Multinuclear NMR study of enzyme hydration in an organic solvent

Biotechnology and Bioengineering

Volumn 57, Issue 6, 1998, Pages 686-693

  Lee, Christopher S ^a   Ru, Michael T ^a   Haake, Mathias ^a   Dordick, Jonathan S ^b   Reimer, Jeffrey A ^a   Clark, Douglas S ^a  

^a University of California   (United States)

^b University of Iowa   (United States)

Author keywords

Enzyme hydration; NMR spectroscopy; Organic solvents; Subtilisin

Indexed keywords

AROMATIC HYDROCARBONS; HEAVY WATER; HYDRATION; MATHEMATICAL MODELS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; ORGANIC SOLVENTS;

SUBTILISIN; TETRAHYDROFURAN; THREE STATE MODEL;

ENZYME KINETICS;

SUBTILISIN; TETRAHYDROFURAN;

ARTICLE; ENZYME ACTIVITY; ENZYME MECHANISM; HYDRATION; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE;

DEUTERIUM; FURANS; MODELS, CHEMICAL; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; SOLVENTS; SUBTILISINS; WATER;

EID: 0032549478     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19980320)57:6<686::AID-BIT6>3.0.CO;2-H     Document Type: Article

References (36)

1. Affleck, R, Xu, Z., Suzawa, V., Focht, K., Clark, D. S., Dordick, J. S. 1992. Enzymatic catalysis and dynamics in low-water environments. Proc. Natl. Acad. Sci. U.S.A. 89: 1100-1104.
2. Andrew, E. R., Bone, D. N., Bryant, D. J., Cashell, E. M., Gaspar, R., Meng, Q. A. 1982. Proton relaxation studies of dynamics of proteins in the solid state. Pure Appl. Chem. 54: 585-594.
3. Belton, P. S. 1994. NMR studies of protein hydration. Prog. Biophys. Mol. Biol. 61: 61-79.
4. Bevington, P. R., Robinson, D. K. 1992. Data reduction and error analysis for the physical sciences, Chaps. 6-11. 2nd ed. McGraw-Hill, New York.
5. Broos, J., Visser, A., Engbersen, J., Verboom, W., van Hoek, A., Reinhoudt, D. N. 1995. Flexibility of enzymes suspended in organic solvents probed by time-resolved fluorescence anisotropy - evidence that enzyme activity and enantioselectivity are directly related to enzyme flexibility. J. Am. Chem. Soc. 117: 12657-12663.
6. Burke, P. A., Griffin, R. G., Klibanov, A. M. 1992. Solid-state NMR assessment of enzyme active center structure under nonaqueous conditions. J. Biol. Chem. 267: 20057-20064.
7. Burke, P. A., Griffin, R. G., Klibanov, A. M. 1993. Solid-state nuclear magnetic resonance investigation of solvent dependence of tyrosyl ring motion in an enzyme. Biotechnol. Bioeng. 42: 87-94.
8. Chen, C. S., Sih, C. J. 1989. General aspects and optimization of enantio-selective biocatalysis in organic solvents - the use of lipases. Angew. Chem., Int. Ed. Engl. 28: 695.
9. Davis, J. H., Jeffrey, K. R., Bloom, M., Valic, M. I., Higgs, T. P. 1976. Quadrupolar echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains. Chem. Phys. Lett. 42: 390-394.
10. Dordick, J. S. 1992. Designing enzymes for use in organic solvents. Biotechnol. Prog. 8: 259-267.
11. Dwek, R. A. 1973. Nuclear magnetic resonance (NMR) in biochemistry, pp. 37-47. Clarendon Press, Oxford.
12. Finney, J. L., Poole, P. L. 1984. Protein hydration and enzyme activity: the role of hydration-induced conformation and dynamic changes in the activity of lysozyme. Comments Mol. Cell. Biophys. 2: 129-151.
13. Halle, B., Anderson, T., Forsén, S., Lindman, B. 1981. Protein hydration from water oxygon-17 magnetic relaxation. J. Am. Chem. Soc. 103: 500-508.
14. Halling, P. J. 1994. Thermodynamic Predictions for biocatalysis in non-conventional media - theory, tests, and recommendations for experimental design and analysis. Enzyme Microb. Technol. 16: 17.
15. Holmes, J. R., Kivelson, D., Drinkard, W. C. 1962. Proton exchange rates and hydrogen-bonding for water in organic solvents. J. Am. Chem. Soc. 84: 4677-4686.
16. James, T. L. 1975. Nuclear magnetic resonance in biochemistry: Principles and applications, pp. 347-363. Academic Press, New York.
17. Jarrell, H. C., Smith, I. 1983. Applications of high resolution deuterium magnetic resonance, pp. 133-149. In: J. B. Lambert, and F. G. Riddel (eds.), The multinuclear approach to NMR spectroscopy. D. Reidel Publishing Co., Boston, MA.
18. Kakalis, L. T., Kumosinski, T. F. 1992. The dynamics of water in protein solutions - the field dispersion of deuterium NMR longitudinal relaxation. Biophys. Chem. 43: 39-49.
19. Kimmich, R., Gneiting, T., Kotitschke, K., Schnur, G. 1990. Fluctuations, exchange processes, and water diffusion in aqueous protein systems - a study of bovine serum albumin by diverse NMR techniques. Biophys. J. 58: 1183-1197.
20. Kingston, B., Symons, M. 1973. Solvation spectra. J. Chem. Soc., Faraday Trans. 2, 69: 978-992.
21. Kintzinger, J. P. 1983. Oxygen-17 NMR, pp 79-100. In: P. Lazlo (ed.), NMR of newly accessible nuclei, Vol. 2. Academic Press, New York.
22. Klibanov, A. M. 1989. Enzymatic catalysis in anhydrous organic solvents. Trends Biochem. Sci. 14: 141.
23. Klibanov, A. M. Why are enzymes less active in organic solvents than in water? Trends Biotechnol. 15: 97-101.
24. 17O nuclear magnetic resonance shift in aqueous solutions of 1:1 electrolytes. J. Phys. Chem. 70: 554-561.
25. Neidhart, D. J., Petsko, G. A. 1988. The refined crystal structure of subtilisin Carlsberg at 2.5 Å resolution. Protein Eng. 2: 271.
26. Otting, G., Liepinsh, E. 1995. Protein hydration viewed by high-resolution NMR spectroscopy -implications for magnetic resonance image contrast. Acc. Chem. Res. 28: 171-177.
27. Otting, G., Liepinsh, E., Wüthrich, K. 1991. Protein hydration in aqueous solution. Science 254: 974-980.
28. Parker, M. C., Moore, B. D., Blacker, A. J. 1995. Measuring enzyme hydration in nonpolar organic solvents using NMR. Biotechnol. Bioeng. 46: 452-458.
29. Pople, J. A., Schneider, W. G., Bernstein, H. J. 1959. High resolution nuclear magnetic resonance, pp. 400-409. McGraw-Hill. New York.
30. Reuben, J. 1969. Hydrogen-bonding effects on oxygen-17 chemical shifts. J. Am. Chem. Soc. 91: 5725-5729.
31. Rupley, J. A., Yang, P. H., Tollin, G. 1980. Thermodynamic and related studies of water interacting with proteins. ACS Symp. Ser. 127: 111-132.
32. Suzawa, V., Khmelnitsky, Y. L., Giarto, L., Dordick, J. S., Clark, D. S. 1995. Suspended and immobilized chymotrypsin in organic media - structure-function relationships revealed by electron spin resonance spectroscopy. J. Am. Chem. Soc. 117: 8435-8440.
33. Tamura, A., Akasaka, K. 1992. Quantitative evaluation of water content in a solid protein by deuterium NMR. Biochim. Biophys. Acta. 1119: 178-184.
34. Wüthrich, K. 1986. NMR of proteins and nucleic acids, pp. 13-25. John Wiley & Sons, New York.
35. Xu, Z., Affleck, R., Wangikar, P., Suzawa, V., Dordick, J. S., Clark, D. S. 1994. Transition state stabilization of subtilisins in organic media. Biotechnol. Bioeng. 43: 515-520.
36. Zaks, A., Klibanov, A. M. 1988. Enzymatic catalysis in nonaqueous solvents. J. Biol. Chem. 263: 8017-8021.