@article{a6a4711c4beb4f63ba6b68501f46414f,
title = "Identification of the elusive hydronium ion exchanging roles with a proton in an enzyme at lower pH values",
abstract = "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).",
keywords = "X-ray diffraction, enzymes, hydronium ions, neutron diffraction, protonation",
author = "Kovalevsky, {Andrey Y.} and Hanson, {B. L.} and Mason, {S. A.} and T. Yoshida and Fisher, {S. Z.} and M. Mustyakimov and Forsyth, {V. T.} and Blakeley, {M. P.} and Keen, {D. A.} and Paul Langan",
year = "2011",
month = aug,
day = "8",
doi = "10.1002/anie.201101753",
language = "English",
volume = "50",
pages = "7520--7523",
journal = "Angewandte Chemie - International Edition",
issn = "1433-7851",
publisher = "wiley",
number = "33",
}