Artificial Metalloenzymes with the Neocarzinostatin Scaffold: Toward a Biocatalyst for the Diels-Alder Reaction

ChemBioChem

Volumn 17, Issue 5, 2016, Pages 433-440

  Ghattas, Wadih ^a   Cotchico Alonso, Lur ^c   Maréchal, Jean Didier ^c   Urvoas, Agathe ^b   Rousseau, Maëva ^a   Mahy, Jean Pierre ^a   Ricoux, Rémy ^a  

^a UNIVERSITÉ PARIS SUD   (France)

^b INSTITUTE FOR INTEGRATIVE BIOLOGY OF THE CELL I2BC   (France)

^c UNIVERSITAT AUTÒNOMA DE BARCELONA   (Spain)

Author keywords

artificial metalloenzymes; biocatalysis; copper complexes; diels alder cyclization reaction; molecular modeling

Indexed keywords

ARTIFICIAL METALLOENZYME; COPPER COMPLEX; ENZYME; TESTOSTERONE; UNCLASSIFIED DRUG; ZINOSTATIN; METALLOPROTEIN;

AFFINITY CHROMATOGRAPHY; ARTICLE; BINDING AFFINITY; BINDING SITE; BIOCATALYST; CROSS COUPLING REACTION; CRYSTAL STRUCTURE; CYCLIZATION; DIELS ALDER REACTION; ELECTROPHILICITY; ENZYME LINKED IMMUNOSORBENT ASSAY; ENZYME SYNTHESIS; ESCHERICHIA COLI; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROPHOBICITY; LIGAND BINDING; MOLECULAR MODEL; NICKEL AFFINITY CHROMATOGRAPHY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DENATURATION; QUANTUM MECHANICS; SIZE EXCLUSION CHROMATOGRAPHY; STOICHIOMETRY; BIOCATALYSIS; CARBON NUCLEAR MAGNETIC RESONANCE; CYCLOADDITION; ELECTROSPRAY MASS SPECTROMETRY; METABOLISM; MOLECULAR DOCKING; PROTON NUCLEAR MAGNETIC RESONANCE;

BIOCATALYSIS; CARBON-13 MAGNETIC RESONANCE SPECTROSCOPY; CYCLOADDITION REACTION; ENZYMES; METALLOPROTEINS; MOLECULAR DOCKING SIMULATION; PROTON MAGNETIC RESONANCE SPECTROSCOPY; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; ZINOSTATIN;

EID: 84959465215     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.201500445     Document Type: Article

References (60)

1. M. Breuer, K. Ditrich, T. Habicher, B. Hauer, M. Keßeler, R. Stürmer, T. Zelinski, Angew. Chem. Int. Ed. 2004, 43, 788-824;
2. Angew. Chem. 2004, 116, 806-843.
3. J.-P. Mahy, J.-D. Maréchal, R. Ricoux, Chem. Commun. 2015, 51, 2476-2494;
4. T. R. Ward, Acc. Chem. Res. 2011, 44, 47-57;
5. M. Dürrenberger, T. R. Ward, Curr. Opin. Chem. Biol. 2014, 19, 99-106;
6. J. Bos, G. Roelfes, Curr. Opin. Chem. Biol. 2014, 19, 135-143;
7. T. Matsuo, S. Hirota, Bioorg. Med. Chem. 2014, 22, 5638-5656;
8. M. V. Doble, A. C. C. Ward, P. J. Deuss, A. G. Jarvis, P. C. J. Kamer, Bioorg. Med. Chem. 2014, 22, 5657-5677;
9. F. Yu, V. M. Cangelosi, M. L. Zastrow, M. Tegoni, J. S. Plegaria, A. G. Tebo, C. S. Mocny, L. Ruckthong, H. Qayyum, V. L. Pecoraro, Chem. Rev. 2014, 114, 3495-3578;
10. J. C. Lewis, ACS Catal. 2013, 3, 2954-2975.
11. A. L. Pinto, H. W. Hellinga, J. P. Caradonna, Proc. Natl. Acad. Sci. USA 1997, 94, 5562-5567;
12. S.-i. Ozaki, H.-J. Yang, T. Matsui, Y. Goto, Y. Watanabe, Tetrahedron: Asymmetry 1999, 10, 183-192;
13. I. Hara, T. Ueno, S.-i. Ozaki, S. Itoh, K. Lee, N. Ueyamaand, Y. Watanabe, J. Biol. Chem. 2001, 276, 36067-36070;
14. S. Kato, H.-J. Yang, T. Ueno, S.-i. Ozaki, G. N. Phillips, Jr., S. Fukuzumi, Y. Watanabe, J. Am. Chem. Soc. 2002, 124, 8506-8507.
15. H. L. Levine, Y. Nakagawa, E. T. Kaiser, Biochem. Biophys. Res. Commun. 1977, 76, 64-70;
16. E. Monzani, G. Alzuet, L. Casella, C. Redaelli, C. Bassani, A. M. Sanangelantoni, M. Gullotti, L. De Gioia, L. Santagostin, F. Chillemi, Biochemistry 2000, 39, 9571-9582;
17. R. R. Davies, M. D. Distefano, J. Am. Chem. Soc. 1997, 119, 11643-11652;
18. S. K. Ma, Y. Lu, J. Inorg. Biochem. 1999, 74, 217-243;
19. M. R. Ermácora, J. M. Delfino, B. Cuenoud, A. Schepartz, R. O. Fox, Proc. Natl. Acad. Sci. USA 1992, 89, 6383-6387;
20. D. S. Sigman, T. W. Bruice, A. Mazumder, C. L. Sutton, Acc. Chem. Res. 1993, 26, 98-104.
21. R. Ricoux, M. Allard, R. Dubuc, C. Dupont, J.-D. Maréchal, J.-P. Mahy, Org. Biomol. Chem. 2009, 7, 3208-3211.
22. M. Allard, C. Dupont, V. Munoz Robles, N. Doucet, A. Lledós, J.-D. Maréchal, A. Urvoas, J.-P. Mahy, R. Ricoux, ChemBioChem 2012, 13, 240-251.
23. M. E. Wilson, G. M. Whitesides, J. Am. Chem. Soc. 1978, 100, 306-307.
24. T. R. Ward, Acc. Chem. Res. 2011, 44, 47-57.
25. J. Collot, J. Gradinaru, N. Humbert, M. Skander, A. Zocchi, T. R. Ward, J. Am. Chem. Soc. 2003, 125, 9030-9031.
26. Q. Raffy, R. Ricoux, J.-P. Mahy, Tetrahedron Lett. 2008, 49, 1865-1869;
27. Q. Raffy, R. Ricoux, E. Sansiaume, S. Pethe, J.-P. Mahy, J. Mol. Catal. A 2010, 317, 19-26;
28. E. Sansiaume, R. Ricoux, D. Gori, J.-P. Mahy, Tetrahedron: Asymmetry 2010, 21, 1593-1600.
29. G. Albers-Schönberg, R. S. Dewey, O. D. Hensens, J. M. Liesch, M. A. Napier, I. H. Goldberg, Biochem. Biophys. Res. Commun. 1980, 95, 1351-1356;
30. J. Meienhofer, H. Maeda, C. B. Glaser, J. Czombos, K. Kuromizu, Science 1972, 178, 875-876;
31. N. Ishida, K. Miyazaki, K. Kumagai, M. Rikimaru, Jpn. J. Antibiot. 1965, 18, 68-76.
32. A. Drevelle, M. Graille, B. Heyd, I. Sorel, N. Ulryck, F. Pecorari, M. Desmadril, H. van Tilbeurgh, P. Minard, J. Mol. Biol. 2006, 358, 455-471.
33. E. Sansiaume-Dagousset, A. Urvoas, K. Chelly, W. Ghattas, J.-D. Maréchal, J.-P. Mahy, R. Ricoux, Dalton Trans. 2014, 43, 8344-8354.
34. A. Urvoas, W. Ghattas, J.-D. Maréchal, F. Avenier, F. Bellande, W. Mao, R. Ricoux, J.-P. Mahy, Bioorg. Med. Chem. 2014, 22, 5678-5686.
35. E. M. Stocking, R. M. Williams, Angew. Chem. Int. Ed. 2003, 42, 3078-3115;
36. Angew. Chem. 2003, 115, 3186-3223.
37. A. Draksharapu, A. J. Boersma, W. R. Browne, G. Roelfes, Dalton Trans. 2015, 44, 3656-3663.
38. A. Drevelle, A. Urvoas, M. Ben Hamida-Rebaï, G. Van Vooren, M. Nicaise, M. Valerio-Lepiniec, M. Desmadril, C. H. Robert, P. Minard, ChemBioChem 2009, 10, 1349-1359.
39. B. Heyd, F. Pecorari, B. Collinet, E. Adjadj, M. Desmadril, P. Minard, Biochemistry 2003, 42, 5674-5683.
40. S. Reymond, J. Cossy, Chem. Rev. 2008, 108, 5359-5406;
41. E. B. Mubofu, J. B. F. N. Engberts, J. Phys. Org. Chem. 2004, 17, 180-186;
42. H. Bauke Albada, F. Rosati, D. Coquière, G. Roelfes, R. M. J. Liskamp, Eur. J. Org. Chem. 2011, 1714-1720.
43. N. K. Sangwan, H.-J. Schneider, J. Chem. Soc. Perkin Trans. 2 1989, 1223-1227;
44. S. P. Kim, A. G. Leach, K. N. Houk, J. Org. Chem. 2002, 67, 4250-4260;
45. B. Talbi, P. Haquette, A. Martel, F. de Montigny, C. Fosse, S. Cordier, T. Roisnel, G. Jaouena, M. Salmain, Dalton Trans. 2010, 39, 5605-5607.
46. J. B. Siegel, A. Zanghellini, H. M. Lovick, G. Kiss, A. R. Lambert, J. L. St Clair, J. L. Gallaher, D. Hilvert, M. H. Gelb, B. L. Stoddard, K. N. Houk, F. E. Michael, D. Baker, Science 2010, 329, 309-313;
47. N. Preiswerk, T. Beck, J. D. Schulz, P. Milovnik, C. Mayer, D. Hilvert, J. B. Siegel, D. Baker, D. Hilver, Proc. Natl. Acad. Sci. USA 2014, 111, 8013-8018;
48. C. B. Eiben, J. B. Siegel, J. B. Bale, S. Cooper, F. Khatib, B. W. Shen, F. Players, B. L. Stoddard, Z. Popovic, D. Baker, Nat. Biotechnol. 2012, 30, 190-192.
49. A. Guellouz, M. Valerio-Lepiniec, A. Urvoas, A. Chevrel, M. Graille, Z. Fourati-Kammoun, M. Desmadril, H. van Tilbeurgh, P. Minard, PLoS One 2013, 8, e71512.
50. M. L. Verdonk, J. C. Cole, M. J. Hartshorn, C. W. Murray, R. D. Taylor, Proteins Struct. Funct. Bioinf. 2003, 52, 609-623.
51. V. Muñoz Robles, P. Vidossich, A. Lledós, T. R. Ward, J.-D. Maréchal, ACS Catal. 2014, 4, 833-842;
52. V. Muñoz Robles, M. Dürrenberger, T. Heinisch, A. Lledós, T. Schirmer, T. R. Ward, J.-D. Maréchal, J. Am. Chem. Soc. 2014, 136, 15676-15683.
53. R. S. Dickson, B. J. Dobney, F. W. Eastwood, Chem. Educ. 1987, 64, 898.
54. V. V. Zakharychev, A. V. Kuzenkov, Chem. Heterocycl. Compd. 2007, 43, 989-995.
55. M. Hissler, W. B. Connick, D. K. Geiger, J. E. McGarrah, D. Lipa, R. J. Lachicotte, R. Eisenberg, Inorg. Chem. 2000, 39, 447-457.
56. C. Lee, W. Yang, R. G. Parr, Phys. Rev. B 1988, 37, 785-789;
57. A. D. Becke, J. Chem. Phys. 1993, 98, 5648.
58. V. A. Rassolov, M. A. Ratner, J. A. Pople, P. C. Redfern, L. A. Curtiss, J. Comput. Chem. 2001, 22, 976-984.
59. H. Stoll, P. Fuentealba, P. Schwerdtfeger, J. Flad, L. v. Szentpály, H. Preuss, J. Chem. Phys. 1984, 81, 2732-2736.
60. E. F. Pettersen, T. D. Goddard, C. C. Huang, G. S. Couch, D. M. Greenblatt, E. C. Meng, T. E. Ferrin, J. Comput. Chem. 2004, 25, 1605-1612.