An artificial redox coenzyme based on a triazine dye template

Enzyme and Microbial Technology

Volumn 18, Issue 8, 1996, Pages 570-580

  Burton, Steven J ^a,b   Stead, C Vivian ^a,c   Ansell, Richard J ^a,d   Lowe, Christopher R ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b Affinity Chromatography Ltd   (United Kingdom)

^c Dyestuffs Consultancy Services   (United Kingdom)

^d LUND UNIVERSITY   (Sweden)

Author keywords

Biomimetic coenzyme; Coenzyme analog; Horse liver alcohol dehydrogenase; Triazine dyes

Indexed keywords

BIOSYNTHESIS; CATALYSIS; DYES; GAS CHROMATOGRAPHY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; PH; REDOX REACTIONS; REDUCTION;

ACETALDEHYDE; BIOMIMETIC ENZYME; COENZYME ANALOG; HORSE LIVER ALCOHOL DEHYDROGENASE; TRIAZINE DYE TEMPLATE;

COENZYMES;

ACETALDEHYDE; ALCOHOL; ALCOHOL DEHYDROGENASE; CIBACRON BLUE F3GA; NICOTINAMIDE ADENINE DINUCLEOTIDE; SODIUM BOROHYDRIDE; TRIAZINE;

ABSORPTION SPECTROSCOPY; ARTICLE; COENZYME; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; GAS CHROMATOGRAPHY; OXIDATION REDUCTION REACTION; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; THIN LAYER CHROMATOGRAPHY;

EQUUS CABALLUS;

EID: 0030175442     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/0141-0229(96)00136-6     Document Type: Article

References (51)

1. + binding domain in proteins. Acc. Chem. Res. 1977, 10, 92-98
2. Subramanian, S. Dye-ligand affinity chromatography: The interaction of Cibacron blue F3G-A with proteins and enzymes. Crit. Rev. Biochem. 1984, 16, 169-205
3. + with sodium borohydride - a correction and extension. J. Am. Chem. Soc. 1953, 75, 5428-5430
4. Jones, J. B. Enzymes in organic synthesis. Tetrahedron 1986, 42, 3351-3403
5. Hummel, W. and Kula, M. R. Dehydrogenases for the synthesis of chiral compounds. Eur. J. Biochem. 1989, 184, 1-13
6. Turner, N. J. Recent advances in the use of enzyme-catalysed reactions in organic synthesis. Natural Prod. Rep. 1994, 10, 1-15
7. Kula, M.-R. Enzyme catalysed reductions of carbonyl groups. In: Proceedings of the Symposium Chiral Europe. Spring Innovations Ltd., Stockport, UK, 1994, 27-33
8. Wong, C.-H. and Whitesides, G. M. Enzymes in Synthetic Organic Chemistry. Pergamon Press, Oxford, UK, 1994
9. Negelein, E. and Haas, E. Über die Wirkungsweise des Zwischenferments. Biochemica Zeitschrift 1935, 282, 206-214
10. Greengard, P. Determination of intermediary metabolites by enzyme fluorimetry. Nature 1956, 178, 632-634
11. Gotoh, M. and Karube, I. Ethanol biosensor using immobilised coenzyme. Anal. Lett. 1994, 27, 273-284
12. May, S.W. and Padgette, R. Oxidoreductase enzymes in biotechnology - current status and future potential. Biotechnology 1983, 1, 677-685
13. Lowe, C. R. The application of coenzyme-dependent enzymes in biotechnology. Phil. Trans. R. Soc. Lond. B 1983, 300, 335-353
14. Falch, E. A. Industrial enzymes - developments in production and application. Biotechnol. Adv. 1991, 9, 643-658
15. Hodgson, J. The changing bulk biocatalyst market. Biotechnology 1994, 12, 789-791
16. Chenault, H. K. and Whitesides, G. M. Regeneration of nicotinamide cofactors for use in organic syntheses. Appl. Biochem. Biotechnol. 1987, 14, 147-197
17. Wichmann, R., Wandrey, C., Bückmann, A. F. and Kula, M.-R. Continuous enzymatic transformation in an enzyme membrane reactor with simultaneous NAD(H) regeneration. Biotechnol. Bioeng. 1981, 23, 2789-2802
18. Kragl, U., Vasicracki, D. and Wandrey, C. Continuous processes with soluble enzymes. Ind. J. Chem. Sect. B. 1993, 32, 103-117
19. Anderson, B. M. Analogues of pyridine nucleotide coenzymes. In: The Pyridine Nucleotide Coenzymes (Everse, J., Anderson, B. M. and You, K. S., eds.). Academic Press, New York, 1982, 91-133
20. Sicsic, S., Durand, P., Langrene, S. and LeGoffic, F. A new approach for using cofactor dependent enzymes: Example of HLADH. FEBS Lett. 1984, 176, 321-324
21. + coenzyme. Eur. J. Biochem. 1986, 155, 403-407
22. Kazlauskas, R. J. Changing coenzymes improves oxidations catalysed by HLADH. J. Org. Chem. 1988, 53, 4633-4635
23. + analogue. Anal. Biochem. 1990, 186, 229-232
24. Burton, S. J. and McLoughlin, S. B. Design and applications of biomimetic anthraquinone dyes 1. Synthesis and characterisation of terminal ring isomers of C.I. Reactive blue 2. J. Chromatogr. 1988, 435, 127-137
25. Burton, S. J., Stead, C. V. and Lowe, C. R. Design and applications of biomimetic anthraquinone dyes 2. The interactions of C.I. Reactive blue 2 analogues bearing terminal ring modifications with HLADH. J. Chromatogr. 1988, 455, 201-216
26. Burton, S. J., Stead, C. V. and Lowe, C. R. Design and applications of biomimetic anthraquinone dyes 3. Anthraquinone-immobilised C.I. Reactive blue 2 analogues and their interactions with HLADH and other adenine nucleotide binding proteins. J. Chromatogr. 1990, 508, 109-125
27. Dean, P. D. G. and Watson, D. H. Protein purification using immobilised triazine dyes. J. Chromatogr. 1979, 165, 301-319
28. Kopperschläger, G., Böhme, H. J. and Hofmann, E. Cibacron Blue F3G-A and related dyes as ligands in affinity chromatography. In Advances in Biochemical Engineering (Fiechter, A., ed.)., Springer-Verlag, Berlin, Germany, 1982, 101-138
29. McLoughlin, S. B. and Lowe, C. R. Applications of triazine dyes in protein purification. Rev. Prog. Coloration 1988, 18, 16-28
30. Biellmann, J. F., Samama, J.-P., Brändén, C.-I. and Eklund, H. X-ray studies of the binding of Cibacron Blue F3G-A to HLADH. Eur. J. Biochem. 1979, 102, 107-110
31. + binding to HLADH. Biochemistry 1984, 23, 5982-5996
32. Small, D. A. P., Lowe, C. R., Atkinson, T. and Bruton, J. Affinity labelling of enzymes with triazine dyes - isolation of a peptide in the catalytic domain of HLADH using Procion Blue MX-R as a structural probe. Eur. J. Biochem. 1982, 128, 119-123
33. Jörnvall, H., Woenckhaus, C. and Johnscher, G. Modification of alcohol dehydrogenases with a reactive coenzyme analogue. Eur. J. Biochem. 1975, 53, 71-81
34. Jones, J. B. An illustrative example of a synthetically useful enzyme; HLADH. In: Enzymes in Organic Syntheses. CIBA Foundation Symposium III, Pitman, London, 1985, 3-21
35. Brändén, C.-I., Jörnvall, H., Eklund, H. and Furguren, B. Alcohol dehydrogenases. In: The Enzymes, Vol. 11 (Boyer, P. D., ed.). Academic Press, New York, 1975, 103-190
36. Eklund, H. and Brändén, C.-I. Alcohol Dehydrogenase. In Biological Macromolecules and Assemblies (Jurnak, F. A. and McPherson, A., eds.). Wiley-Interscience, New York, 1987, 73-142
37. + analogues with pentose and purine ring modifications. J. Biol. Chem. 1962, 237, 1709-1715
38. Cannon, D. J. and McKay, R. H. The amino acid composition of HLADH. Biochem. Biophys. Res. Commun. 1969, 35, 403-409
39. Eklund, H., Nordström, B., Zeppezauer, E., Söderlund, G., Ohlsson, I., Boiwe, T., Söderberg, B.-O., Tapia, O. and Brändén, C.-I. Three-dimensional structure of HLADH at 2.4 Å resolution. J. Mol. Biol. 1976, 102, 27-59
40. Beech, W. F. Fibre Reactive Dyes. Logos Press, London, 1970
41. Siegel, E. In: The Chemistry of Synthetic Dyes, Vol. 6 (Venkatraman, K., ed.). Academic Press, New York, 1972, 1-209
42. Göbbeler, K. H. and Woenckhaus, C. Die intramolekulare Wechselwirkung in Coenzymen III. Nicotinamid-pentamethylen-adenosin-pyrophosphate. Justus Liebigs Annalen de Chemie 1966, 700, 180-186
43. Kaplan, N. O. The pyridine coenzymes. In: The Enzymes, Vol. 3 (Boyer, P. D., Lardy, M., and Myrback, K., eds.). Academic Press, London, 1960, 105-169
44. Lehninger, A. L. Reduced diphosphorydine nucleotide. Reduction using sodium dithionite. Biochem. Prep. 1952, 2, 92-96
45. Clonis, Y. D. Affinity chromatography on immobilised dyes. Post-immobilisation chemical modification of triazine dyes. J. Chromatogr. 1982, 236, 69-80
46. Stollar, V. Studies with phenazine methosulphate; effect on mitochondria - an assay for reduced pyridine nucleotide coenzymes. Biochim. Biophys. Acta 1960, 44, 245-250
47. +-pyrazole complex: A model of a ternary intermediate in the enzyme reaction. Biochimica Zeitschrift 1963, 338, 537-553
48. Shore, J. D. and Gilleland, M. J. Binding and kinetic studies of HLADH-coenzyme-pyrazole complexes. J. Biol. Chem. 1970, 245, 3422-3425
49. Eklund, H., Plapp, B. V., Samama, J.-P. and Brändén, C.-I. Binding of substrate in a ternary complex of HLADH. J. Biol. Chem. 1982, 257, 14349-14358
50. Anderson, D. C. and Dahlquist, F. W. Properties of bound trifluoroethanol complexes with HLADH. Biochem. J. 1982, 21, 3569-3578
51. Ansell, R. J., Small, D. A. P. and Lowe, C. R. Characterisation of the artificial coenzyme CL4. In preparation.