Fifty years of X-ray crystallography of vitamin B12 and its derivatives

South African Journal of Science

Volumn 100, Issue 7-8, 2004, Pages 368-380

  Perry, Christopher B ^a   Marques, Helder M ^a  

^a UNIVERSITY OF THE WITWATERSRAND   (South Africa)

Author keywords

[No Author keywords available]

Indexed keywords

ANEMIA;

ANIMALIA;

EID: 24944458544     PISSN: 00382353     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (134)

1. 12. Academic Press, London.
2. 12. Science 107, 396-397.
3. Smith E.L. (1948). Presence of cobalt in the antipernicious anemia factor. Nature 162, 144-145.
4. Smith E.L. and Parker L.F. (1948). The antipernicious anaemia factor. Proc. Biochem. Soc. 43, viii.
5. 12 by acid hydrolysis. J. Pharm. Pharmacol. 1, 287-291.
6. 12. J. Pharm. Pharmacol. 1, 950-956.
7. 12, J. Pharm. Pharmacol. 1, 957-970.
8. 12 group. Chem. Rev. 63, 573-605.
9. Dodson G., Glusker J.P. and Syre D. (eds) (1981). Structural Studies on Molecules of Biological Interest - A volume in honour of Dorothy Hodgkin. Clarendon Press, Oxford.
10. Adams M.J., Blundell T.L., Dodson E.J., Dodson G.G., Vijayan M., Baker E.N., Harding M.M., Hodgkin D.C., Rimmer R. and Sheet S. (1969). Structure of rhombohedral 2 zinc insulin crystals. Nature 224, 491-496.
11. Baker E.N., Blundell T.L., Cutfield J.F., Cutfield S.M., Dodson E.J., Dodson E.G., Hodgkin D.M.C., Hubbard E.H., Isaacs N.W., Reynolds C.D., Sakabe K., Sakabe N. and Vijayan N.M. (1988). The structure of 2Zn pig insulin at 1.5 A° resolution. Phil. Trans. R. Soc. Lond. B 319, 369-156.
12. Hodgkin D.C., Porter M.W. and Spiller R.C. (1950). Crystalline anti-pernicious anaemia factor from liver: crystallographic measurements on the anti-pernicious anaemia factor. Proc. R. Soc. Lond. B 136, 609-613.
13. 12. Proc. R. Soc. Lond. A 242, 228-163.
14. 12. Proc. R. Soc. Lond. A 266, 494-517.
15. 12 grown from and immersed in water. Proc. R. Soc. Lond. A 278, 1-26.
16. Hodgkin D.C. (1965). The structure of the corrin nucleus from X-ray analysis. Proc. R. Soc. Lond. A 288, 294-305.
17. Beck W.S., Flavin M. and Ochoa S. (1957). Metabolism of propionic acid in animal tissues. III. Formation of succinate J. Biol. Chem. 229, 997-1010.
18. 12-Poteins, eds B. Krautler, D. Arigoni and B.J. Golding, pp. 461-475. Wiley-VCH, Weinheim.
19. Wardlaw G.M. and Insel P.M. (1993). Perspectives in Nutrition, 2nd edn. Mosby, St Louis, Missouri.
20. 12: biochemical derivation of cobyrinic add from uroporphyrinogen III, studies with the corresponding c methyl hepta-carboxylic porphyrinogen, and proof of seven intact methyl transfers. J. Chem. Soc. Perkin I, 166-178.
21. 12 coenzyme. Proc. R. Soc. Lond. A 303, 45-84.
22. Lenhert P.G. and Hodgkin D.C. (1961). Structure of the 5,6-dimethyl-benzimidazolylcobamide coenzyme. Nature 192, 937-938.
23. 12 coenzyme: methylcobalamin studies by x-ray and nmr methods. J. Am. Chem. Soc. 107, 1729-1738.
24. 12, ed. R. Banerjee, pp. 681-706. Wiley, New York.
25. 12, ed. R. Banerjee, pp. 633-653. Wiley, New York.
26. 12 (cobalamin)-dependent enzymes. Essays Biochem. 34, 139-154.
27. 12, ed. R. Banerjee, pp. 731-755. Wiley, New York.
28. Hay B.P. and Finke R.G. (1986). Thermolysis of the cobalt-carbon bond of adenosylcobalamin. 2. Products, kinetics and cobalt-carbon bond dissociation energy in aqueous solution. J. Am. Chem. Soc. 108, 4820-4829.
29. 12- dependent ribonucleotide reductase from Lactobacillus leichmannii. J. Am. Chem. Soc. 120, 9466-9474.
30. 12-dependent enzymes. Chem. Soc. Rev. 329-337.
31. 12 is coordinated by histidine and not dimethylbenzimidazole on methylamolonyl-CoA mutase. J. Am. Chem. Soc. 117, 7033-7034.
32. 12-dependent glutamate mutase from Clostridium cochlearium. FEBS Lett. 369, 252-254.
33. 12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 Å resolution. Structure 4, 339-350.
34. Thomä N.H., Meier T.W., Evans P.R. and Leadley P.F. (1998). Stabilization of radical intermediates by an active-site tyrosine residue in methylmalonyl-CoA mutase. Biochemistry 37, 14386.
35. Mancia F. and Evans P.R. (1998). Conformational changes on substrate binding to methylmalonyl CoA moutase and new insights into the free radical mechanism. Structure 6, 711.
36. 12-dependent enzyme provides new mechanistic insights. Structure 891-899.
37. 12-binding domains of methionine synthase. Science 266, 1669-1674.
38. 12-dependent enzymes. Annu. Rev. Biochem. 66, 269-313.
39. Yamanishi M., Yamada S., Muguruma H., Murakami Y., Tobimatsu T., Ishida A., Yamauchi J. and Toraya T. (1998). Evidence for axial coordination of 5,6-dimethyibenzimidazole to the cobalt atom of adenosylcobalamin bound to dial dehydratase. Biochemistry 37, 4799-4803.
40. 12 in the base-on mode: ESR investigations on cob(II)alamin. Angew. Chem., Int. Ed. 37(5), 625-627.
41. Lawrence C.C., Gerfen G.J., Samano V., Nitsche R., Robins M.J., Retey J. and Stubbe J. (1999). Binding of cob(II)alamin to the adenosylcobalamin- dependent ribonucleotide reductase fmm Lactobacillus leichmannii. Identification of dimethylbenzimidazole as the axial ligand. J. Biol. Chem. 274, 7039-7042.
42. Tobimatsu T., Azuma M., Matsubara H., Takatovi H., Niida T., Nishimoto K., Satoh H., Hayashi R. and Toraya T. (1996). Cloning, sequencing and high level expression of the genes encoding adenosylcobalamin-dependent glycerol dehydrase of Klebsiella pneumoniae. J. Biol. Chem. 271, 22352-22357.
43. Tobimatsu T., Hara T., Sakaguchi M., Kishimoto Y., Wada Y., Sakai M. and Toraya T. (1995). Molecular cloning, sequencing and expression of the genes encoding adenosylcobalamin-dependent diol dehydratase of Klebsiella oxytoca. J. Biol. Chem. 270, 7142-7148.
44. Faust L.R., Connor J.A., Roof D.M., Hoch J.A. and Babior B.M. (1990). Cloning, sequencing, and expression of the genes encoding the adenosylcobalamin-dependent ethanolamine ammonia-lyase of Salmonella typhimurium. J. Biol. Chem. 265, 12461-12466.
45. Booker S.B. and Stubbe J. (1993). Cloning, sequencing and expression of the adenosylcobalamin-dependent ribonucleotide reductase from Lactobacillus leichmanii. Proc. Natl Acad. Sci. USA 90, 8352-8356.
46. 12 binding and the direct participation of potassium ion in enzyme catalysis: X-ray structure of diol dehydratase. Structure 7, 997-1008.
47. Allen F.H., v. 5.22, Oct. 2001, 2002.
48. 2, SCN and SeCN to Co in cobalamins. Acta Cryst., Sec. B, 51-59.
49. 12 coenzyme. Acta Cryst. B43, 280-295.
50. 12. Proc. R. Soc. Lond. A 251, 306-352.
51. 12-Proteins, eds B. Krautler, D. Arigoni and B.J. Golding, pp. 335-347. Wiley-VCH, Weinheim.
52. 12 chemistry: the crystal and molecular structure of cob(II)alamin. J. Am. Chem. Soc. 111, 8936-8938.
53. 12: synthesis and solution spectroscopic and crystal structure analysis of Co-β- cyanoimidazolylcobamide. Inorg. Chem. 33, 4128-4139.
54. Fasching M., Schmidt W., Kräutler B., Stupperich E., Schmidt A. and Kratky C. (2000). Co-a-(1H-imidazolyl)-Co-β-methylcob(III)amide: model for protein-bound corrinoid cofactors. Helv. Chim. Acta 83, 2295-2316.
55. Wagner T., Afshar C.E., Carrell H.L. and Glusker J.P. (1999). Difluoromethyl-cobalamin: structural aspects of an old tree with a new branch. Inorg. Chem. 38, 1785-1794.
56. 12 analog. Inorg. Chim. Acta 267, 305-308.
57. 3-adenine. J. Am. Chem. Soc. 113, 531-542.
58. Alcock N.W., Dixon R.M. and Golding B.T. (1985). The crystal structure of (R)-and (S)-dihydroxypropylcobalamin: comparison with the structure of adenosylcobalamin. J. Chem. Soc., Chem. Commun. 603-605.
59. Randaccio L., Geremia S., Nardin G., Slouf M. and Srnova I. (1999). Crystal chemistry of cobalamins. Structural characterization of the Co-S bond in cobalamins. Inorg. Chem. 38, 4087-4092.
60. 12 systems - a density functional study. Eur. J. Inorg. Chem. 93-103.
61. Suto R.K., Brasch N.E., Anderson O.P. and Finke R.G. (2001). Synthesis, characterization, solution stability and x-ray crystal structure of the thiolatocobalamin gamma-glutamylcysteinylcobalamin, a dipeptide analogue of glutathionylcobalamin: insights into the enhanced Co-S bond stability of the natural product glutathionylcobalamin. Inorg. Chem. 40, 2686-2692.
62. 12-Proteins, eds B. Krautler, D. Arigoni B.J. and Golding, pp. 133-155. Wiley-VCH, Weinheim.
63. Pezacka E.H. (1993). Identification and characterization of two enzymes involved in the intracellular metabolism of cobalamin. Cyanocobalamin beta-ligand transferase and microsomal cob(III)alamin reductase. Biochim. Biophys. Acta 1157, 167-177.
64. Pezacka E.H., Green R. and Jacobsen D.W. (1990). Glutathionylcobalamin as an intermediate in the formation of cobalamin coenzymes. Biochem. Biophys. Res. Commun. 169, 443-150.
65. Randaccio L., Furlan M., Geremia S. and Iouf M. (1998). Preparation and x-ray analysis of azido- and chlorocobalamin containing LiCl: a structural model for the interaction of the corrin ring with ionic species. Inorg. Chem. 37, 5390-5393.
66. 12: high resolution solid-state structure of aquocobalamin perchlorate and structural analysis of the aquocobalamin ion in solution. J. Am. Chem. Soc. 117, 4654-4670.
67. 12 derivative cob(II)alamin. J. Am. Chem. Soc. 113, 4523-4530.
68. Marques H.M., Marsh J.H., Mellor J.R. and Munro O.Q. (1990). The coordination of imidazole and its derivatives by aquocobalamin. Inorg. Chim. Acta 170, 259-269.
69. Davies M.T., Mamalis P., Petrow V. and Sturgeon B. (1951). The chemistry of anti-pernicious anemia factors. Part VIII. The basicity of some benzimidazoles and benzimidazole glycosides. J. Pharm. Pharmacol. 3, 420-430.
70. Kamiya K. and Kennard O. (1982). The X-ray structure analysis of anhydrous heptamehyl dicyanocobyrinate (cobester). J. Chem. Soc., Perkin Trans. 1, 2279-2288.
71. 12. Part 28. Crystal structure of dicyanocobyrinic acid heptamethyl ester and its interaction with alcohols: the effect of hydrogen bonding to co-ordinated cyanide. J. Chem. Soc., Dalton Trans. 1349-1357.
72. Schlingmann G., Dresow B., Koppenhagen V.B., Becker W. and Sheldrick W.S. (1980). The crystal structure of 6-amino-dicyano-5,6-dihydrocobyrinic- pentamethylester-a-amide-c-lactam hemihydrate. Angew. Chem. Int. Ed. Engl. 19, 321-322.
73. Grüning B., Holze G., Jenny T., Nesvadba P. and Gossauer A. (1985). Structure and reactivity of xanthocorrins. Influence of the c-acetic acid chain on the course of the hydroxylation of the corrin chromophore by oxygen in the presence of ascorbic acid. Helv. Chim. Acta 68, 1754-1770.
74. Fischli A. and Daly J.J. (1980). Cob(I)alamin and heptamethyl cob(I)yrinate during the reduction of a,b-unsaturated carbonyl derivatives. Helv. Chim. Acta 63, 1628-1643.
75. Holze G., Jenny T, Gossauer A., Ernst L., Keller W. and Kratky C. (1981). Structure and reactivity of xanthocorrinoids. Formation of trans-diol derivatives of 5,6-dihydrocobyrinic acid from xanthocorrinoids under acidic conditions. Helv. Chim. Acta 74, 1287-1295.
76. Kräutler B., Caderas C., Konrat R., Puchberger M. and Kratky C. (1995). Lipophilic functionalized cobyrinic acid derivatives. Cobester a-monoacids. Helv. Chim. Acta 78, 581-599.
77. Battersby A.R., Grgurina I., Raithby P.R., Egert E., Harms K. and Sheldrick G.M. (1989). Structure of dicayno-15-norcobyrinic acid heptamethyl ester. Acta Cryst. C45, 1589-1593.
78. 12: preparation and X-ray crystal structure. J. Chem. Soc., Chem. Commun. 1678-1680.
79. Pett V.B., Liebman M.N., Murray-Rust P., Prasad K. and Glusker J.P. (1987). Conformational variability of corrins. Some methods of analysis. J. Am. Chem. Soc. 109, 3207-3215.
80. Brown K.L., Cheng S., Zubkowski J.D. and Valente E.J. (1997). Side chain entropy and activation of organocobalamins for carbon-cobalt bond homolysis: synthesis, characterization, and thermolysis of the neopentyl derivative of a unique cobalamin analog lacking a c side chain. Inorg. Chem. 36, 1772-1781.
81. 12. J. Chem. Soc., Perkin Trans. 2, 605-614.
82. 12, vol. 1, ed. D. Dolphin, pp. 23-107. Wiley Interscience, New York.
83. Brown K.L., Evans D.R., Zubkowski J.D. and Valente E.J. (1996). Heteronuclear NMR studies of cobalt corrinoids. 18. Correlation of structure and magnetic resonance parameters in base-on cobalamins. Inorg. Chem. 35, 415-423.
84. Brown K.L., Cheng S., Zubkowski J.D. and Valente E.J. (1996). Synthesis and characterisation of a novel green cobalt corrinoid. Inorg. Chem. 35, 3442-3446.
85. 15N NMR. Polyhedron 14, 1621-1639.
86. 12 coenzymes in the reaction catalyzed by dioldehydrase. Biochemistry 18, 417-426.
87. Toraya T., Shirakashi T., Fukui S. and Hogenkamp H.P.C. (1975). Coenzyme action of adenosyl-13-epicobalamin in the diol dehydrase system. Biochemistry 14, 3949-3952.
88. 12 and its coenzymes: structures and reactivities. In Molecular Structure and Energetics, vol. X, eds J.F. Liebman and A. Greenberg, pp. 1-58. VCH, Weinheim.
89. 12, vol. 1, ed. D. Dolphin, pp. 23-107. Wiley-Interscience, New York.
90. Randaccio L., Furlan M., Geremia S., Iouf M., Srnova I. and Toffoli D. (2000). Similarities and differences between cobalamins and cobaloximes. Accurate structural determination of methylcobalamin and of LiCl- and KCl-containing cyanocobalamins by synchotron radiation. Inorg. Chem. 39, 3403-3413.
91. 12 coenzyme at 15K: structure analysis and comparison with the structure at 279K. Acta Cryst. B49, 79-89.
92. 12 coenzyme at 15K: solvent structure. Acta Cryst. B50, 566-578.
93. 12 coenzyme crystals. I. Analysis of the neutron and x-ray solvent densities. Biophys. J. 50, 947-965.
94. 12, ed. R. Banerjee, pp. 73-112. Wiley, New York.
95. 12-dependent enzymes. J. Mol. Struct. 374, 63-83.
96. Andruniow T., Zgierski M.Z. and Kozlowski P.M. (2000). SQM force field for cobalt corrinoids. Chem. Phys. Lett. 331, 502-508.
97. Jensen K.P. and Ryde U. (2002). The axial N-base has minor influence on Co-C bond cleavage in cobalamins. J. Mol. Str. Theochem. 585, 239-255.
98. Brown K.L., Cheng S., Zou X., Zubkowski J.D., Valente E.J., Knapton L. and Marques H.M. (1997). Cis effects in the cobalt corrins. 1. Crystal structures of 10-chloroaquacobalamin perchlorate, 10-chlorocyanocobalamin and 10-chloromethylcobalamin. Inorg. Chem. 36, 3666-3675.
99. 12. Proc. Natl Acad. Sci. USA 44, 1093-1097.
100. Guest J.R., Friedman S., Woods D.D. and Smith E.L. (1962). A methyl analogue of cobamide coenzyme in relation to methionine synthesis by bacteria. Nature 193, 349-342.
101. 12 cofactors: the proteins make a difference. Structure 4, 505-512.
102. 12-dependent enzymes. Curr. Opin. Struct. Biol. 4, 919-929.
103. Banerjee R. (1997). The ying-yang of cobalamin chemistry. Chem. Biol. 4, 175-186.
104. 12-dependent isomerase enzymes: how the protein controls the active site. Chem. Soc. Rev. 14, 161-170.
105. Hay B.P. and Finke R.G. (1987). Thermolysis of the cobalt-carbon bond in adenosylcorrins. 3. Quantification of the axial base effect in adenosylcobalamin by the synthesis and thermolysis of axial base-free adenosylcobinamide. Insights into the energetics of enzyme-assisted cobalt-carbon bond homolysis. J. Am. Chem. Soc. 109, 8012-8018.
106. 12-dependent diol dehydratase. Chem. Record 2, 352-366.
107. 12-Proteins, vol. eds B. Krautler, D. Arigoni and B.J. Golding, pp. 383-402. Wiley-VCH, Weinheim.
108. 12 dependent rearrangements. Science 227, 869-875.
109. Williams R.J.P. (1995). Energised (entatic) states of groups and of secondary structures in proteins and metalloproteins. Eur. J. Biochem. 234, 363-381.
110. Toraya T. and Ishida A. (1988). Acceleration of cleavage of the carbon-cobalt bond of sterically hindered alkykobalamins by binding to apoprotein of diol dehydrase. Biochemistry 27, 7677-7681.
111. 12 chemistry and its use to probe the plausibility of an axial-base-induced, ground-state. Inorg. Chim. Acta 300-302, 545-555.
112. 12. J. Am. Chem. Soc. 105, 6259-6263.
113. 12. J. Inorg. Biochem. 83, 121-132.
114. 12-binding subunit of glutamate mutase from Clostridium tetanomorphum. Structure 6, 1021-1033.
115. 12-dependent enzymes glutamate mutase and 2-methyleneglutarate mutase. J. Am. Chem. Soc. 121, 11780-11789.
116. 12, ed. R. Banerjee, pp. 289-313. Wiley, New York.
117. Marques H.M., Ngoma B., Egan T.J. and Brown K.L. (2001). Parameters for the AMBER force field for the molecular mechanics modeling of the cobalt corrinoids. J. Mol. Str. 561, 71-91.
118. 12-Proteins, eds B. Krautier, D Arigoni, and B.T. Golding, pp. v-vi. Wiley-VCH, Weinheim.
119. 12-dependent enzyme glutamate mutase. Angew. Chem., Int. Ed. Eng. 40, 3377.
120. 12, vol. ed. R. Banerjee, pp. 707-729. Wiley Interscience New York.
121. 12-5′-phosphate. Proc. R. Soc. Lond. A 318, 143-167.
122. 12 analogue. Z. Naturforsch. C 36, 506.
123. Moore F.H., O'Connor B.H., Willis B.T.M. and Hodgkin D.C. (1984). X-ray and neutron diffraction studies of the crystal and molecular structure of the predominant monocarboxylic acid obtained by mild acid hydrolysis of cyanocobalamin. III. Neutron diffraction studies of wet crystals. Proc. Indian Acad. Sci., Chem. Sci. 93, 235.
124. Nockolds C.E. and Ramaseshan S. (1984). X-ray and neutron diffraction studies of the crystal and molecular structure of the predominant monocarboxylic acid obtained by mild acid hydrolysis of cyanocobalamin. I. X-ray diffraction studies of air-dried crystals. Proc. Indian Acad. Sci., Chem. Sci. 93, 197.
125. Waters J.M. and Waters T.N.M. (1984). X-ray and neutron diffraction studies of the crystal and molecular structure of the predominant monocarboxylic acid obtained by mild acid hydrolysis of cyanocobalamin. II. X-ray diffraction studies of wet crystals. Proc. Indian Acad Sci., Chem. Sci. 93, 219-234.
126. 12 dimers. Angew. Chem. Int. Ed. Engl. 34, 84-86.
127. 12. IX. The crystal structure of cobyric acid, Factor V Ia. Proc. R. Soc. Lond. A 323, 455-487.
128. 12. Structure 4, 1263-1275.
129. Mancia F. and Evans P.R. (1999). Crystal structure of substrate complexes of methylmalonyl-CoA mutase. Biochemistry 38, 7999.
130. Thoma N.H., Evans P.R. and Leadley P.F. (2000). Protection of radical intermediates at the active site of adenosylcobalamin-dependent methylmalonyl-CoA mutase. Biochemistry 39, 9213.
131. 12-dependent methionine synthase. Nature Struct. Biol. 9, 53.
132. 12-dependent glycerol dehydratase in complex with cobalamin and propane-1,2-diol. Eur. J. Biochem. 269, 4484-4494.
133. 12. J. Mol. Biol. 309, 777.
134. 12-binding subunit of glutamate mutase from Clostridium tetanomorphum. Eur. J. Chem. Biol. 2, 643.