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Originally published as Biophys J. BioFAST on July 1, 2005.
doi:10.1529/biophysj.104.055798
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Biophysical Journal 89:1990-2003 (2005)
© 2005 The Biophysical Society

Influence of the Water Structure on the Acetylcholinesterase Efficiency

Angela S. F. Ramos and Simone Techert

Max-Planck-Institut für biophysikalische Chemie, Abteilung Spektroskopie und Photochemische Kinetik-Strukturdynamik (bio)chemischer Systeme, 37077 Göttingen, Germany

Correspondence: Address reprint requests to Dr. Simone Techert, Max-Planck-Institut für biophysikalische Chemie, Abteilung Spektroskopie und Photochemische Kinetik-Strukturdynamik (bio)chemischer Systeme, 37077 Göttingen, Germany. Tel.: 49-551-201-1268; Fax: 49-551-201-1501; E-mail: stecher{at}gwdg.de.

We have studied the catalytic efficiency of acetylcholinesterase (AChE) in various solutions with ion-disturbed water structure to explore the role that the water structure plays in the substrate-enzyme encounter. The extent of water structuring in the different aqueous solutions was determined by near-infrared spectroscopy. The influence of water structure on the degree of solvation and on the intramolecular mobility of AChE was investigated for different aqueous ionic solutions by small-angle x-ray scattering technique and depolarization fluorescence spectroscopy. It was found that the encounter process between AChE and acetylthiocholine was promoted in solutions with less structured water. In these solutions it was also found that AChE is less solvated coinciding with higher intramolecular mobility. The found experimental results suggest that the water structure may influence the substrate-enzyme encounter process by diminishing the AChE solvation shell and may help diffusion of the substrate through the gorge by enhancing the intramolecular mobility of AChE.






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