De novo metallonucleases based on helix-loop-helix motifs

Chemistry - A European Journal

Volumn 10, Issue 17, 2004, Pages 4163-4170

  Rossi, Paola ^a   Tecilla, Paolo ^c   Baltzer, Lars ^b   Scrimin, Paolo ^a  

^a UNIVERSITY OF PADOVA   (Italy)

^b LINKÖPING UNIVERSITY   (Sweden)

^c UNIVERSITY OF TRIESTE   (Italy)

Author keywords

Enzyme models; Kinetics; Peptides; Phosphate cleavage; Zinc

Indexed keywords

AMINES; CATALYST ACTIVITY; COMPLEXATION; DIMERIZATION; ESTERIFICATION; PHOSPHATES; RNA;

CIRCULAR DICHROISM (CD); METALLONUCLEASES; TRIAZACYCLONONANE METAL-ION BINDING SITE (ATANP);

AMINO ACIDS;

2 HYDROXYPROPYL 4 NITROPHENYLPHOSPHATE; AMINE; AMINO ACID; COORDINATION COMPOUND; HELIX LOOP HELIX PROTEIN; HETEROCYCLIC COMPOUND; METAL ION; METALLONUCLEASE; NUCLEASE; PEPTIDE DERIVATIVE; PHOSPHATE; RNA; TRIAZACYCLONONANE; UNCLASSIFIED DRUG; ZINC ION;

AMINO ACID SEQUENCE; ARTICLE; BINDING KINETICS; BINDING SITE; CATALYST; CHEMICAL INTERACTION; CHEMICAL REACTION; CIRCULAR DICHROISM; COMPLEX FORMATION; CONCENTRATION RESPONSE; CONFORMATIONAL TRANSITION; DIMERIZATION; ENZYME SUBSTRATE; METAL BINDING; MICHAELIS MENTEN KINETICS; MOLECULAR MODEL; PEPTIDE SYNTHESIS; PH; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; PROTON TRANSPORT; STRUCTURE ANALYSIS; TRANSESTERIFICATION;

CATALYSIS; CIRCULAR DICHROISM; DEOXYRIBONUCLEASES; DRUG DESIGN; HELIX-LOOP-HELIX MOTIFS; HYDROGEN-ION CONCENTRATION; INDICATORS AND REAGENTS; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; ORGANOPHOSPHORUS COMPOUNDS; PEPTIDES; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; ZINC;

EID: 4644225362     PISSN: 09476539     EISSN: None     Source Type: Journal    
DOI: 10.1002/chem.200400160     Document Type: Article

References (57)

1. N. Voyer, J. Lamothe, Tetrahedron 1995, 51, 9241-9284.
2. S. M. Gellman, Acc. Chem. Res. 1998, 31, 173-180.
3. N. H. William, P. Wyman, Chem. Commun. 2001, 1268-1269.
4. a) D. E. Wilcox, Chem. Rev. 1996, 96, 2435-2458;
5. (b) N. Sträter, W. N. Lipscomb, T. Klabunde, B. Krebs, Angew. Chem. 1996, 108. 2158-2191; Angew. Chem. Int. Ed. Engl. 1996, 35, 2024-2055.
6. (b) N. Sträter, W. N. Lipscomb, T. Klabunde, B. Krebs, Angew. Chem. 1996, 108. 2158-2191; Angew. Chem. Int. Ed. Engl. 1996, 35, 2024-2055.
7. M. D. Sam, J. J. Perona, Biochemistry 1999, 38, 6576-6586.
8. a) N. H. Williams, B. Takasaki, M. Wall, J. Chin, Acc. Chem. Res 1999, 32, 485-493;
9. (b) E. L. Hegg, J. N. Burstyn, Coord. Chem. Rev. 1998, 17, 133-165.
10. a) P. Molenveld, J. F. J. Engbersen, D. N. Reinhoudt, Angew. Chem. 1999, 111, 3387-3340; Angew. Chem. Int. Ed. 1999, 38, 3189-3191;
11. a) P. Molenveld, J. F. J. Engbersen, D. N. Reinhoudt, Angew. Chem. 1999, 111, 3387-3340; Angew. Chem. Int. Ed. 1999, 38, 3189-3191;
12. (b) M. J. Young, J. Chin, J. Am. Chem. Soc. 1995. 117, 10577-10578;
13. (c) K. O. A. Chin, J. R. Morrow, Inorg. Chem. 1994, 33, 5036-5041;
14. (d) S. Liu, Z. Luo, A. D. Hamilton, Angew. Chem. 1997. 109, 2744-2796; Angew. Chem. Int. Ed. Engl. 1997, 36, 2678-2680;
15. (d) S. Liu, Z. Luo, A. D. Hamilton, Angew. Chem. 1997. 109, 2744-2796; Angew. Chem. Int. Ed. Engl. 1997, 36, 2678-2680;
16. (e) M. Irisawa, N. Takeda, M. Komijama, J. Chem. Soc. Chem. Commun. 1995, 1221-1222;
17. (f) B. Linkletter, J. Chin. Angew. Chem. 1995, 107, 529; Angew. Chem. Int. Ed. Engl. 1995, 34, 472-474;
18. (f) B. Linkletter, J. Chin. Angew. Chem. 1995, 107, 529; Angew. Chem. Int. Ed. Engl. 1995, 34, 472-474;
19. (g) W. H. Chapman Jr., R. Breslow, J. Am. Chem. Soc. 1995, 117, 5462-5469.
20. a) K. G. Ragunhatan, H.-J. Schneider, Angew. Chem. 1996, 108, 1314-1316; Angew. Chem. Int. Ed. Engl. 1996, 35, 1214-1221;
21. a) K. G. Ragunhatan, H.-J. Schneider, Angew. Chem. 1996, 108, 1314-1316; Angew. Chem. Int. Ed. Engl. 1996, 35, 1214-1221;
22. (b) H.-J. Schneider, R. Hettich, J. Am. Chem. Soc. 1997, 119, 5638-5647.
23. a) P. Rossi, F. Felluga, P. Tecilla, F. Formaggio, M. Crisma, C. Toniolo, P. Scrimin, J. Am. Chem. Soc. 1999, 121, 6948-6949;
24. (b) P. Rossi, F. Felluga, P. Tecilla, F. Formaggio, M. Crisma, C. Toniolo, P. Scrimin, Biopolymers, Pept. Sci. 2000, 55, 496-501;
25. (c) C. Sissi, P. Rossi, F. Felluga, F. Formaggio, M. Palumbo, P. Tecilla, C. Toniolo, P. Scrimin, J. Am. Chem. Soc. 2001, 123. 3169-3170;
26. (d) A. Scarso. U. Scheffer, M. Göbel, Q. B. Broxterman, B. Kaptein, F. Formaggio, C. Toniolo, P. Scrimin, Proc. Natl. Acad. Sci. USA 2002, 99, 5144-5149.
27. P. Pengo, L. Pasquato, S. Moro, A. Brigo, F. Fogolari, Q. B. Broxterman, B. Kaptein, P. Scrimin, Angew. Chem. 2003, 115, 3510-3514; Angew. Chem. Int. Ed. 2003, 42, 3388-3392.
28. P. Pengo, L. Pasquato, S. Moro, A. Brigo, F. Fogolari, Q. B. Broxterman, B. Kaptein, P. Scrimin, Angew. Chem. 2003, 115, 3510-3514; Angew. Chem. Int. Ed. 2003, 42, 3388-3392.
29. P. Rossi, F. Felluga, P. Scrimin, Tetrahedron Lett. 1998, 39, 7159-7162.
30. L. Baltzer, K. S. Broo, Biopolymers 1998, 47, 31-40.
31. G.T. Dolphin, L. Brive, G. Johansson, L. Baltzer, J. Am. Chem. Soc. 1996, 118, 11297-11298.
32. L. Brive, G. T. Dolphin, L. Baltzer, J. Am. Chem. Soc. 1997, 119, 8548-8607.
33. R. B. Hill, W. F. De Grado, J. Am. Chem. Soc. 1998, 120, 1138-1145.
34. S. F. Betz, W. F. De Grado, Biochemistry, 1996, 35, 6955-6962.
35. M. D. Struthers, R. P. Cheng, B. Imperiali, Science. 1996, 271, 342-325.
36. S. K. Broo, L. Brive, P. Ahlberg, L. Baltzer, J. Am. Chem. Soc. 1997, 119, 11362-11372.
37. a) S. Olofsson, G. Johansson, L. Baltzer, J. Chem. Soc. Perkin Trans. 2 1995, 2047-2056;
38. (b) J. Nilsson, K. S. Broo, R. S. Sott, L. Baltzer, Can. J. Chem. 1999, 77, 990-996;
39. (c) J. Nilsson, L. Baltzer, Chem. Eur. J. 2000, 6, 2214-2220.
40. S. Olofsson, L. Baltzer, Folding Des. 1996, 1, 347-356.
41. Y. H. Chen, J. T. Yang, K. H. Chan, Biochemistry 1974, 13, 3350-3359.
42. M. Engel. R. W. Williams, B. W. Erickson, Biochemistry 1991, 30, 3161-3169.
43. R. M. Smith, A. E. Martell, Critical Stability Constants. Vol. 6 Plenum, New York, 1989.
44. L. Baltzer, H. Nilsson, J. Nilsson, Chem. Rev. 2001, 101, 3153-3164.
45. N. Greenfield, G. D. Fasmanm, Biochemistry 1969, 8, 4108-4116.
46. "Mechanisms in Protein Folding": Frontiers in Molecular Biology (Ed.: R. H. Pain), Oxford University Press, Oxford, 1994.
47. II contrary to expectations (the plateaux is reached at ca. four equivalents of added ions). We believe that the apparent levelling off of the ellipticity is the result of two opposite effects due to metal ion binding: a higher lipophilicity of the peptide related to deprotonation (helical content increases, see Figure 3) and electrostatic repulsion (helical content decreases). Likely in that concentration range the two effects are very similar.
48. S. Y. M. Lau, A. K. Taneja, R. S. Hodges, J. Biol. Chem. 1984. 259, 13253-13261.
49. II to indicate these complexes. This does not imply that we are dealing with the n nuclear complexes. In fact, as clearly shown for PR I. the real molecularity of the complexes is not known and in most cases is less than n.
50. -4M concentration of substrate.
51. a) K. Michaelis, M. Kalesse, Angew. Chem. 1999, 111, 2382-2385; Angew. Chem. Int. Ed. 1999, 38, 2243-2245;
52. a) K. Michaelis, M. Kalesse, Angew. Chem. 1999, 111, 2382-2385; Angew. Chem. Int. Ed. 1999, 38, 2243-2245;
53. (b) J. C. Verheijen, B. Deiman, E. Y. Yeheskiely, G. A. van der Marel, J. H. Van Boom, Angew. Chem. 2000, 112, 377-380; Angew. Chem. Int. Ed. 2000, 39, 369-372.
54. (b) J. C. Verheijen, B. Deiman, E. Y. Yeheskiely, G. A. van der Marel, J. H. Van Boom, Angew. Chem. 2000, 112, 377-380; Angew. Chem. Int. Ed. 2000, 39, 369-372.
55. K. Worm, F. Chu, K. Matsumoto, M. D. Best, V. Lynch, E. V. Anslyn, Chem. Eur. J. 2003, 9, 741-747.
56. P. Molenveld, W. M. G. Stickvoort, H. Kooijman, A. L. Spek, J. F. J. Engbersen, D. N. Reinhoudt, J. Org. Chem. 1999, 64, 3896-3906.
57. A. Scarso, P. Scrimin in Pseudo-Peptides in Drug Development (Ed.: P. E. Nielsen), Wiley-VCH, Weinheim, 2004, pp. 223-240.