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Dr. Andrey Y. Kovalevsky, Dr. B. L. Hanson, Dr. S. A. Mason, Dr. T. Yoshida, Dr. S. Z. Fisher, Dr. M. Mustyakimov, Dr. V. T. Forsyth, Dr. M. P. Blakeley, Dr. D. A. Keen and Dr. Paul Langan Identification of the Elusive Hydronium Ion Exchanging Roles with a Proton in an Enzyme at Lower pH Values Angewandte Chemie International Edition 50

Version of Record online: 23 MAY 2011 | DOI: 10.1002/anie.201101753

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Visible to neutrons: Although thought to be involved in biological processes, hydronium ions had never been identified in biomacromolecular crystallographic structures. A hydronium ion has now been found by neutron and X-ray crystallography to interchange with metal cofactors in the active site of an enzyme. Under more acidic conditions, the hydronium ion is dehydrated to a proton, and the binding site collapses (see picture).

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