Covalent hemin-DNA adducts for generating a novel class of artificial heme enzymes

Angewandte Chemie - International Edition

Volumn 44, Issue 17, 2005, Pages 2603-2606

  Fruk, Ljiljana ^a   Niemeyer, Christof M ^a  

^a TU DORTMUND UNIVERSITY   (Germany)

Author keywords

DNA; Enzymes; Heme proteins; Immobilization; Self assembly

Indexed keywords

BIOMATERIALS; CATALYSTS; CHEMICAL BONDS; DNA; SENSORS;

APO-ENZYMES; ARTIFICIAL HEME ENZYMES; BINDING PROPERTIES; RECONSTITUTION;

ENZYMES;

ENZYME; HEMIN;

ARTICLE; CHEMISTRY; DNA ADDUCT;

DNA ADDUCTS; ENZYMES; HEMIN;

EID: 18144406582     PISSN: 14337851     EISSN: None     Source Type: Journal    
DOI: 10.1002/anie.200462567     Document Type: Article

References (34)

1. C. M. Niemeyer, C. A. Mirkin, Nanobiotechnology: Concepts, Methods and Applications, Wiley-VCH, Weinheim, 2004.
2. C. M. Niemeyer, Trends Biotechnol. 2002, 20, 395-401.
3. The reconstitution of apo-enzymes, in particular glucose oxidase with chemically modified flavin adenine dinucleotide (FAD) cofactors, has been used to generate artificial enzyme conjugates and to immobilize such enzymes to electrode surfaces. For examples, see: a) A. Riklin, E. Katz, I. Willner, A. Stocker, A. F. Buckmann, Nature 1995, 376, 672-675; b) M. Zayats, E. Katz, I. Willner, J. Am. Chem. Soc. 2002, 124, 2120-2121; c) M. Zayats, E. Katz, I. Willner, J. Am. Chem. Soc. 2002, 124, 14 724-14 735; d) Y. Xiao, F. Patolsky, E. Katz, J. F. Hainfeld, I. Willner, Science 2003, 299, 1877-1881; e) E. Katz, L. Sheeney-Haj-Ichia, I. Willner, Angew. Chem. 2004, 116, 3354-3362; Angew. Chem. Int. Ed. 2004, 43, 3292-3300, and references therein.
4. The reconstitution of apo-enzymes, in particular glucose oxidase with chemically modified flavin adenine dinucleotide (FAD) cofactors, has been used to generate artificial enzyme conjugates and to immobilize such enzymes to electrode surfaces. For examples, see: a) A. Riklin, E. Katz, I. Willner, A. Stocker, A. F. Buckmann, Nature 1995, 376, 672-675; b) M. Zayats, E. Katz, I. Willner, J. Am. Chem. Soc. 2002, 124, 2120-2121; c) M. Zayats, E. Katz, I. Willner, J. Am. Chem. Soc. 2002, 124, 14 724-14 735; d) Y. Xiao, F. Patolsky, E. Katz, J. F. Hainfeld, I. Willner, Science 2003, 299, 1877-1881; e) E. Katz, L. Sheeney-Haj-Ichia, I. Willner, Angew. Chem. 2004, 116, 3354-3362; Angew. Chem. Int. Ed. 2004, 43, 3292-3300, and references therein.
5. The reconstitution of apo-enzymes, in particular glucose oxidase with chemically modified flavin adenine dinucleotide (FAD) cofactors, has been used to generate artificial enzyme conjugates and to immobilize such enzymes to electrode surfaces. For examples, see: a) A. Riklin, E. Katz, I. Willner, A. Stocker, A. F. Buckmann, Nature 1995, 376, 672-675; b) M. Zayats, E. Katz, I. Willner, J. Am. Chem. Soc. 2002, 124, 2120-2121; c) M. Zayats, E. Katz, I. Willner, J. Am. Chem. Soc. 2002, 124, 14 724-14 735; d) Y. Xiao, F. Patolsky, E. Katz, J. F. Hainfeld, I. Willner, Science 2003, 299, 1877-1881; e) E. Katz, L. Sheeney-Haj-Ichia, I. Willner, Angew. Chem. 2004, 116, 3354-3362; Angew. Chem. Int. Ed. 2004, 43, 3292-3300, and references therein.
6. The reconstitution of apo-enzymes, in particular glucose oxidase with chemically modified flavin adenine dinucleotide (FAD) cofactors, has been used to generate artificial enzyme conjugates and to immobilize such enzymes to electrode surfaces. For examples, see: a) A. Riklin, E. Katz, I. Willner, A. Stocker, A. F. Buckmann, Nature 1995, 376, 672-675; b) M. Zayats, E. Katz, I. Willner, J. Am. Chem. Soc. 2002, 124, 2120-2121; c) M. Zayats, E. Katz, I. Willner, J. Am. Chem. Soc. 2002, 124, 14 724-14 735; d) Y. Xiao, F. Patolsky, E. Katz, J. F. Hainfeld, I. Willner, Science 2003, 299, 1877-1881; e) E. Katz, L. Sheeney-Haj-Ichia, I. Willner, Angew. Chem. 2004, 116, 3354-3362; Angew. Chem. Int. Ed. 2004, 43, 3292-3300, and references therein.
7. The reconstitution of apo-enzymes, in particular glucose oxidase with chemically modified flavin adenine dinucleotide (FAD) cofactors, has been used to generate artificial enzyme conjugates and to immobilize such enzymes to electrode surfaces. For examples, see: a) A. Riklin, E. Katz, I. Willner, A. Stocker, A. F. Buckmann, Nature 1995, 376, 672-675; b) M. Zayats, E. Katz, I. Willner, J. Am. Chem. Soc. 2002, 124, 2120-2121; c) M. Zayats, E. Katz, I. Willner, J. Am. Chem. Soc. 2002, 124, 14 724-14 735; d) Y. Xiao, F. Patolsky, E. Katz, J. F. Hainfeld, I. Willner, Science 2003, 299, 1877-1881; e) E. Katz, L. Sheeney-Haj-Ichia, I. Willner, Angew. Chem. 2004, 116, 3354-3362; Angew. Chem. Int. Ed. 2004, 43, 3292-3300, and references therein.
8. The reconstitution of apo-enzymes, in particular glucose oxidase with chemically modified flavin adenine dinucleotide (FAD) cofactors, has been used to generate artificial enzyme conjugates and to immobilize such enzymes to electrode surfaces. For examples, see: a) A. Riklin, E. Katz, I. Willner, A. Stocker, A. F. Buckmann, Nature 1995, 376, 672-675; b) M. Zayats, E. Katz, I. Willner, J. Am. Chem. Soc. 2002, 124, 2120-2121; c) M. Zayats, E. Katz, I. Willner, J. Am. Chem. Soc. 2002, 124, 14 724-14 735; d) Y. Xiao, F. Patolsky, E. Katz, J. F. Hainfeld, I. Willner, Science 2003, 299, 1877-1881; e) E. Katz, L. Sheeney-Haj-Ichia, I. Willner, Angew. Chem. 2004, 116, 3354-3362; Angew. Chem. Int. Ed. 2004, 43, 3292-3300, and references therein.
9. T. Yonetani, H. R. Drott, J. S. Leigh, Jr., G. H. Reed, M. R. Waterman, T. Asakura, J. Biol. Chem. 1970, 245, 2998-3003.
10. T. Yonetani, H. Yamamoto, G. V. Woodrow, J. Biol. Chem. 1974, 249, 682-690.
11. a) T. Hayashi, Y. Hisaeda, Acc. Chem. Res. 2002, 35, 35-43;
12. b) T. Hayashi, H. Dejima, T. Matsuo, H. Sato, D. Murata, Y. Hisaeda, J. Am. Chem. Soc. 2002, 124, 11 226-11 227;
13. c) H. Sato, T. Hayashi, T. Ando, Y. Hisaeda, T. Ueno, Y. Watanabe, J. Am. Chem. Soc. 2004, 126, 436-437, and references therein.
14. T. Hayashi, T. Takimura, H. Ogoshi, J. Am. Chem. Soc. 1995, 117, 11 606-11 607.
15. Y. Hitomi, T. Hayashi, K. Wada, T. Mizutani, Y. Hisaeda, H. Ogoshi, Angew. Chem. 2001, 113, 1132-1135; Angew. Chem. Int. Ed. 2001, 40, 1098-1101.
16. Y. Hitomi, T. Hayashi, K. Wada, T. Mizutani, Y. Hisaeda, H. Ogoshi, Angew. Chem. 2001, 113, 1132-1135; Angew. Chem. Int. Ed. 2001, 40, 1098-1101.
17. L. Wan, M. B. Twitchett, L. D. Eltis, A. G. Mauk, M. Smith, Proc. Natl. Acad. Sci. USA 1998, 95, 12 825-12 831.
18. T. Hayashi, Y. Hitomi, T. M. Ando, Y. Hisaeda, S. Kitagawa, H. Ogoshi, J. Am. Chem. Soc. 1999, 121, 7747-7750.
19. 2 as well as MALDI MS spectra and details on the solid-phase coupling of DNA with hemin, the reconstitution of apo-Mb, and the enzyme activity assays are available in the Supporting Information.
20. 2. Notably, the peroxidase activity of Mb is much lower than that of other peroxidases such as horseradish peroxidase.
21. 2 at a stoichiometric ratio of 1:1 to produce a brightly fluorescent and strongly absorbing reaction product. The chemical structure and reaction path of Amplex Red are shown in the Supporting Information (Figure S4).
22. a) C. M. Niemeyer, T. Sano, C. L. Smith, C. R. Cantor, Nucleic Acids Res. 1994, 22, 5530-5539;
23. b) C. M. Niemeyer, L. Boldt, B. Ceyhan, D. Blohm, Anal. Biochem. 1999, 268, 54-63;
24. c) C. M. Niemeyer, B. Ceyhan, Angew. Chem. 2001, 113, 3798-3801; Angew. Chem. Int. Ed. 2001, 40, 3685-3688;
25. c) C. M. Niemeyer, B. Ceyhan, Angew. Chem. 2001, 113, 3798-3801; Angew. Chem. Int. Ed. 2001, 40, 3685-3688;
26. d) M. Lovrinovic, R. Seidel, R. Wacker, H. Schroeder, O. Seitz, M. Engelhard, R. Goody, C. M. Niemeyer, Chem. Commun. 2003, 822-823;
27. e) U. Feldkamp, R. Wacker, W. Banzhaf, C. M. Niemeyer, ChemPhysChem 2004, 5, 367-372;
28. f) R. Wacker, C. M. Niemeyer, ChemBioChem 2004, 5, 453-459;
29. g) R. Wacker, H. Schroeder, C. M. Niemeyer, Anal. Biochem. 2004, 330, 281-287;
30. h) F. Kukolka, C. M. Niemeyer, Org. Biomol. Chem. 2004, 2, 2203-2206.
31. C. M. Niemeyer, W. Bürger, J. Peplies, Angew. Chem. 1998, 110, 2391-2395; Angew. Chem. Int. Ed. 1998, 37, 2265-2268.
32. C. M. Niemeyer, W. Bürger, J. Peplies, Angew. Chem. 1998, 110, 2391-2395; Angew. Chem. Int. Ed. 1998, 37, 2265-2268.
33. C. M. Niemeyer, J. Koehler, C. Wuerdemann, ChemBioChem 2002, 3, 242-245.
34. Previous work on electron transfer reactions occurring in a composite material prepared from myoglobin containing double-stranded DNA-modified hemin in poly(ethylene oxide) oligomers was carried out without characterization of the DNA-protein conjugate: K. Muneyasu, N. Y. Kawahara, H. Ohno, Solid State Ionics 1998, 113-115, 167-171.