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1 Precise Functional Analysis of Biological Macromolecules Promoted by the Encounter of Crystallographic and Spectroscopic Molecular Structure Analyses Takamitsu Kohzuma*, Sachiko Yanagisawa, and Tomotake Niizeki Faculty of Science, Ibaraki University The three dimensional structure of protein molecule is an essential for the comprehension of numerous life phenomena and the industrial utilization of biological systems. It is important to determine the three dimensional structure of biological macromolecule components by a certain techniques, X-ray crystallographic structure analysis, neutron crystallographic structure analysis or NMR. Although these structure analyses are very sophisticated methods for the determination of the biological macromolecule, the spectroscopic techniques are very important for the complete understanding of the time-dependent biological phenomena accompanying with the structural alternation of the relevant functional components, such as proteins and nucleic acids. The UV resonance Raman spectroscopy is introduced as an example for the precise local structure analysis with the X-ray crystallographic structure of protein molecules. DNA X NMR X X X
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3 1000 O 2 O 2 O 2 T R T R T 215cm -1 R 221cm -1 T R T R Kitagawa T O 2 H + C 13 =C 14 K L M N O / Cu(II) Dave S Cu(II)-S - Cu-S - Kohzuma
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5 (a) ph 4.0 (b) ph 6.9 (c) ph 11.0 (a) 244 nm 244 nm (b) 244 nm (a)
6 ph (b) (c) 244 nm 1616 cm -1 (Y8a) 1604 cm cm -1 pk a 880 cm -1 W17 NH 1360 / 1340 cm -1 I (1360) / I (1340) 1 1 C α C β -C 3 C 2 2 χ 2,1 11 NCN ND 12 N ph* pk a 1602 cm -1 C 4 C 5 C α C β -C 4 C 5 χ 2, cm cm cm C 4 C cm
7 T R ph 229nm Bohr 15 Nagai His (HRP) IX 6 His42( His) Arg38 Asn X Hashimoto 17 SOD O - 2 O 2 H 2 O 2 SOD O OD nm nm Cys78 Met86 His40 His81 20
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16 (1982). 12. L. M. Markham, L. C. Mayne, B. S. Hudson, M. Z. Zgierski, J. Phys. Chem., 97, (1993). 13. H. Takeuchi, Y. Kimura, I. Koitabashi and I. Harada, J. Raman Spectrosc., 22, , (1991). 14. T. Miura, T. Satoh, A. Hori-i and H. Takeuchi, J. Raman Spectrosc., 29, (1998). 15. X. Zhao, D. Wang, T. G. Spiro, J. Am. Chem. Soc. 120, (1998). 16. M. Nagai, M. Aki, R. Li, Y. Jin, H. Sakai, S. Nagatomo, T. Kitagawa, Biochemistry, 39, 43, (2000). 17. S. Hashimoto and H. Takeuchi, J. Am. Chem. Soc., 120, (1998). 18. S. Hashimoto, K. Ono, H. Takeuchi, J. Raman. Spectrosc., 24, (1998). 19. K. Sato, S. Nagatamo, C. Dennison, T. Niizeki, T. Kitagawa, T. Kohzuma, Inorg. Chim. Acta, in press. 20. T. Inoue, N. Nishio, S. Suzuki, K. Kataoka, T. Kohzuma, Y. Kai, J. Biol. Chem., 274, (1999). 21. S. Yanagisawa, M. Aki, T. Kitagawa, T. Kohzuma, unpublished results. 22. S. Katoh and A. Takamiya, Nature, 189, 665 (1961). 23. P. M. Colman, H. C. Freeman, J. M. Guss, M. Murata, V. A. Norris, J. A. Ramshaw, M. P. Venkatappa, Nature, 272, (1978). 24. J. M. Guss, P. R. Harrowell, M. Murata, V. A. Norris, H. C. Freeman, J. Mol. Biol., 192, (1986). 25. M. G. Segal, A. G. Sykes, J. Am. Chem. Soc., 100, 4585 (1978) 26. P. Crowley, G. Otting, B. G. Schlarb-Ridley, G. W. Canters, M. Ubbink, J. Am. Chem. Soc., in press. 27. S. Hirota, M. Endo, K. Hayamizu, T. Tsukazki, T. Takabe, T. Kohzuma, O. Yamauchi, J. Am. Chem. Soc., 121, (1999). 28. T. Kohzuma, T. Inoue, F. Yoshizaki, Y. Sasakawa, K. Onodera, S. Nagatomo, T. Kitagawa, S. Uzawa, Y. Isobe, Y. Sugimura, M. Gotowda, Y. Kai, J Biol. Chem., 274, (1999). 29. T. Inoue, M. Gotowda, H. Sugawara, T. Kohzuma, F. Yoshizaki, Y. Sugimura, Y. Kai, Biochemistry, 38, (1999). 30. O. Yamauchi, A. Odani, T. Kohzuma, H. Masuda, K. Toriumi, K. Saito, Inorg. Chem., 28, (1989). 31. E. V. Pletneva, D. B. Fulton, T. Kohzuma, N. M. Kostic, J. Am. Chem. Soc., 122, (2000).
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