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Minimum energy pathways for proton transfer between adjacent sites exposed to water
Tel Aviv University, Israel. (Computational Chemistry and Biochemistry (CCBG))ORCID iD: 0000-0001-8696-3104
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2007 (English)In: Journal of Physical Chemistry B, ISSN 1520-6106, E-ISSN 1520-5207, Vol. 111, no 21, 6059-6070 p.Article in journal (Refereed) Published
Abstract [en]

The capacity to transfer protons between surface groups is an innate property of many proteins. The transfer of a proton between donor and acceptor, located as far as 6−7 Å apart, necessitates the participation of water molecules in the process. In a previous study we investigated the mechanism of proton transfer (PT) between bulk exposed sites, a few ångströms apart, using as a model the proton exchange between the proton-binding sites of the fluorescein molecule in dilute aqueous solution.1 The present study expands the understanding of PT reactions between adjacent sites exposed to water through the calculation the minimum energy pathways (MEPs) by the conjugate peak refinement algorithm2 and a quantum-mechanical potential. The PT reaction trajectories were calculated for the fluorescein system with an increasing number of water molecules. The MEP calculations reveal that the transition state is highly strained and involves a supramolecular structure in which fluorescein and the interconnecting water molecules are covalently bonded together and the protons are shared between neighboring oxygens. These findings are in accord with the high activation energy, as measured for the reaction, and indicate that PT reactions on the surface proceed by a semi- or fully concerted rather than stepwise mechanism. A similar mechanism is assumed to be operative on the surface of proteins and renders water-mediated PT reactions as highly efficient as they are.

Place, publisher, year, edition, pages
2007. Vol. 111, no 21, 6059-6070 p.
National Category
Theoretical Chemistry
Research subject
Natural Science
Identifiers
URN: urn:nbn:se:lnu:diva-14227DOI: 10.1021/jp070781rOAI: oai:DiVA.org:lnu-14227DiVA: diva2:445520
Available from: 2011-10-04 Created: 2011-09-16 Last updated: 2016-11-01Bibliographically approved

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