of new
protein catalysts. J Am Chem Soc 127:6556–6562. https://doi.org/10.1021/ja045995q
39. Ohashi M, Koshiyama T, Ueno T, Yanase M, Fujii H, Watanabe Y (2003) Preparation of
artificial metalloenzymes by insertion of chromium(III) Schiff base complexes into
apomyoglobin Mutants. Angew Chem Int Ed 42:1005–1008. https://doi.org/10.1002/anie.
200390256
40. Carey JR, Ma SK, Pfister TD, Garner DK, Kim HK, Abramite JA, Wang Z, Guo Z, Lu Y
(2004) A site-selective dual anchoring strategy for artificial metalloprotein design. J Am
Chem Soc 126:10812–10813. https://doi.org/10.1021/ja046908x
41. Zhang J-L, Garner DK, Liang L, Chen Q, Lu Y (2008) Protein scaffold of a designed
metalloenzyme enhances the chemoselectivity in sulfoxidation of thioanisole. Chem
Commun 1665. https://doi.org/10.1039/b718915j
42. Hayashi T, Murata D, Makino M, Sugimoto H, Matsuo T, Sato H, Shiro Y, Hisaeda Y
(2006) Crystal structure and peroxidase activity of myoglobin reconstituted with iron
porphycene. Inorg Chem 45:10530–10536. https://doi.org/10.1021/ic061130x
43. Ducros V, Charnock SJ, Derewenda U, Derewenda ZS, Dauter Z, Dupont C, Shareck F,
Morosoli R, Kluepfel D, Davies GJ (2000) Substrate specificity in glycoside hydrolase
family 10: structural and kinetic analysis of the Streptomyces Lividans Xylanase 10A. J Biol
Chem 275:23020–23026. https://doi.org/10.1074/jbc.275.30.23020
44. Komatsu T, Ishihara S, Tsuchida E, Nishide H, Morokuma C, Nakamura S (2005)
Heat-resistant oxygen-carrying hemoproteins consist of recombinant xylanases and synthetic
iron(II) porphyrin. Biomacromol 6:1489–1494. https://doi.org/10.1021/bm049255l
45. Ricoux R, Allard M, Dubuc R, Dupont C, Maréchal J-D, Mahy J-P (2009) Selective
oxidation of aromatic sulfide catalyzed by an artificial metalloenzyme: new activity of
hemozymes. Org Biomol Chem 7:3208–3211. https://doi.org/10.1039/b907534h
46. Allard M, Dupont C, Muñoz Robles V, Doucet N, Lledós A, Maréchal J-D, Urvoas A, Mahy
J-P, Ricoux R (2012) Incorporation of manganese complexes into xylanase: new artificial
metalloenzymes for enantioselective epoxidation. ChemBioChem 13:240–251. https://doi.
org/10.1002/cbic.201100659
Current Applications of Artificial Metalloenzymes …
403