Adenosylcobinamide, the Base-Free Analog of Coenzyme B12 (Adenosylcobalamin). 1.1 Probing the Role of the Axial 5,6-Dimethylbenzimidazole Base in Coenzyme B12 via Exogenous Axial Base Kassociation, ΔH, and ΔS Measurements plus a Critical Review of the Relevant Biochemical Literature

Inorganic Chemistry

Volumn 35, Issue 20, 1996, Pages 5912-5922

  Garr, Cheryl D ^a,b   Sirovatka, Jeanne M ^a   Finke, Richard G ^a  

^a Veterinary Dentistry and Oral Surgery   (United States)

^b MDS Inc   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0001171085     PISSN: 00201669     EISSN: None     Source Type: Journal    
DOI: 10.1021/ic951272j     Document Type: Article

References (162)

1. 12's Axial Base. Ph.D. Dissertation, February 1993.
2. (b) Part 2, Garr, C. D.; Sirovatka, J. M.; Finke, R. G. J. Am. Chem. Soc., in press.
3. assoc, ΔH, ΔS, and Co - C cleavage product and kinetic studies; to be submitted for publication in J. Am. Chem. Soc.).
4. (a) Lenhert, P. G. Proc. R. Soc. London, Ser. A 1968, 303, 45.
5. 12 are available: Bouquiere, J. P.; Finney, J. L.; Lehmann, M. S.; Lindley, P. F.; Savage, H. F. J. Acta Crystallogr. 1993, B49, 79-89 (a 15 K structure). See also: Savage, H. F. J.; Lindley, P. F.; Finney, J. L.; Timmins, P. A. Acta Cryslallogr. 1987, B43, 280-295 (a 279 K structure).
6. 12 are available: Bouquiere, J. P.; Finney, J. L.; Lehmann, M. S.; Lindley, P. F.; Savage, H. F. J. Acta Crystallogr. 1993, B49, 79-89 (a 15 K structure). See also: Savage, H. F. J.; Lindley, P. F.; Finney, J. L.; Timmins, P. A. Acta Cryslallogr. 1987, B43, 280-295 (a 279 K structure).
7. + (adenosylcobinamide methyl phosphate; that is, the methylated phosphate (but 5,6-dimethylbenzimidazole free) form of AdoCbl); TEMPO (2,2,6,6-tetramethylpiperidinyl-1-oxy).
8. 12 and Intrinsic Factor; Zagalak, B., Friedrich, W., Eds.; Walter de Gruyter: New York, 1979. (c) Babior, B. M.; Krouwer, J. S. CRC Crit. Rev. Biochem. 1979, 6, 35. (d) Abeles, R. H.; Dolphin, D. Acc. Chem. Res. 1976, 9, 114. (e) Golding, B. T.; Rao, D. N. R. In Enzyme Mechanisms; Page, M. I., Williams, A., Eds.; Royal Society of Chemistry: London, 1987. (f) For a concise discussion of the possibility of an "ideal" Co - N bond to the axial 5,6-dimethylbenzimidazole ligand, see pp 248-249 of: Marzilli, L. In Bioinorganic Catalysis; Reedijk, J. Ed.; Marcel Dekker, Inc.: New York, 1993; pp 227-259. (g) Finke, R. G. In Molecular Mechanisms in Bioorganic Processes; Bleasdale, C., Golding, B. T., Eds.; The Royal Society of Chemistry: Cambridge, England 1990. (h) Finke, R. G.; Schiraldi, D. A.; Mayer, B. J. Coord. Chem. Rev. 1984, 54, 1.
9. 12 and Intrinsic Factor; Zagalak, B., Friedrich, W., Eds.; Walter de Gruyter: New York, 1979. (c) Babior, B. M.; Krouwer, J. S. CRC Crit. Rev. Biochem. 1979, 6, 35. (d) Abeles, R. H.; Dolphin, D. Acc. Chem. Res. 1976, 9, 114. (e) Golding, B. T.; Rao, D. N. R. In Enzyme Mechanisms; Page, M. I., Williams, A., Eds.; Royal Society of Chemistry: London, 1987. (f) For a concise discussion of the possibility of an "ideal" Co - N bond to the axial 5,6-dimethylbenzimidazole ligand, see pp 248-249 of: Marzilli, L. In Bioinorganic Catalysis; Reedijk, J. Ed.; Marcel Dekker, Inc.: New York, 1993; pp 227-259. (g) Finke, R. G. In Molecular Mechanisms in Bioorganic Processes; Bleasdale, C., Golding, B. T., Eds.; The Royal Society of Chemistry: Cambridge, England 1990. (h) Finke, R. G.; Schiraldi, D. A.; Mayer, B. J. Coord. Chem. Rev. 1984, 54, 1.
10. 12 and Intrinsic Factor; Zagalak, B., Friedrich, W., Eds.; Walter de Gruyter: New York, 1979. (c) Babior, B. M.; Krouwer, J. S. CRC Crit. Rev. Biochem. 1979, 6, 35. (d) Abeles, R. H.; Dolphin, D. Acc. Chem. Res. 1976, 9, 114. (e) Golding, B. T.; Rao, D. N. R. In Enzyme Mechanisms; Page, M. I., Williams, A., Eds.; Royal Society of Chemistry: London, 1987. (f) For a concise discussion of the possibility of an "ideal" Co - N bond to the axial 5,6-dimethylbenzimidazole ligand, see pp 248-249 of: Marzilli, L. In Bioinorganic Catalysis; Reedijk, J. Ed.; Marcel Dekker, Inc.: New York, 1993; pp 227-259. (g) Finke, R. G. In Molecular Mechanisms in Bioorganic Processes; Bleasdale, C., Golding, B. T., Eds.; The Royal Society of Chemistry: Cambridge, England 1990. (h) Finke, R. G.; Schiraldi, D. A.; Mayer, B. J. Coord. Chem. Rev. 1984, 54, 1.
11. 12 and Intrinsic Factor; Zagalak, B., Friedrich, W., Eds.; Walter de Gruyter: New York, 1979. (c) Babior, B. M.; Krouwer, J. S. CRC Crit. Rev. Biochem. 1979, 6, 35. (d) Abeles, R. H.; Dolphin, D. Acc. Chem. Res. 1976, 9, 114. (e) Golding, B. T.; Rao, D. N. R. In Enzyme Mechanisms; Page, M. I., Williams, A., Eds.; Royal Society of Chemistry: London, 1987. (f) For a concise discussion of the possibility of an "ideal" Co - N bond to the axial 5,6-dimethylbenzimidazole ligand, see pp 248-249 of: Marzilli, L. In Bioinorganic Catalysis; Reedijk, J. Ed.; Marcel Dekker, Inc.: New York, 1993; pp 227-259. (g) Finke, R. G. In Molecular Mechanisms in Bioorganic Processes; Bleasdale, C., Golding, B. T., Eds.; The Royal Society of Chemistry: Cambridge, England 1990. (h) Finke, R. G.; Schiraldi, D. A.; Mayer, B. J. Coord. Chem. Rev. 1984, 54, 1.
12. 12 and Intrinsic Factor; Zagalak, B., Friedrich, W., Eds.; Walter de Gruyter: New York, 1979. (c) Babior, B. M.; Krouwer, J. S. CRC Crit. Rev. Biochem. 1979, 6, 35. (d) Abeles, R. H.; Dolphin, D. Acc. Chem. Res. 1976, 9, 114. (e) Golding, B. T.; Rao, D. N. R. In Enzyme Mechanisms; Page, M. I., Williams, A., Eds.; Royal Society of Chemistry: London, 1987. (f) For a concise discussion of the possibility of an "ideal" Co - N bond to the axial 5,6-dimethylbenzimidazole ligand, see pp 248-249 of: Marzilli, L. In Bioinorganic Catalysis; Reedijk, J. Ed.; Marcel Dekker, Inc.: New York, 1993; pp 227-259. (g) Finke, R. G. In Molecular Mechanisms in Bioorganic Processes; Bleasdale, C., Golding, B. T., Eds.; The Royal Society of Chemistry: Cambridge, England 1990. (h) Finke, R. G.; Schiraldi, D. A.; Mayer, B. J. Coord. Chem. Rev. 1984, 54, 1.
13. 12 and Intrinsic Factor; Zagalak, B., Friedrich, W., Eds.; Walter de Gruyter: New York, 1979. (c) Babior, B. M.; Krouwer, J. S. CRC Crit. Rev. Biochem. 1979, 6, 35. (d) Abeles, R. H.; Dolphin, D. Acc. Chem. Res. 1976, 9, 114. (e) Golding, B. T.; Rao, D. N. R. In Enzyme Mechanisms; Page, M. I., Williams, A., Eds.; Royal Society of Chemistry: London, 1987. (f) For a concise discussion of the possibility of an "ideal" Co - N bond to the axial 5,6-dimethylbenzimidazole ligand, see pp 248-249 of: Marzilli, L. In Bioinorganic Catalysis; Reedijk, J. Ed.; Marcel Dekker, Inc.: New York, 1993; pp 227-259. (g) Finke, R. G. In Molecular Mechanisms in Bioorganic Processes; Bleasdale, C., Golding, B. T., Eds.; The Royal Society of Chemistry: Cambridge, England 1990. (h) Finke, R. G.; Schiraldi, D. A.; Mayer, B. J. Coord. Chem. Rev. 1984, 54, 1.
14. 12 and Intrinsic Factor; Zagalak, B., Friedrich, W., Eds.; Walter de Gruyter: New York, 1979. (c) Babior, B. M.; Krouwer, J. S. CRC Crit. Rev. Biochem. 1979, 6, 35. (d) Abeles, R. H.; Dolphin, D. Acc. Chem. Res. 1976, 9, 114. (e) Golding, B. T.; Rao, D. N. R. In Enzyme Mechanisms; Page, M. I., Williams, A., Eds.; Royal Society of Chemistry: London, 1987. (f) For a concise discussion of the possibility of an "ideal" Co - N bond to the axial 5,6-dimethylbenzimidazole ligand, see pp 248-249 of: Marzilli, L. In Bioinorganic Catalysis; Reedijk, J. Ed.; Marcel Dekker, Inc.: New York, 1993; pp 227-259. (g) Finke, R. G. In Molecular Mechanisms in Bioorganic Processes; Bleasdale, C., Golding, B. T., Eds.; The Royal Society of Chemistry: Cambridge, England 1990. (h) Finke, R. G.; Schiraldi, D. A.; Mayer, B. J. Coord. Chem. Rev. 1984, 54, 1.
15. 12 and Intrinsic Factor; Zagalak, B., Friedrich, W., Eds.; Walter de Gruyter: New York, 1979. (c) Babior, B. M.; Krouwer, J. S. CRC Crit. Rev. Biochem. 1979, 6, 35. (d) Abeles, R. H.; Dolphin, D. Acc. Chem. Res. 1976, 9, 114. (e) Golding, B. T.; Rao, D. N. R. In Enzyme Mechanisms; Page, M. I., Williams, A., Eds.; Royal Society of Chemistry: London, 1987. (f) For a concise discussion of the possibility of an "ideal" Co - N bond to the axial 5,6-dimethylbenzimidazole ligand, see pp 248-249 of: Marzilli, L. In Bioinorganic Catalysis; Reedijk, J. Ed.; Marcel Dekker, Inc.: New York, 1993; pp 227-259. (g) Finke, R. G. In Molecular Mechanisms in Bioorganic Processes; Bleasdale, C., Golding, B. T., Eds.; The Royal Society of Chemistry: Cambridge, England 1990. (h) Finke, R. G.; Schiraldi, D. A.; Mayer, B. J. Coord. Chem. Rev. 1984, 54, 1.
16. 12 contains a flexible and formally - 1 corrin ring and six important amide side chains and also contains an intramolecularly appended axial 5,6-dimethylbenzimidazole base.
17. For lead references see: (b) Schnauzer, G. N.; Windgassen, R. J. J. Am. Chem. Soc. 1966, 88, 3738. (c) Toscano, P. J.; Marzilli, L. G. Prog. Inorg. Chem. 1984, 31, 105. (d) Bresciani-Pahor, N.; Forcolin, M.; Marzilli, L. G.; Randaccio, L.; Summers, M. F.; Toscano, P. J. Coord. Chem. Rev. 1985, 63, 1. (e) Randaccio, L; Bresciani-Pahor, N.; Zangrando, E.; Marzilli, L. G. Chem. Soc. Rev. 1989, 18, 225. (f) See also ref 1a - r provided as part of the Supporting Information.
18. For lead references see: (b) Schnauzer, G. N.; Windgassen, R. J. J. Am. Chem. Soc. 1966, 88, 3738. (c) Toscano, P. J.; Marzilli, L. G. Prog. Inorg. Chem. 1984, 31, 105. (d) Bresciani-Pahor, N.; Forcolin, M.; Marzilli, L. G.; Randaccio, L.; Summers, M. F.; Toscano, P. J. Coord. Chem. Rev. 1985, 63, 1. (e) Randaccio, L; Bresciani-Pahor, N.; Zangrando, E.; Marzilli, L. G. Chem. Soc. Rev. 1989, 18, 225. (f) See also ref 1a - r provided as part of the Supporting Information.
19. For lead references see: (b) Schnauzer, G. N.; Windgassen, R. J. J. Am. Chem. Soc. 1966, 88, 3738. (c) Toscano, P. J.; Marzilli, L. G. Prog. Inorg. Chem. 1984, 31, 105. (d) Bresciani-Pahor, N.; Forcolin, M.; Marzilli, L. G.; Randaccio, L.; Summers, M. F.; Toscano, P. J. Coord. Chem. Rev. 1985, 63, 1. (e) Randaccio, L; Bresciani-Pahor, N.; Zangrando, E.; Marzilli, L. G. Chem. Soc. Rev. 1989, 18, 225. (f) See also ref 1a - r provided as part of the Supporting Information.
20. For lead references see: (b) Schnauzer, G. N.; Windgassen, R. J. J. Am. Chem. Soc. 1966, 88, 3738. (c) Toscano, P. J.; Marzilli, L. G. Prog. Inorg. Chem. 1984, 31, 105. (d) Bresciani-Pahor, N.; Forcolin, M.; Marzilli, L. G.; Randaccio, L.; Summers, M. F.; Toscano, P. J. Coord. Chem. Rev. 1985, 63, 1. (e) Randaccio, L; Bresciani-Pahor, N.; Zangrando, E.; Marzilli, L. G. Chem. Soc. Rev. 1989, 18, 225. (f) See also ref 1a - r provided as part of the Supporting Information.
21. For lead references see: (b) Schnauzer, G. N.; Windgassen, R. J. J. Am. Chem. Soc. 1966, 88, 3738. (c) Toscano, P. J.; Marzilli, L. G. Prog. Inorg. Chem. 1984, 31, 105. (d) Bresciani-Pahor, N.; Forcolin, M.; Marzilli, L. G.; Randaccio, L.; Summers, M. F.; Toscano, P. J. Coord. Chem. Rev. 1985, 63, 1. (e) Randaccio, L; Bresciani-Pahor, N.; Zangrando, E.; Marzilli, L. G. Chem. Soc. Rev. 1989, 18, 225. (f) See also ref 1a - r provided as part of the Supporting Information.
22. (a) Marzilli, L. G.; Toscano, P. J.; Randaccio, L.; Bresciani-Pahor, N.; Calligaris, M. J. Am. Chem. Soc. 1979, 101, 6754.
23. (b) Randaccio, L.; Bresciani-Pahor, N.; Toscano, P. J.; Marzilli, L. G. J. Am. Chem. Soc. 1980, 102, 7372.
24. (c) Randaccio, L.; Bresciani-Pahor, N.; Toscano, P. J.; Marzilli, L. G. J. Am. Chem Soc. 1981, 103, 6347.
25. (d) Bresciani-Pahor, N.; Randaccio, L.; Toscano, P. J.; Marzilli, L. G. J. Chem. Soc., Dalton Trans. 1982, 567.
26. (e) Summers, M. F.; Toscano, P. J.; Bresciani-Pahor, N.; Nardin, G.; Randaccio, L.; Marzilli, L. G. J. Am. Chem. Soc. 1983, 105, 6259.
27. (f) Summers, M. F.; Marzilli, L. G.; Bresciani-Pahor, N. Randaccio, L. J. Am. Chem. Soc. 1984, 106, 4478.
28. (g) Bresciani-Pahor, N.; Randaccio, L.; Zangrando, E.; Summers, M. F.; Ramsden, J. H., Jr.; Marzilli, P. A.; Marzilli, L. G. Organometallics 1985, 4, 2086.
29. (h) Parker, W. O., Jr.; Bresciani-Pahor, N.; Zangrando, E. Randaccio, L.; Marzilli, L. G. Inorg. Chem. 1985, 24, 3908.
30. (i) Bresciani-Pahor, N.; Randaccio, L.; Zangrando, E.; Toscano, P. J. Inorg. Chim. Acta 1985, 96, 193.
31. (j) Marzilli, L. G.; Summers, M. F.; Bresciani-Pahor, N.; Zangrando, E.; Charland, J.-P.; Randaccio, L. J. Am. Chem. Soc. 1985, 107, 6880.
32. (k) Mealli, C.; Sabat, M.; Marzilli, L. G. J. Am. Chem. Soc. 1987, 109, 1593.
33. (a) Grate, J. H.; Schrauzer, G. N. J. Am. Chem. Soc. 1979, 101, 4601.
34. (b) Schrauzer, G. N.; Grate, J. H. J. Am. Chem. Soc. 1981, 103, 541.
35. Chemaly, S. M.; Pratt, J. M. J. Chem. Soc., Dalton Trans. 1980, 2274.
36. (a) Luschinsky-Drennan, C.; Huang, S.; Drummond, J. T.; Matthews, R. G.;Ludwig, M. L. Science 1994, 260, 1669-1674. (See also the introductory comments about this landmark paper: Stubbe, J. Science 1994, 1663-1664.)
37. (a) Luschinsky-Drennan, C.; Huang, S.; Drummond, J. T.; Matthews, R. G.;Ludwig, M. L. Science 1994, 260, 1669-1674. (See also the introductory comments about this landmark paper: Stubbe, J. Science 1994, 1663-1664.)
38. (b) Drennan, L. C.; Matthews, R. G.; Ludwig, M. L. Curr. Opin. Struct. Biol. 1994, 4, 919-929.
39. (c) Mancia, F.; Keep, N. H.; Nakagawa, A.; Leadlay, P. F.; McSweeney, S.; Rasmussen, B.; Böscke, P.; Dial, O.; Evans, P. R. Structure 1996, 4, 339. We thank Professor Leadlay for sharing this important development with us prior to publication.
40. (d) Ludwig, M. L.; Drenan, C. L.; Matthews, R. G. Structure 1996, 4, 505.
41. . atom-abstractor is present, see: Marsh, E. G. N. Biochemisty 1995, 34, 7542.
42. (a) Ishida, A.; Ichikawa, M.; Kobayashi, K.; Hitomi, T.; Kojima, S.; Toraya, T. J. Nutr. Sci. Vitaminol. 1993, 39, 115.
43. (b) Toraya, T.; Ishida, A. J. Biol. Chem. 1991, 266, 5430.
44. (c) Ishida, A.; Toraya, T. Biochemistry, 1993, 32, 1535.
45. IICbl with methylmalonyl-CoA.
46. IICbl with methylmalonyl-CoA.
47. (a) Hay, B. P.; Finke, R. G. J. Am. Chem. Soc. 1987, 109, 8012.
48. (b) For a 2D NMR study of AdoCbi+ see: Pagaro, T. G.; Yohannes, P. G.; Hay, B. P.; Scott, J. R.; Finke, R. G.; Marzilli, L. G. J. Am. Chem. Soc. 1989, 111, 1484.
49. (a) Pailes, W. H.; Hogenkamp, H. P. C. Biochemistry 1968, 7, 4160.
50. (b) Baldwin, D. A.; Betterson, E. A.; Chemaly, S. M.; Pratt, J. M. J. Chem. Soc., Dalton Trans. 1985, 1613.
51. (c) Brown, K. L.; Brooks, H. B. Inorg. Chem. 1991, 30, 3420.
52. (d) Brodie, J. D. Proc. Natl. Acad. Sci. U.S.A. 1969, 62, 461.
53. (e) Brown, K. L.; Satyanarayana, S. Inorg. Chim. Acta 1992, 201, 113-119.
54. + product complexes in this work.
55. (a) Brown K. L.; Gupta, B. D. Inorg. Chem. 1990, 29, 3854.
56. (b) Brown, K. L.; Hakimi, J. M. J. Am. Chem. Soc. 1986, 108, 496.
57. (c) Brown K. L.; Satyanarayana, S. Inorg. Chem. 1992, 31, 1366.
58. Thusius, D. J. Am. Chem. Soc. 1971, 93, 2629.
59. (a) Streuli, C. A. Anal. Chem. 1960, 32, 985.
60. (b) Henderson, W. A.; Streuli, C. A. J. Am. Chem. Soc. 1960, 82, 5791.
61. Ng, F. T. T.; Rempel, G. L.; Halpern, J. J. Am. Chem. Soc. 1982, 104, 621.
62. - binding to alkycobamides that is provided as part of the Supplementary Materials.
63. Garr, C. D.; Sirovatka, J. M.; Finke, R. G. Unpublished results and experiments in progress.
64. Simonov, A. M.; Pozharskii, A. E.; Marianovskii, V. M. Ind. J. Chem. 1967, 5, 81.
65. 20b-d
66. (b) Firth, R. A.; Hill, H. A. O.; Mann, B. E.; Pratt, J. M.; Thorp, R. G.; Williams, R. J. P. J. Chem. Soc. A 1968, 2419.
67. (c) Brown, K. L.; Peck-Siler, S. Inorg. Chem. 1988, 27, 3548.
68. eq studies).
69. (a) Drago, R. S. Physical Methods in Chemistry; W. B. Saunders: Philadelphia, PA 1977; p 90.
70. (b) Alelyunas, Y. A.; Fleming, P. F.; Finke, R. G.; Pagano, T. G.; Marzilli, L. G. J. Am. Chem. Soc. 1991, 113, 3781.
71. 27
72. Tolman, C. A. Chem. Rev. 1977, 77, 313.
73. assoc constants for phosphines are not reported)].
74. assoc constants for phosphines are not reported)].
75. (b) Firth, R A.; Hill, H. A. O.; Pratt, J. M.; Thorp, R. G.; Williams, R. J. P. J. Chem. Soc. A 1969, 381.
76. + studies provided in Table 3: adocobaloxime(solvent), adoCo(SALEN/SALOPH), and adoCo(tropocoronands).
77. + studies provided in Table 3: adocobaloxime(solvent), adoCo(SALEN/SALOPH), and adoCo(tropocoronands).
78. + studies provided in Table 3: adocobaloxime(solvent), adoCo(SALEN/SALOPH), and adoCo(tropocoronands).
79. + studies provided in Table 3: adocobaloxime(solvent), adoCo(SALEN/SALOPH), and adoCo(tropocoronands).
80. + studies provided in Table 3: adocobaloxime(solvent), adoCo(SALEN/SALOPH), and adoCo(tropocoronands).
81. + studies provided in Table 3: adocobaloxime(solvent), adoCo(SALEN/SALOPH), and adoCo(tropocoronands).
82. + studies provided in Table 3: adocobaloxime(solvent), adoCo(SALEN/SALOPH), and adoCo(tropocoronands).
83. + studies provided in Table 3: adocobaloxime(solvent), adoCo(SALEN/SALOPH), and adoCo(tropocoronands).
84. 26b-d (a) Brown K. L. J. Am. Chem. Soc. 1987, 109, 2277. (b) Hayward, G. C.; Hill, H. A. O.; Pratt, J. M.; Vanston, N. J.; Williams, R. J. P. J. Chem. Soc. 1965, 6485. (c) Dolphin, D. H.; Johnson, A. W.; Rodrigo, R. Ann. N. Y. Acad. Sci. 1964, 112, 590. (d) Broadie, J. D.; Poe, M. Biochemistry 1972, 11, 2534.
85. 26b-d (a) Brown K. L. J. Am. Chem. Soc. 1987, 109, 2277. (b) Hayward, G. C.; Hill, H. A. O.; Pratt, J. M.; Vanston, N. J.; Williams, R. J. P. J. Chem. Soc. 1965, 6485. (c) Dolphin, D. H.; Johnson, A. W.; Rodrigo, R. Ann. N. Y. Acad. Sci. 1964, 112, 590. (d) Broadie, J. D.; Poe, M. Biochemistry 1972, 11, 2534.
86. 26b-d (a) Brown K. L. J. Am. Chem. Soc. 1987, 109, 2277. (b) Hayward, G. C.; Hill, H. A. O.; Pratt, J. M.; Vanston, N. J.; Williams, R. J. P. J. Chem. Soc. 1965, 6485. (c) Dolphin, D. H.; Johnson, A. W.; Rodrigo, R. Ann. N. Y. Acad. Sci. 1964, 112, 590. (d) Broadie, J. D.; Poe, M. Biochemistry 1972, 11, 2534.
87. 26b-d (a) Brown K. L. J. Am. Chem. Soc. 1987, 109, 2277. (b) Hayward, G. C.; Hill, H. A. O.; Pratt, J. M.; Vanston, N. J.; Williams, R. J. P. J. Chem. Soc. 1965, 6485. (c) Dolphin, D. H.; Johnson, A. W.; Rodrigo, R. Ann. N. Y. Acad. Sci. 1964, 112, 590. (d) Broadie, J. D.; Poe, M. Biochemistry 1972, 11, 2534.
88. (a) Finke, R. G.; Hay, B. P. Inorg. Chem. 1984, 23, 3041.
89. (b) Hay, B. P.; Finke, R. G. Polyhedron 1988, 7, 1469.
90. (c) Hay, B. P.; Finke, R. G. J. Am. Chem. Soc. 1986, 108, 4820.
91. Brown, K. L.; Chernoff, D.; Keljo, D. J.; Kallen, R. G. J. Am. Chem. Soc. 1972, 94, 6697.
92. 2 or toluene with a series of p-subsituted and other axial bases, see: Murakami, Y.; Hisaeda, Y.; Kajihara, A. Bull. Chem. Soc. Jpn. 1983, 56, 3642.
93. 31a
94. 31a,b (a) Halpern, J. Bull. Chem. Soc. Jpn. 1988, 61, 13. (b) Wolowiec, S.; Balt, S.; De Bolster, M. W. G. Inorg. Chim. Acta 1991, 181, 131.
95. 31a,b (a) Halpern, J. Bull. Chem. Soc. Jpn. 1988, 61, 13. (b) Wolowiec, S.; Balt, S.; De Bolster, M. W. G. Inorg. Chim. Acta 1991, 181, 131.
96. Hogenkamp, H. P. C.; Bratt, G. T.; Kotchevar, A. T. Biochemistry 1987, 26, 4723.
97. 12 plus thiols and related topics.
98. (a) Frick, T.; Francia, M. D.; Wood, J. M. Biochim. Biophys. Acta 1976, 428, 808-818.
99. 33
100. Nome, F.; Fendler, J. H. J. Chem. Soc., Dalton Trans 1976, 1212.
101. Adler, N.; Medwick, T.; Poznanski, T. J. J. Am. Chem. Soc. 1966, 88, 5018.
102. (a) Brown, K. L.; Chernoff, D.; Keljo, D. J.; Kallen, R. G. J. Am. Chem. Soc. 1972, 94, 1894.
103. 2(pyridine) complex has been identified in the following work: Schrauzer, G. N.; Windgassen, R. J. J. Am. Chem. Soc. 1967, 89, 3607.
104. (a) Pellizer, G.; Tauszik, G. R.; Costa, G. J. Chem. Soc., Dalton Trans 1973, 317.
105. (b) Alexander, V. Inorg. Chim. Acta 1989, 163, 143.
106. 39b plus others (and references 3f, 6, 15, 18c therein).
107. 12; Dolphin, D., Ed., Wiley-Interscience: New York, 1982; Vol. 1, Chapter 3.
108. (c) See also: Glusker, J. P. Vitamins Hormones 1995, 50, 1-76.
109. (a) Lien, E. L.; Ellenbogen, L.; Law, P. Y.; Wood, J. M. Biochem. Biophys. Res. Commun. 1973, 55, 730.
110. (b) Lien, E. L.; Ellenbogen, L.; Law, P. Y.; Wood, J. M. J. Biol. Chem. 1974, 249, 890.
111. (c) Histidine has been identified as the axial ligand to cobalt in the p-cresoyl cobamide in the acetogenic bacterium Sporomusa ovata: Stupperich, E.; Eisinger, H., J.; Albracht, S. P. J. Eur. J. Biochem. 1990, 193, 105.
112. (a) Pratt, J. M. Inorg. Chim. Acta 1983, 79, 27.
113. 41a mention anything unusual about the spectra they see (or the 440 nm absorbance), even though two of the three studies were specifically concerned with the identification of enzyme-bound intermediates.
114. (c) Hollaway, M. R.; White, H. A.; Joblin, K. N.; Johnson, A. W.; Lappert, M. F.; Wallis, O. C. Eur. J. Biochem. 1978, 82, 143.
115. +, plus α-ribazole or α-ribazole-phosphate, binding to Intrinsic Factor: Andrews, E. R.; Pratt, J. M.; Brown, K. L. FEBS Lett. 1991, 281, 90.
116. 25
117. 12 model complexes simultaneously lengthen or shorten): De Ridder, D. J. A.; Zangrando, E.; Bürgi, H.-B. J. Mol. Struct. 1996, 374, 63-83.
118. (a) That is, a relatively long Co - N distance is apparently important in avoiding the the Co - C heterolysis that is expected from a shorter Co - N distance and its implied stronger σ-donation to cobalt.
119. (b) Dawkins, R. The Blind Watchmaker; Longman Scientific and Technical: Essex, England, 1986.
120. 12: (a) Eschenmosher, A. Angew. Chem. Int. Ed. 1988, 27, 5; Angew. Chem. 1988, 100, 5. (b) Brown, K. L. Inorg. Chem. 1986, 25, 3111 (see the statement on p 3113). (c) Brown, K. L.; Evans, D. R. Inorg. Chem. 1993, 32, 2544 (see the statement about the progressive strain in the nucleotide loop on p 2546).
121. 12: (a) Eschenmosher, A. Angew. Chem. Int. Ed. 1988, 27, 5; Angew. Chem. 1988, 100, 5. (b) Brown, K. L. Inorg. Chem. 1986, 25, 3111 (see the statement on p 3113). (c) Brown, K. L.; Evans, D. R. Inorg. Chem. 1993, 32, 2544 (see the statement about the progressive strain in the nucleotide loop on p 2546).
122. 12: (a) Eschenmosher, A. Angew. Chem. Int. Ed. 1988, 27, 5; Angew. Chem. 1988, 100, 5. (b) Brown, K. L. Inorg. Chem. 1986, 25, 3111 (see the statement on p 3113). (c) Brown, K. L.; Evans, D. R. Inorg. Chem. 1993, 32, 2544 (see the statement about the progressive strain in the nucleotide loop on p 2546).
123. 12: (a) Eschenmosher, A. Angew. Chem. Int. Ed. 1988, 27, 5; Angew. Chem. 1988, 100, 5. (b) Brown, K. L. Inorg. Chem. 1986, 25, 3111 (see the statement on p 3113). (c) Brown, K. L.; Evans, D. R. Inorg. Chem. 1993, 32, 2544 (see the statement about the progressive strain in the nucleotide loop on p 2546).
124. (a) Foster, M. A.; Hill, H. A. O.; Williams, R. J. P. Biochem. Soc. Symp. 1970, 31, 187.
125. (b) Rudiger, H. Eur. J. Biochem. 1971, 21, 264.
126. (a) Kato, T.; Shimizu, S.; Fukui, S. J. Vitaminol. (Kyoto) 1964, 10, 89.
127. (b) Toraya, T.; Ohashi, K.; Ueno, H.; Fukui, S. Bioinorg. Chem. 1975, 4, 245.
128. (c) Toraya, T.; Fukui, S. Adv. Chem. Ser. 1980, 191, 139.
129. 48
130. 50
131. 47b were performed.
132. 10a
133. (c) For related work see: Brown, K. L.; Wu, G.-Z. Organometallics 1993, 12, 496.
134. 11a (see p 8017 and ref 37).
135. + is reported therein to be a "very weak inhibitor" for ribonucleotide reductase. The authors concluded (p 182) that "the lower axial ligand (and, we would now add, nucleotide loop) may play an important role in binding the coenzyme ... to the active site.
136. (a) Padmakumar, R.; Taoka, S.; Padmakumar, R.; Banerjee, R. J. Am. Chem. Soc. 1995, 117, 7033.
137. 12 binding, methionine synthase. But, overall and by themselves, these initial studies do not unequivocally demonstrate that the 5,6-dimethylbenzimidazole base-off form of AdoCbl is involved in the catalytic cycle of MMCoA mutase. Note added in proof: Professor Banerjee kindly informs us that they now have submitted for publication data indicating that the protein-derived nitrogen ligand is bonded to cobalt in a radical-pair directly observed by EPR.
138. +·MMCoA holoenzyme). We thank Professor Banerjee for sharing this unpublished information.
139. +·MMCoA holoenzyme). We thank Professor Banerjee for sharing this unpublished information.
140. Hamilton, J. A.; Blakley, R. L.; Looney, F. D.; Winfield, M. E. Biochem. Biophys. Acta 1969, 177, 374.
141. 18
142. 12 : Dolphin, D., Ed.; Wiley-Interscience: New York. 1982; Vol. 2, Chapter 13.
143. - transfer step from the Co(II) cofactor to the substrate radical is actually occurring.
144. + is incorporated into the product. However, definitive evidence for kinetically preferred rearrangement at the carbanion stage must await further mechanistic study.
145. (c) Wollowitz, S.;Halpern, J. J. Am. Chem. Soc. 1988, 110, 3112-3120.
146. (d) He, M; Dowd, P. J. Am. Chem. Soc. 1996, 118, 711. There is an unnecessary assumption in this paper: the possible cyclopropyl ring-opened rearrangement product, around which the logic in this paper centers (i.e., the
147. For lead references, see: Toraya, T.; Krodel, E.; Mildvan, A. S.; Abeles, R. H. Biochemistry 1979, 18, 417 and references therein.
148. IICbl). (a) Brown, K. L.; Hakimi, J. M.; Nuss, D. M.; Montejano, Y. D.; Jacobsen, D. W. Inorg. Chem. 1984, 23, 1463. (b) Brown, K. L.; Zou, X.; Evans, D. R. Inorg, Chem. 1994, 33, 5713. (c) Brown, K. L.; Cheng, S.; Marques, H. M. Inorg. Chem. 1995, 34, 3038. (d) Brown, K. L.; Evans, D. R.; Cheng, S.; Jacobsen, D. W. Inorg. Chem. 1996, 35, 217. In this work, neopentylcobalamin derivatives are found to be stabilized by a ΔG‡ (25 °C) of 2.8 ± 1.0 kcal/mol to Co - C homolysis upon complexation to haptocorrin, a net effect that is 67 (±38)% enthalpic (the expected radical-cage effect by the haptocorrin) and 33 (±10)% entropic at 25 °C.
149. IICbl). (a) Brown, K. L.; Hakimi, J. M.; Nuss, D. M.; Montejano, Y. D.; Jacobsen, D. W. Inorg. Chem. 1984, 23, 1463. (b) Brown, K. L.; Zou, X.; Evans, D. R. Inorg, Chem. 1994, 33, 5713. (c) Brown, K. L.; Cheng, S.; Marques, H. M. Inorg. Chem. 1995, 34, 3038. (d) Brown, K. L.; Evans, D. R.; Cheng, S.; Jacobsen, D. W. Inorg. Chem. 1996, 35, 217. In this work, neopentylcobalamin derivatives are found to be stabilized by a ΔG‡ (25 °C) of 2.8 ± 1.0 kcal/mol to Co - C homolysis upon complexation to haptocorrin, a net effect that is 67 (±38)% enthalpic (the expected radical-cage effect by the haptocorrin) and 33 (±10)% entropic at 25 °C.
150. IICbl). (a) Brown, K. L.; Hakimi, J. M.; Nuss, D. M.; Montejano, Y. D.; Jacobsen, D. W. Inorg. Chem. 1984, 23, 1463. (b) Brown, K. L.; Zou, X.; Evans, D. R. Inorg, Chem. 1994, 33, 5713. (c) Brown, K. L.; Cheng, S.; Marques, H. M. Inorg. Chem. 1995, 34, 3038. (d) Brown, K. L.; Evans, D. R.; Cheng, S.; Jacobsen, D. W. Inorg. Chem. 1996, 35, 217. In this work, neopentylcobalamin derivatives are found to be stabilized by a ΔG‡ (25 °C) of 2.8 ± 1.0 kcal/mol to Co - C homolysis upon complexation to haptocorrin, a net effect that is 67 (±38)% enthalpic (the expected radical-cage effect by the haptocorrin) and 33 (±10)% entropic at 25 °C.
151. IICbl). (a) Brown, K. L.; Hakimi, J. M.; Nuss, D. M.; Montejano, Y. D.; Jacobsen, D. W. Inorg. Chem. 1984, 23, 1463. (b) Brown, K. L.; Zou, X.; Evans, D. R. Inorg, Chem. 1994, 33, 5713. (c) Brown, K. L.; Cheng, S.; Marques, H. M. Inorg. Chem. 1995, 34, 3038. (d) Brown, K. L.; Evans, D. R.; Cheng, S.; Jacobsen, D. W. Inorg. Chem. 1996, 35, 217. In this work, neopentylcobalamin derivatives are found to be stabilized by a ΔG‡ (25 °C) of 2.8 ± 1.0 kcal/mol to Co - C homolysis upon complexation to haptocorrin, a net effect that is 67 (±38)% enthalpic (the expected radical-cage effect by the haptocorrin) and 33 (±10)% entropic at 25 °C.
152. Finke, R. C.; Martin, B. M. J. Inorg. Biochem. 1990, 40, 19.
153. Garr, C. D.; Finke, R. G. Inorg. Chem. 1993, 32, 4414.
154. (a) Martin, B. D.; Finke, R. G. J. Am. Chem. Soc. 1990, 112, 2419.
155. (b) Martin, B. D.; Finke, R. G. J. Am. Chem. Soc. 1992, 114, 585.
156. 1la
157. binding = -18 eu, see: Marchaj, A.; Jacobsen, D. W.; Savon, S. R.; Brown, K. L. J. Am. Chem. Soc. 1995, 117, 11640. The observation of much smaller binding constants for the AdoCbl-dependent enzymes is very strong evidence for the labilization of AdoCbl's Co - C bond via the expression of a considerable amount of intrinsic binding energy toward catalysis (e.g., tow:ard Co - C lengthening and Co - C - C angular distortion).
158. Jones, C. C.; Sinnott, M. L.; Souchard, I. J. L. J. Chem. Soc. Perkin Trans. 2 1977, 1191.
159. If this picture is correct, then AdoCbl enzymes emerge as prototype examples of "enthalpy machines", that is highly entropicaily preorganized from the reference point of free amino acids (i.e., having lost considerable translational and other entropy), hut in turn being able to perform considerable enthalpic work along the Co - C homolysis reaction coordinate.
160. (a) Eyring, H.; Lumry, R.; Spikes. J. D. In A Symposium on "The Mechanism of Enzyme Action": McElroy, W. D., Glass, B., Eds., Johns Hopkins Press: Baltimore, MD, 1954; pp 123-140.
161. 64c Note that a comparison, by X-ray crystallography or other structural methods, of the structures of the cofactor and enzyme alone to the structure of the cofactor-enzyme complex, will in principle unequivocally distinguish these different Co - C activation mechanisms as defined above.
162. (c) Williams, R. J. P. Eur. J. Biochem. 1995, 234, 363-381.