臺灣博碩士論文加值系統

Intrinsic properties of molecules provide an important benchmark for understanding properties in solution and are usually investigated by theoretical calculations and gas-phase experiments. Proton and metal-ion affinities are examples of intrinsic properties and have been measured successfully. Data obtained using kinetic methods have been analyzed to provide relative ion affinities for the competitive dissociation involved. In this work, we studied the relative sodium and calcium ion affinities of 20 common α–amino acids. The relative sodium ion affinities of amino acid anions are obtained by comparing the ratios of intensities of [A.A.1-H+]- and [A.A.2-H+]- dissociating from [NaI(A.A.1)(A.A.2)-2H+]-. The relative calcium ion affinities of amino acid complexes are obtained by comparing the ratios of [CaII(A.A.1)(A.A.2)-H+]+ and [CaII(A.A.1)2 -H+]+ dissociating from [CaII(A.A.1)2(A.A.2)-H+]+ and the ratios of [CaII(A.A.1)(A.A.2)-H+]+ and [CaII(A.A.2)2-H+]+ dissociating from [CaII(A.A.1)(A.A.2)2-H+]+. Calcium-bound dimeric cluster ions are too strongly bound to create simple Ca2+-bound monomeric ions. By contrast with the dimeric cluster ions, the Ca2+-bound trimeric cluster ions fragment readily by simple ligand losses. The affinities involve both deprotonation and calcium ion binding energies, so we subtracted the deprotonation energies to obtain the relative calcium ion binding energies. The temperature required in calculating the metal binding energies of amino acids was obtained by measuring the ratio of [A.A.1+H+]+ and [A.A.2+H+]+ dissociating from [A.A.1+ A.A.2+H+]+.

Catalog

Abstract
Introduction……………………………………………………………1

1.1 Importance of Metal in Biology………………………………1
1.2 The Kinetic Method…………………………………………....3
1.3 The Development of Mass Spectrometry………………………5
1.4 Principles of Electrospray Ionization…….………………8
1.5 Tandem Mass Spectrometry………………………………….…11

Experimental Section……………………………………………….12

2.1 Chemicals…………………………………………………………12
2.2 Mass Spectrometry………………………………………………12
2.3 The Kinetic Method…..……………………………………….14
2.3.1. Sodium Ion Affinities…………………….………………14
2.3.2. Calcium Ion Affinities…………………………………..17
2.3.3. Effective Temperature…………………………………….19

Results and Discussion………………………….…………………20

3.1 Dissociation of the Na+-Bound Heterodimers………….…20
3.2 Sodium Affinities of Amino Acids………………………….27
3.3 Sodium Affinity Order of Amino Acids…………………….37
3.4 Dissociation of the Ca2+-Bound Trimers………………….38
3.5 Calcium Affinities of Amino Acid Complexes…………….44
3.6 Comparison of the Calcium Ion Affinity Order to Alkali Metal Ion Affinities………………………………………………52
3.7 The Relative Metal Binding Energies of Amino Acids….54
3.8 The Calcium Binding Energies of Amino Acids Complexes…..............................................61

Conclusions……………………………………………………………64

References……………………………………………………………65

Appendix I. Twenty Commonα–Amino Acids………………………71

Appendix II. Standard Deviation of Metal-Bound Amino Acid Pairs….................................................73

References

1. (a) Hughes, M. N. The Inorganic Chemistry of Biological Processes, 2nd ed.; Wiley: New York, 1972. (b) Berg, J. M. Cold Spring Harbor Symp. Quant. Biol. 1987.
2. (a) Creighton, T. E. Proteins: Structure and Molecular Properties, 2nd ed.; Freeman; New York, 1993. (b) Bertini, I.; Gray, H. B.; Lippard, S. J.; Valentine, J. S. Bioinorganic Chemistry; University Science Book: Mill Valley, CA, 1994.
3. (a) Kaim, W.; Schwedersli, B. Bioinorganic Chemistry: Inorganic Elements in the Chemistry of Life; John Wiley & Sons: Chichester, 1994. (b) Aidley D. J.; Stanfield P. R. Ion Channels: Molecules in Action, Cambridge University Press, Cambridge, 1996.
4. Baker, W. C.; Ketcham, L. K.; Dayhoff, M. O.; In Atlas of Protein Sequence and Structure, Vol. 5; Dayhoff, M. O., Ed.; National Biochemical Research Foundation: Silver Spring, MD, 1965.
5. Vogt, H. P.; Strassburger, W.; Wollmer, A.; Fleischhauer, J.; Bullard, B.; Mercola, D. J. Theor. Biol. 1979, 76, 297-310.
6. Reid, R. E.; Hodges, R. S. J. Theor. Biol. 1980, 84, 401-444.
7. Gariépy, J.; Hodges, R. S. FEBS Lett. 1983, 160, 1-6.
8. Crivici, A.; Ikura, M. Annu. Rev. Biophys. Struct. 1995, 24, 85-116.
9. Kretsinger, R. H.; Nockolds, C. E. J. Biol. Chem. 1973, 248, 3313-3326.
10. Cooks, R. G.; Patrick, J. S.; Kotiaho, T.; McLuckey, S. A. Mass Spectrom. Rev. 1994, 13, 287-339.
11. Cooks, R G.; Kruger, T. L. J. Am. Chem. Soc. 1977, 99, 1279-1281.
12. Grual, S. T.; Schnute, M. E.; Squires, R. R. Int. J. Mass Spectrom. Ion Processes, 1990, 96, 181-198.
13. Boand, G.; Hourient, R.; Gaumann, T. J. Am. Chem. Soc. 1983, 105, 2203-2206.
14. McLuckey, S. A.; Shoen, A. E.; Cooks, R. G., J. Am. Chem. Soc. 1982, 104, 848-850.
15. Fourine, J. J.; Puzo, G. Anal. Chem. 1985, 57, 2287-2289.
16. Eberlin, M. N.; Kotiaho, T.; Shay, B. J.; Yang, S. S.; Cooks, R. G. J. Am. Chem. Soc. 1994, 116, 2457-2465.
17. Burinsky, D. J.; Fukuda E. K.; Campana, J. E. J. Am. Chem. Soc. 1984, 106, 2770-2771.
18. (a) Bojesen, G. J. Am. Chem. Soc. 1987, 109, 5557-5558. (b) Isa, K.; Omote, T.; Amaya, M. Org. Mass Spectrom. 1990, 25, 620-628. (c) Wu, Z.; Fenselau, C. Rapid Commun. Mass Spectrom. 1992, 6, 403-405. (d) Bojesen, G.; Breindahl, T. J. Chem. Soc., Perkin Trans. II 1994, 1029-1037.
19. Wu, Z.; Fenselau, C. J. Am. Chem. Soc. Mass Spectrom. 1992, 3, 863-866.
20. Zhang, K.; Zimmerman, D. M.; Chung-Phillips, A.; Cassady, C. J. J. Am. Chem. Soc. 1993, 115, 10812-10822.
21. Meot-Ner, M.; Hunter, E. P.; Field, F. H. J. Am. Chem. Soc. 1979, 101, 686-689.
22. Locke, M. J.; McIver, R. T. J. Am. Chem. Soc. 1983, 105, 4226-4232.
23. Gorman, G. S.; Speir, J. P.; Turner, C. A.; Amster, I. J. J. Am. Chem. Soc. 1992, 114, 3986-3988.
24. Wu, J.; Lebrilla, C. B. J. Am. Chem. Soc. 1993, 115, 3270-3275.
25. Yao, Z.; Wan, T. S. M.; Kwong, K.; Che, C. Chem. Commun. 1999, 20, 2119-2120.
26. Tao, W. A.; Zhang, D.; Wang, F.; Thomas, P.; Cooks, R. G. Anal. Chem. 1999, 71, 4427-4429.
27. Tao, W. A.; Zhang D., Nikolaev, E. N., Cooks, R. G., J. Am. Chem. Soc. 2000, 122, 10598-10609.
28. Thomson, J. J. Rays of Positive Electricity and Their Application to Chemical Analyses. Longmans, Green and Co, London, 1913.
29. Aston, F. W. Mass Spectra and isotopes, ed 3. Edward Arnold and Co, London, 1942.
30. Meyerson, S. Anal Chem 1994, 66, 960A-964A.
31. Biemann, K. Mass Spectrometry: Applications to Organic Chemistry. McGraw-Hill, New York, 1962.
32. Nier, A. O. Rev Sci Instrum. 1947, 18, 415-421.
33. Munson, M. S. B.; Field, F. H. J. Am. Chem. Soc. 1960, 88, 2621-2630.
34. Beckey, H. D.; Oxford, P. 1977.
35. Barber, M.; Bordoli, R. S.; Elliott, G. J.; Sedgwick, R. D.; Tyler, A. N. Anal. Chem. 1982, 54, 645A-657A.
36. Benninghoven, A.; Rudenauer, F. G.; Werner, H. W. Wiley, New York, 1987.
37. Cotter, R. J. Anal. Chem. 1988, 60, 817A.
38. Unsold, E.; Hillenkamp, F.; Nitsche, R. Analysis. 1990, 4, 115.
39. Detter, L.; Hand, O.; Cooks, R. G.; Walton, R. A. Mass Spectrom Rev 1988, 7, 465-502.
40. David, D. E.; Michel, J. Prog Solid St. Chem. 1989, 19, 283-328.
41. Magnera, T. F.; David, D. E.; Stulik, D.; Orth, R. G.; Jonkman, H. T.; Michel, J. J. Am. Chem. Soc. 1989, 111, 5036-5043.
42. Yamashita, M.; Fenn, J. B. J. Phys. Chem. 1984, 88, 4451-4459.
43. Karas, M.; Hillenkamp, F. Anal. Chem. 1988, 60, 2299-2301.
44. Gaskell, S. J. J. Mass Spectrom. 1997, 32, 677-688.
45. Luettgens, U.; Roellgen, F. W. Proceeding of 39th ASMS Conference on Mass Spectrometry and Allied Topics, Nashville, Tenn., 1991, 439-440.
46. Waston, J. T. Introduction to Mass Spectrometry, Lippincott-Raven Publisher, New York, 1997.
47. Hoffmann E. D. J. Mass Spectrom. 1996, 31, 129-137.
48. Bojesen, G.; Breindahl, T.; Andersen, U. N. Org. Mass Spectrom. 1993, 28, 1448-1452.
49. Wan, Y. F.; Gronert, S.; Lebrilla, C. B. J. Am. Chem. Soc. 1999, 121, 1365-1371.
50. Robinson, P. J.; Holbrook, K. A. Unimolecular Reactions; Wiley- Interscience: Lodon, 1972.
51. McLuckey, S. A.; Cameron, D.; Cooks, R. G. J. Am. Chem. Soc. 1981, 103, 1313-1317.
52. (a) Wu, Z.; Fenselau, C. Rapid Commun. Mass Spectrom. 1994, 8, 777-780. (b) Lias, S. G.; Bartmess, J. E.; Liebman, J. F.; Holmes, J. L.; Levin, R. D.; Mallard, W. G. J. Phys. Chem. Ref. Data 1988, 17, Suppl. 1. (c) Cerda, B. A.; Wesdemiotis, C. J. Am. Chem. Soc. 1995, 117, 9734-9739.
53. (a) Sigel, H.; Martin, R. B. Chem. Rev. 1982, 82, 385-426. (b) Meot-Ner, M. J. Am. Chem. Soc. 1988, 110, 3071-3075.
54. Kish, M. M.; Ohanessian, G.; Wesdemiotis, C. Int. J. Mass Spectrom. 2003, 227, 509-524.
55. Bai, Y.; Milne, J. S.; Mayne, L.; Englander, S. W. Proteins: Structure, Function, and Genetics 1993, 17, 75-86.
56. Nemirovskiy, O. V.; Gross, M. L. J. Am. Soc. Mass Spectrom. 2000, 11, 770-779.
57. (a) Moision, R. M.; Armentrout, P. B. J. Phys. Chem. A. 2006, 110, 3933-3946. (b) Moision, R. M.; Armentrout, P. B. Phys. Chem. Phys. Chem. 2004, 6, 2588-2599. (C) Ruan, C. H.; Yang, Z. B.; Hallowita, N.; Rogers, M. T. J. Phys. Chem. A. 2005, 109, 11539-11550.
58. Armentrout, P. B.; Rodgers, M. T. Acc. Chem. Res. 2004, 37, 989-998.
59. Andersen, U. N.; Bojesen, G. J. Chem. Soc., Perkins Trans. II 1997, 2, 323-327.
60. Thomas, P. D.; Koskinen, J. T.; Cooks, R. G. J. Mass Spectrom. 1999, 34, 85-92.
61. Vékey, K. J. Mass Spectrom. 1996, 31, 445-463.
62. Brauman, J. I.; Choo, B.; Zhong, M.; Craig, S. L. J. Phys. Chem. A 1997, 101, 19-24.
63. Majundar, T. J.; Clairet, F.; Tabet, J. C.; Cooks, R. G. J. Am. Chem. Soc. 1992, 114, 2897-2903.
64. Chen, L. Z.; Miller, J. M. Org. Mass Spectrom. 1992, 27, 883-890.
65. C. X.; Wu, Z.; Fenselau, C. J. Am. Chem. Soc. Mass Spectrom. 1993, 115, 4844-4848.
66. McLuckey, S. A.; Cooks, R. G.; Fulford, J. E. Int. J. Mass Spectrom. Ion Processes, 1983, 52, 165-174.
67. Chen, L. Z.; Miller, J. M. J. Organoment. Chem. 1993, 448, 225-232.
68. Cox, M. M.; Nelson, D. L. Lehninger Principles of Biochemistry, ed 3. Worth Publisher, New York, 2000.