Water as it applies to the function of enzymes.

作者: J.A. Kornblatt , M.J. Kornblatt

DOI: 10.1016/S0074-7696(02)15005-4

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摘要: Abstract Escherichia coli and Saccharomyces cerevisiae can metabolize, grow, divide over osmotic pressures ranging from 0.24 atm to about 100 [ Record, T M. et al. (1999). Trends Biochem. Sci. 23 , 143–148, 190–194 ; Wood, J. Microbiol. MoL Biol. Rev. 63 230–262 Marachal, P. A., Gervais, (1994). Appl. Biotechnol. 42 617–622 ]. At the higher end of range, they perform their functions with difficulty, but survive. Over full span pressures, activity water goes 0.9998 0.93. Neither authors survive at anything like these extremes; some enzymes enzymatic complexes would “fall apart,” either cease function or denature. We very much know just how two microbes manage.

参考文章(71)
V.Adrian Parsegian, R.Peter Rand, Donald C. Rau, [3] Macromolecules and water: Probing with osmotic stress Methods in Enzymology. ,vol. 259, pp. 43- 94 ,(1995) , 10.1016/0076-6879(95)59039-0
Clifford R. Robinson, Stephen G. Sligar, Hydrostatic and osmotic pressure as tools to study macromolecular recognition. Methods in Enzymology. ,vol. 259, pp. 395- 427 ,(1995) , 10.1016/0076-6879(95)59054-4
Michael GROSS, Rainer JAENICKE, Proteins under pressure FEBS Journal. ,vol. 221, pp. 617- 630 ,(1994) , 10.1111/J.1432-1033.1994.TB18774.X
Robert Huber, Dietmar Kukla, Wolfram Bode, Peter Schwager, Klaus Bartels, Johann Deisenhofer, Wolfgang Steigemann, Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor: II. Crystallographic refinement at 1.9 Å resolution Journal of Molecular Biology. ,vol. 89, pp. 73- 101 ,(1974) , 10.1016/0022-2836(74)90163-6
Karl Edman, Peter Nollert, Antoine Royant, Hassan Belrhali, Eva Pebay-Peyroula, Janos Hajdu, Richard Neutze, Ehud M. Landau, High-resolution X-ray structure of an early intermediate in the bacteriorhodopsin photocycle Nature. ,vol. 401, pp. 822- 826 ,(1999) , 10.1038/44623
R. Spolar, M. Record, Coupling of local folding to site-specific binding of proteins to DNA Science. ,vol. 263, pp. 777- 784 ,(1994) , 10.1126/SCIENCE.8303294
So Iwata, Christian Ostermeier, Bernd Ludwig, Hartmut Michel, Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans Nature. ,vol. 376, pp. 660- 669 ,(1995) , 10.1038/376660A0
Clifford R. Robinson, Stephen G. Sligar, Hydrostatic pressure reverses osmotic pressure effects on the specificity of EcoRI-DNA interactions. Biochemistry. ,vol. 33, pp. 3787- 3793 ,(1994) , 10.1021/BI00179A001
V. A. Parsegian, R. P. Rand, D. C. Rau, Osmotic stress, crowding, preferential hydration, and binding: A comparison of perspectives Proceedings of the National Academy of Sciences of the United States of America. ,vol. 97, pp. 3987- 3992 ,(2000) , 10.1073/PNAS.97.8.3987
J.A. Kornblatt, M.J. Kornblatt, G.H. Hoa, A.G. Mauk, Responses of two protein-protein complexes to solvent stress: does water play a role at the interface? Biophysical Journal. ,vol. 65, pp. 1059- 1065 ,(1993) , 10.1016/S0006-3495(93)81168-8