Pinch-porphyrins, new spectroscopic and kinetic models of peroxidases

Abstract

The novel complexes [1,9-bis(2-pyridyl)-2,5,8-triazanonane]-(protoporphyrinato)iron(III) 4, -(mesoporphyrinato)iron(III) 5 and -(deuteroporphyrinato)iron(III) 6 were synthesized from the parent compounds chloro-(porphyrinato)iron(III) 1, -(mesoporphyrinato)iron(III) 2 and -(deuteroporphyrinato)iron(III) 3 and 1,9-bis(2-pyridyl)-2,5,8-triazanonane (picdien). The complexes 1–6 were characterized by UV/VIS, ¹H NMR and ESR spectroscopies and their catalytic activity was determined. The measured theoretical maximum rate constant (k_cat) for guaiacol + H₂O₂ → oxidation guaiacol products (guaiacol = 2-methoxyphenol) in the presence of complexes 4–6, were 7.6 × 10⁶, 4.4 × 10⁵ and 9.0 × 10⁴ mol^–1 s^–1, respectively. These peroxidase activities are to our knowledge the largest reported for model complexes. The UV/VIS spectra show Soret and Q bands for all compounds at energies typical of axially co-ordinated complexes with symmetry D_4h or lower. The intensity of the charge-transfer transitions indicates that the presence of the picdien ligand diminishes the distortion of the parent compounds. The ¹H NMR spectra of complexes 4–6 are indicative of six-co-ordinated complexes with different degrees of quantum mixed-spin (qms) state S = [/] into S = [/]. The ESR spectral features are characteristic of qms species, A and B, for each compound. Maltempo’s theory for qms states gives the admixture percentage of species A (53–64%) and species B (<8%) for each compound. The area ratio of the ESR B∶A signals follows the same order as the peroxidase activity shown by these complexes. A clear correlation is established among the peroxidase activity, the iron(III) out-of-porphyrin plane configuration and the qms state S = [/] and S = [/].

References

1. C. A. Reed and F. Guiset, J. Am. Chem. Soc., 1996, 118, 3281.
2. M. M. Maltempo, T. H. Moss and M. A. Cusanovich, Biochim. Biophys. Acta, 1974, 342, 290.
3. S. Ozaki, T. Matsui and Y. Watanabe, J. Am. Chem. Soc., 1996, 118, 9784.
4. M. M. Maltempo and T. H. Moss, Q. Rev. Biophys., 1976, 9, 181.
5. C. E. Schulz, R. Rutter, J. T. Sage, P. G. Debrunner and L. P. Hager, Biochemistry, 1984, 23, 4743.
6. B. G. J. M. Bolscher, H. Plat and R. Wever, Biochim. Biophys. Acta, 1984, 784, 177.
7. L. Casella, M. Gullotti, S. Poli, R. P. Ferrari, E. Laurenti and A. Marchesini, BioMetals, 1993, 6, 213.
8. G. La Mar, Biological Applications of Magnetic Resonance, Academic Press, New York, 1979, 305.
9. H. A. O. Hill and K. G. Morallee, J. Am. Chem. Soc., 1972, 94, 731.
10. M. Zobrist and G. N. La Mar, J. Am. Chem. Soc., 1978, 100, 1944.
11. T. G. Traylor, W. A. Lee and D. V. Stynes, J. Am. Chem. Soc., 1984, 106, 755.
12. H. M. Goff and M. A. Phillippi, J. Am. Chem. Soc., 1983, 105, 7567.
13. G. N. La Mar, D. B. Viscio, K. M. Smith, W. S. Caughey and M. L. Smith, J. Am. Chem. Soc., 1978, 100, 8085.
14. D. L. Budd, G. N. La Mar, K. C. Langry, K. M. Smith and R. Nayyir-Mazhir, J. Am. Chem. Soc., 1979, 101, 6091.
15. R. J. Kurland, R. G. Little, D. G. Davis and Ch. Ho, Biochemistry, 1971, 12, 2237.
16. T. G. Traylor and R. Popovitz-Biro, J. Am. Chem. Soc., 1988, 110, 239.
17. J. T. Groves, R. C. Haushalter, M. Nakamura, T. E. Nemo and B. J. Evans, J. Am. Chem. Soc., 1981, 103, 2884.
18. H. Fuji, J. Am. Chem. Soc., 1993, 115, 4641.
19. T. Castner, jun., G. S. Newell, W. C. Holton and C. P. Slichter, J. Chem. Phys., 1960, 32, 668.
20. R. D. Dowsing and J. F. Gibson, J. Chem. Phys., 1969, 50, 294.
21. C. Schaefer, M. Momenteau, J. Mispelter, B. Loock, C. Huel and J.-M. Lhoste, Inorg. Chem., 1986, 25, 4577.
22. F. S. Woo and H. C. Kelly, Inorg. Chim. Acta, 1994, 225, 255.
23. P. Jones, D. Mantle and I. Wilson, J. Chem. Soc., Dalton Trans., 1983, 29, 1434.
24. R. E. Rodriguez, F. S. Woo, D. A. Huckaby and H. C. Kelly, Inorg. Chem., 1990, 29, 1438.
25. H. M. Goff, E. T. Shimomura and M. A. Phillippi, Inorg. Chem., 1983, 22, 66.
26. M. M. Maltempo, J. Chem. Phys., 1974, 61, 2540.
27. C. A. Reed, T. Mashiko, S. P. Bentley, M. E. Kastner, W. R. Scheidt, K. Spartalian and G. Lang, J. Am. Chem. Soc., 1979, 101, 2948.
28. A. Boersma and H. M. Goff, Inorg. Chem., 1982, 21, 581.
29. B. J. Kennedy, K. S. Murray, P. R. Zwack, H. Homborg and W. Kalz, Inorg. Chem., 1986, 25, 2539.
30. L. N. Ohlhausen, D. Cockrum, J. Register, K. Roberts, G. J. Long, G. L. Powell and B. B. Huitchinson, Inorg. Chem., 1990, 29, 4886.
31. M. Kastner, T. Mashiko and C. A. Reed, J. Am. Chem. Soc., 1978, 100, 666.
32. H. Ogoshi, H. Sugimoto and Z. Yoshida, Biochim. Biophys. Acta, 1980, 621, 19.
33. D. A. Summerville, I. A. Cohen, K. Hatano and W. R. Scheidt, Inorg. Chem., 1978, 17, 2906.
34. D. H. Dolphin, J. R. Sams and T. B. Tsin, Inorg. Chem., 1977, 16, 711.
35. H. Masuda, T. Taga, K. Osaki, H. Sugimoto, Z. Yoshida and H. Ogoshi, Inorg. Chem., 1980, 19, 950.
36. G. P. Gupta, G. Lang, Y. J. Lee, R. Scheidt, K. Shelly and C. A. Reed, Inorg. Chem., 1987, 26, 3022.
37. M. Zerner, M. Gouterman and H. Kobayashi, Theor. Chim. Acta, 1966, 6, 363.
38. J. W. Owens and Ch. O'Connor, Coord. Chem. Rev., 1988, 84, 1.
39. M. Gouterman, in The Porphyrins, ed. D. Dolphin, Academic Press, New York, 1978, vol. 3. p. 69.
40. F. Adar, in The Porphyrins ed. D. Dolphin, Academic Press, New York, 1978, vol. 4, p. 167.
41. D. Dolphin, Isr. J. Chem., 1981, 21, 67.
42. E. I. Solomon, M. L. Kirk, D. R. Gamelin and S. Pulver, Methods Enzymol., 1995, 246, 71.
43. L. B. Dugad and S. Mitra, Proc. Indian Acad. Sci., Chem. Sci., 1984, 93, 295.
44. J. D. Satterlee and J. E. Erman, J. Am. Chem. Soc., 1981, 103, 199.
45. G. N. La Mar and F. A. Walker, in The Porphyrins, ed. D. Dolphin, Academic Press, London, 1978, vol. 4, p. 61.
46. E. González-Vergara, M. Meyer and H. M. Goff, Biochemistry, 1985, 24, 6561.
47. H. M. Goff, E. González-Vergara and M. R. Bird, Biochemistry, 1985, 24, 1007.
48. S. Mazumdar, O. K. Medhi and S. Mitra, Inorg. Chem., 1988, 27, 2541.
49. H. B. Dunford, in Peroxidases in Chemistry and Biology, eds. J. Everse, K. E. Everse and M. B. Grisham, CRC Press, Boca Raton, FL, 1990, vol. 2, p. 2.
50. R. H. Ilgner and A. E. Woods, Comp. Biochem. Physiol., B: Comp. Biochem., 1985, 82, 433.
51. A. L. Balch, Inorg. Chim. Acta, 1992, 198–200, 297.
52. F. S. Woo, M. Cahiwat-Alquiza and H. C. Kelly, Inorg. Chem., 1990, 29, 4718.
53. A. D. Falk, The Porphyrins and Metalloporphyrins, Elsevier, New York, 1964, p. 800.
54. A. D. Adler, D. L. Ostfeld and E. H. Abbot, Bioinorg. Chem., 1977, 7, 187.
55. E. Ahmed, C. Chartterjee, C. J. Coosksey, M. L. Tobe and G. Williams, J. Chem. Soc., Dalton Trans., 1989, 645.
56. H. U. Bergmeyer(Editor), Methods of Enzymatic Analysis, Academic Press, New York, 1974, p. 494.