13. Mahy J-P, Ricoux R (2016) Design, synthesis and reactivity for a new kind of
eco-compatible hybrid biocatalyst : artificial hemoproteins. Handb Porphyr Sci Appl Chem
Phys Mater Sci Eng Biol Med, 38 Green Chem
14. Kaplan J, DeGrado WF (2004) De novo design of catalytic proteins. Proc Natl Acad Sci
101:11566–11570. https://doi.org/10.1073/pnas.0404387101
15. Summa CM, Rosenblatt MM, Hong J-K, Lear JD, DeGrado WF (2002) Computational de
novo design, and characterization of an A2B2 Diiron protein. J Mol Biol 321:923–938.
https://doi.org/10.1016/S0022-2836(02)00589-2
16. Faiella M, Andreozzi C, de Rosales RTM, Pavone V, Maglio O, Nastri F, DeGrado WF,
Lombardi A (2009) An artificial di-iron oxo-protein with phenol oxidase activity. Nat Chem
Biol 5:882–884. https://doi.org/10.1038/nchembio.257
17. Reig AJ, Pires MM, Snyder RA, Wu Y, Jo H, Kulp DW, Butch SE, Calhoun JR,
Szyperski T, Solomon EI, DeGrado WF (2012) Alteration of the oxygen-dependent
reactivity of de novo Due Ferri proteins. Nat Chem 4:900–906. https://doi.org/10.1038/
nchem.1454
18. Snyder RA, Butch AJ, Reig AJ, DeGrado WF, Solomon EI (2012) Molecular-level insight
into the differential oxidase and oxygenase reactivities of De Novo Due Ferri proteins. J Am
Chem Soc 137:9302–9314. https://doi.org/10.1021/jacs.5b03524
19. Thomas CM, Letondor C, Humbert N, Ward TR (2005) Aqueous oxidation of alcohols
catalyzed by artificial metalloenzymes based on the biotin–avidin technology. J Organomet
Chem 690:4488–4491. https://doi.org/10.1016/j.jorganchem.2005.02.001
20. Choi YS, Zhang H, Brunzelle JS, Nair SK, Zhao H (2008) In vitro reconstitution and crystal
structure of p-aminobenzoate N-oxygenase (AurF) involved in aureothin biosynthesis. Proc
Natl Acad Sci 105:6858–6863. https://doi.org/10.1073/pnas.0712073105
21. van de Velde F, Arends IWCE, Sheldon RA (2000) Vanadium-catalysed enantioselective
sulfoxidations: rational design of biocatalytic and biomimetic systems. Top Catal 13:259–
265. https://doi.org/10.1023/A:1009094619249
22. van de Velde F, Arends IWCE, Sheldon RA (2000) Biocatalytic and biomimetic oxidations
with vanadium. J Inorg Biochem 80:81–89. https://doi.org/10.1016/S0162-0134(00)00043-X
23. van de Velde F, Könemann L (1998) Enantioselective sulfoxidation mediated by
vanadium-incorporated phytase: a hydrolase acting as a peroxidase. Chem Commun
1891–1892. https://doi.org/10.1039/a804702b
24. Pordea A, Creus M, Panek J, Duboc C, Mathis D, Novic M, Ward TR (2008) Artificial
metalloenzyme for enantioselective sulfoxidation based on vanadyl-loaded streptavidin.
J Am Chem Soc 130:8085–8088. https://doi.org/10.1021/ja8017219
25. Pordea A, Mathis D, Ward TR (2009) Incorporation of biotinylated manganese-salen
complexes into streptavidin: new artificial metalloenzymes for enantioselective sulfoxidation. J Organomet Chem 694:930–936. https://doi.org/10.1016/j.jorganchem.2008.11.023
26. Sansiaume-Dagousset E, Urvoas A, Chelly K, Ghattas W, Maréchal J-D, Mahy J-P,
Ricoux R (2014) Neocarzinostatin-based hybrid biocatalysts for oxidation reactions. Dalton
Trans 43:8344–8354. https://doi.org/10.1039/c4dt00151f
27. Nakagawa A, Komatsu T, Iizuka M, Tsuchida E (2008) O 2 binding to human serum
albumin incorporating iron porphyrin with a covalently linked methyl- L -histidine isomer.
Bioconjug Chem 19:581–584. https://doi.org/10.1021/bc700400n
28. Komatsu T, Nakagawa A, Qu X (2009) Structural and mutagenic approach to create human
serum albumin-based oxygen carrier and photosensitizer. Drug Metab Pharmacokinet
24:287–299. https://doi.org/10.2133/dmpk.24.287
29. Zunszain PA, Ghuman J, Komatsu T, Tsuchida E, Curry S (2003) Crystal structural analysis
of human serum albumin complexed with hemin and fatty acid. BMC Struct Biol 3:6. https://
doi.org/10.1186/1472-6807-3-6
30. Mahammed A, Gray HB, Weaver JJ, Sorasaenee K, Gross Z (2004) Amphiphilic corroles
bind tightly to human serum albumin. Bioconjug Chem 15:738–746. https://doi.org/10.1021/
bc034179p
402
J.-P. Mahy et al.
eco-compatible hybrid biocatalyst : artificial hemoproteins. Handb Porphyr Sci Appl Chem
Phys Mater Sci Eng Biol Med, 38 Green Chem
14. Kaplan J, DeGrado WF (2004) De novo design of catalytic proteins. Proc Natl Acad Sci
101:11566–11570. https://doi.org/10.1073/pnas.0404387101
15. Summa CM, Rosenblatt MM, Hong J-K, Lear JD, DeGrado WF (2002) Computational de
novo design, and characterization of an A2B2 Diiron protein. J Mol Biol 321:923–938.
https://doi.org/10.1016/S0022-2836(02)00589-2
16. Faiella M, Andreozzi C, de Rosales RTM, Pavone V, Maglio O, Nastri F, DeGrado WF,
Lombardi A (2009) An artificial di-iron oxo-protein with phenol oxidase activity. Nat Chem
Biol 5:882–884. https://doi.org/10.1038/nchembio.257
17. Reig AJ, Pires MM, Snyder RA, Wu Y, Jo H, Kulp DW, Butch SE, Calhoun JR,
Szyperski T, Solomon EI, DeGrado WF (2012) Alteration of the oxygen-dependent
reactivity of de novo Due Ferri proteins. Nat Chem 4:900–906. https://doi.org/10.1038/
nchem.1454
18. Snyder RA, Butch AJ, Reig AJ, DeGrado WF, Solomon EI (2012) Molecular-level insight
into the differential oxidase and oxygenase reactivities of De Novo Due Ferri proteins. J Am
Chem Soc 137:9302–9314. https://doi.org/10.1021/jacs.5b03524
19. Thomas CM, Letondor C, Humbert N, Ward TR (2005) Aqueous oxidation of alcohols
catalyzed by artificial metalloenzymes based on the biotin–avidin technology. J Organomet
Chem 690:4488–4491. https://doi.org/10.1016/j.jorganchem.2005.02.001
20. Choi YS, Zhang H, Brunzelle JS, Nair SK, Zhao H (2008) In vitro reconstitution and crystal
structure of p-aminobenzoate N-oxygenase (AurF) involved in aureothin biosynthesis. Proc
Natl Acad Sci 105:6858–6863. https://doi.org/10.1073/pnas.0712073105
21. van de Velde F, Arends IWCE, Sheldon RA (2000) Vanadium-catalysed enantioselective
sulfoxidations: rational design of biocatalytic and biomimetic systems. Top Catal 13:259–
265. https://doi.org/10.1023/A:1009094619249
22. van de Velde F, Arends IWCE, Sheldon RA (2000) Biocatalytic and biomimetic oxidations
with vanadium. J Inorg Biochem 80:81–89. https://doi.org/10.1016/S0162-0134(00)00043-X
23. van de Velde F, Könemann L (1998) Enantioselective sulfoxidation mediated by
vanadium-incorporated phytase: a hydrolase acting as a peroxidase. Chem Commun
1891–1892. https://doi.org/10.1039/a804702b
24. Pordea A, Creus M, Panek J, Duboc C, Mathis D, Novic M, Ward TR (2008) Artificial
metalloenzyme for enantioselective sulfoxidation based on vanadyl-loaded streptavidin.
J Am Chem Soc 130:8085–8088. https://doi.org/10.1021/ja8017219
25. Pordea A, Mathis D, Ward TR (2009) Incorporation of biotinylated manganese-salen
complexes into streptavidin: new artificial metalloenzymes for enantioselective sulfoxidation. J Organomet Chem 694:930–936. https://doi.org/10.1016/j.jorganchem.2008.11.023
26. Sansiaume-Dagousset E, Urvoas A, Chelly K, Ghattas W, Maréchal J-D, Mahy J-P,
Ricoux R (2014) Neocarzinostatin-based hybrid biocatalysts for oxidation reactions. Dalton
Trans 43:8344–8354. https://doi.org/10.1039/c4dt00151f
27. Nakagawa A, Komatsu T, Iizuka M, Tsuchida E (2008) O 2 binding to human serum
albumin incorporating iron porphyrin with a covalently linked methyl- L -histidine isomer.
Bioconjug Chem 19:581–584. https://doi.org/10.1021/bc700400n
28. Komatsu T, Nakagawa A, Qu X (2009) Structural and mutagenic approach to create human
serum albumin-based oxygen carrier and photosensitizer. Drug Metab Pharmacokinet
24:287–299. https://doi.org/10.2133/dmpk.24.287
29. Zunszain PA, Ghuman J, Komatsu T, Tsuchida E, Curry S (2003) Crystal structural analysis
of human serum albumin complexed with hemin and fatty acid. BMC Struct Biol 3:6. https://
doi.org/10.1186/1472-6807-3-6
30. Mahammed A, Gray HB, Weaver JJ, Sorasaenee K, Gross Z (2004) Amphiphilic corroles
bind tightly to human serum albumin. Bioconjug Chem 15:738–746. https://doi.org/10.1021/
bc034179p
402
J.-P. Mahy et al.