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Lookup NU author(s): Dr Eimer TuiteORCiD
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The source of the activation energy that allows cutting of DNA by restriction enzymes is unclear. A systematic study of the cutting efficiency of the type-II restriction endonuclease EcoRI. with varying background electrolyte ion pair and buffer reported here, shows only a modest dependence of efficiency on cation type. Surprisingly, efficiency does depend strongly on the presumed indifferent anion of the background salt. What emerges is that competition between the background salt anion and the buffer anion for the enzyme and DNA surfaces is crucial. The results are unexpected and counterintuitive from the point of view of conventional electrolyte theory. However, taken together with recent developments in surface chemistry, the results do fall into place and could also suggest a novel mechanism for enzyme activity as an alternative to metal-activated hydrolysis: microscopic cavitation in a hydrophobic pocket might be the source of activation energy.
Author(s): Tuite E; Kim H-K; Norden B; Ninham BW
Publication type: Article
Publication status: Published
Journal: European Physical Journal E. Soft Matter
Year: 2001
Volume: 4
Issue: 4
Pages: 411-417
ISSN (print): 1292-8941
ISSN (electronic): 1292-895X
Publisher: Springer
URL: http://dx.doi.org/10.1007/s101890170096
DOI: 10.1007/s101890170096
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