47. Cherrier MV, Cavazza C, Bochot C, Lemaire D, Fontecilla-Camps JC (2008) Structural
characterization of a putative endogenous metal chelator in the periplasmic nickel transporter
NikA. Biochemistry 47:9937–9943. https://doi.org/10.1021/bi801051y
48. Cherrier MV, Martin L, Cavazza C, Jacquamet L, Lemaire D, Gaillard J, Fontecilla-Camps
JC (2005) Crystallographic and spectroscopic evidence for high affinity binding of FeEDTA
(H 2 O)
- to the periplasmic nickel transporter NikA. J Am Chem Soc 127:10075–10082.
https://doi.org/10.1021/ja0518530
49. Esmieu C, Cherrier MV, Amara P, Girgenti E, Marchi-Delapierre C, Oddon F, Iannello M,
Jorge-Robin A, Cavazza C, Ménage S (2013) An artificial oxygenase built from scratch:
substrate binding site identified using a docking approach. Angew Chem Int Ed 52:3922–
3925. https://doi.org/10.1002/anie.201209021
50. Buron C, Sénéchal-David K, Ricoux R, Le Caër J-P, Guérineau V, Méjanelle P, Guillot R,
Herrero C, Mahy J-P, Banse F (2015) An artificial enzyme made by covalent grafting of an
Fe
II complex into b-lactoglobulin: molecular chemistry, oxidation catalysis, and
reaction-intermediate monitoring in a protein. Chem Eur J 21:12188–12193. https://doi.
org/10.1002/chem.201501755
51. Fujieda N, Hasegawa A, Ishihama K, Itoh S (2012) Artificial dicopper oxidase: rational
reprogramming of bacterial metallo-b-lactamase into a catechol oxidase. Chem Asian J
7:1203–1207. https://doi.org/10.1002/asia.201101014
52. Ricoux R, Girgenti E, Sauriat-Dorizon H, Blanchard D, Mahy J-P (2002) Regioselective
nitration of phenol induced by catalytic antibodies. J Protein Chem 21:473–477. https://doi.
org/10.1023/A:1021351120772
53. Håkansson K, Wehnert A, Liljas A (1994) X-ray analysis of metal-substituted human
carbonic anhydrase II derivatives. Acta Crystallogr D Biol Crystallogr 50:93–100. https://
doi.org/10.1107/S0907444993008790
54. Okrasa K, Kazlauskas RJ (2006) Manganese-substituted carbonic anhydrase as a new
peroxidase. Chem Eur J 12:1587–1596. https://doi.org/10.1002/chem.200501413
55. Fernández-Gacio A, Codina A, Fastrez J, Riant O, Soumillion P (2006) Transforming
carbonic anhydrase into epoxide synthase by metal exchange. Chem Bio Chem 7:1013–
1016. https://doi.org/10.1002/cbic.200600127
56. Reetz MT (2002) Directed evolution of selective enzymes and hybrid catalysts. Tetrahedron
58:6595–6602. https://doi.org/10.1016/S0040-4020(02)00668-3
57. Reetz MT, Rentzsch M, Pletsch A, Maywald M, Maiwald P, Peyralans JJ-P, Maichele A,
Fu Y, Jiao N, Hollmann F, Mondière R, Taglieber A (2007) Directed evolution of
enantioselective hybrid catalysts: a novel concept in asymmetric catalysis. Tetrahedron
63:6404–6414. https://doi.org/10.1016/j.tet.2007.03.177
58. Kolb HC, VanNieuwenhze MS, Sharpless KB (1994) Catalytic asymmetric dihydroxylation.
Chem Rev 94:2483–2547. https://doi.org/10.1021/cr00032a009
59. Abu-Omar MM, Loaiza A, Hontzeas N (2005) Reaction mechanisms of mononuclear
non-heme iron oxygenases. Chem Rev 105:2227–2252. https://doi.org/10.1021/cr040653o
60. Kokubo T, Sugimoto T, Uchida T, Tanimoto S, Okano M (1983) The bovine serum
albumin–2-phenylpropane-1,2-diolatodioxo-osmium(VI) complex as an enantioselective
catalyst for cis-hydroxylation of alkenes. J Chem Soc Chem Commun 769–770. https://doi.
org/10.1039/C39830000769
61. Köhler V, Mao J, Heinisch T, Pordea A, Sardo A, Wilson YM, Knörr L, Creus M, Prost J-C,
Schirmer T, Ward TR (2011) OsO4ÁStreptavidin: a tunable hybrid catalyst for the
enantioselective cis-dihydroxylation of olefins. Angew Chem Int Ed 50:10863–10866.
https://doi.org/10.1002/anie.201103632
62. Cavazza C, Bochot C, Rousselot-Pailley P, Carpentier P, Cherrier MV, Martin L,
Marchi-Delapierre C, Fontecilla-Camps JC, Ménage S (2010) Crystallographic snapshots of
the reaction of aromatic C–H with O 2 catalysed by a protein-bound iron complex. Nat Chem
2:1069–1076. https://doi.org/10.1038/nchem.841
404
J.-P. Mahy et al.
characterization of a putative endogenous metal chelator in the periplasmic nickel transporter
NikA. Biochemistry 47:9937–9943. https://doi.org/10.1021/bi801051y
48. Cherrier MV, Martin L, Cavazza C, Jacquamet L, Lemaire D, Gaillard J, Fontecilla-Camps
JC (2005) Crystallographic and spectroscopic evidence for high affinity binding of FeEDTA
(H 2 O)
- to the periplasmic nickel transporter NikA. J Am Chem Soc 127:10075–10082.
https://doi.org/10.1021/ja0518530
49. Esmieu C, Cherrier MV, Amara P, Girgenti E, Marchi-Delapierre C, Oddon F, Iannello M,
Jorge-Robin A, Cavazza C, Ménage S (2013) An artificial oxygenase built from scratch:
substrate binding site identified using a docking approach. Angew Chem Int Ed 52:3922–
3925. https://doi.org/10.1002/anie.201209021
50. Buron C, Sénéchal-David K, Ricoux R, Le Caër J-P, Guérineau V, Méjanelle P, Guillot R,
Herrero C, Mahy J-P, Banse F (2015) An artificial enzyme made by covalent grafting of an
Fe
II complex into b-lactoglobulin: molecular chemistry, oxidation catalysis, and
reaction-intermediate monitoring in a protein. Chem Eur J 21:12188–12193. https://doi.
org/10.1002/chem.201501755
51. Fujieda N, Hasegawa A, Ishihama K, Itoh S (2012) Artificial dicopper oxidase: rational
reprogramming of bacterial metallo-b-lactamase into a catechol oxidase. Chem Asian J
7:1203–1207. https://doi.org/10.1002/asia.201101014
52. Ricoux R, Girgenti E, Sauriat-Dorizon H, Blanchard D, Mahy J-P (2002) Regioselective
nitration of phenol induced by catalytic antibodies. J Protein Chem 21:473–477. https://doi.
org/10.1023/A:1021351120772
53. Håkansson K, Wehnert A, Liljas A (1994) X-ray analysis of metal-substituted human
carbonic anhydrase II derivatives. Acta Crystallogr D Biol Crystallogr 50:93–100. https://
doi.org/10.1107/S0907444993008790
54. Okrasa K, Kazlauskas RJ (2006) Manganese-substituted carbonic anhydrase as a new
peroxidase. Chem Eur J 12:1587–1596. https://doi.org/10.1002/chem.200501413
55. Fernández-Gacio A, Codina A, Fastrez J, Riant O, Soumillion P (2006) Transforming
carbonic anhydrase into epoxide synthase by metal exchange. Chem Bio Chem 7:1013–
1016. https://doi.org/10.1002/cbic.200600127
56. Reetz MT (2002) Directed evolution of selective enzymes and hybrid catalysts. Tetrahedron
58:6595–6602. https://doi.org/10.1016/S0040-4020(02)00668-3
57. Reetz MT, Rentzsch M, Pletsch A, Maywald M, Maiwald P, Peyralans JJ-P, Maichele A,
Fu Y, Jiao N, Hollmann F, Mondière R, Taglieber A (2007) Directed evolution of
enantioselective hybrid catalysts: a novel concept in asymmetric catalysis. Tetrahedron
63:6404–6414. https://doi.org/10.1016/j.tet.2007.03.177
58. Kolb HC, VanNieuwenhze MS, Sharpless KB (1994) Catalytic asymmetric dihydroxylation.
Chem Rev 94:2483–2547. https://doi.org/10.1021/cr00032a009
59. Abu-Omar MM, Loaiza A, Hontzeas N (2005) Reaction mechanisms of mononuclear
non-heme iron oxygenases. Chem Rev 105:2227–2252. https://doi.org/10.1021/cr040653o
60. Kokubo T, Sugimoto T, Uchida T, Tanimoto S, Okano M (1983) The bovine serum
albumin–2-phenylpropane-1,2-diolatodioxo-osmium(VI) complex as an enantioselective
catalyst for cis-hydroxylation of alkenes. J Chem Soc Chem Commun 769–770. https://doi.
org/10.1039/C39830000769
61. Köhler V, Mao J, Heinisch T, Pordea A, Sardo A, Wilson YM, Knörr L, Creus M, Prost J-C,
Schirmer T, Ward TR (2011) OsO4ÁStreptavidin: a tunable hybrid catalyst for the
enantioselective cis-dihydroxylation of olefins. Angew Chem Int Ed 50:10863–10866.
https://doi.org/10.1002/anie.201103632
62. Cavazza C, Bochot C, Rousselot-Pailley P, Carpentier P, Cherrier MV, Martin L,
Marchi-Delapierre C, Fontecilla-Camps JC, Ménage S (2010) Crystallographic snapshots of
the reaction of aromatic C–H with O 2 catalysed by a protein-bound iron complex. Nat Chem
2:1069–1076. https://doi.org/10.1038/nchem.841
404
J.-P. Mahy et al.