Identification of the elusive hydronium ion exchanging roles with a proton in an enzyme at lower pH values

Andrey Y. Kovalevsky; B. L. Hanson; S. A. Mason; T. Yoshida; S. Z. Fisher; M. Mustyakimov; V. T. Forsyth; M. P. Blakeley; D. A. Keen; Paul Langan

doi:10.1002/anie.201101753

Identification of the elusive hydronium ion exchanging roles with a proton in an enzyme at lower pH values

Andrey Y. Kovalevsky
, B. L. Hanson
, S. A. Mason
, T. Yoshida
, S. Z. Fisher
, M. Mustyakimov
, V. T. Forsyth
, M. P. Blakeley
, D. A. Keen
, Paul Langan

Research output: Contribution to journal › Article › peer-review

63 Scopus citations

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).

Original language	English
Pages (from-to)	7520-7523
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	50
Issue number	33
DOIs	https://doi.org/10.1002/anie.201101753
State	Published - Aug 8 2011

Keywords

X-ray diffraction
enzymes
hydronium ions
neutron diffraction
protonation

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10.1002/anie.201101753

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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",

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T1 - Identification of the elusive hydronium ion exchanging roles with a proton in an enzyme at lower pH values

AU - Kovalevsky, Andrey Y.

AU - Hanson, B. L.

AU - Mason, S. A.

AU - Yoshida, T.

AU - Fisher, S. Z.

AU - Mustyakimov, M.

AU - Forsyth, V. T.

AU - Blakeley, M. P.

AU - Keen, D. A.

AU - Langan, Paul

PY - 2011/8/8

Y1 - 2011/8/8

N2 - 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).

AB - 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).

KW - X-ray diffraction

KW - enzymes

KW - hydronium ions

KW - neutron diffraction

KW - protonation

UR - https://www.scopus.com/pages/publications/79961217081

U2 - 10.1002/anie.201101753

DO - 10.1002/anie.201101753

M3 - Article

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AN - SCOPUS:79961217081

SN - 1433-7851

VL - 50

SP - 7520

EP - 7523

JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 33

ER -

Identification of the elusive hydronium ion exchanging roles with a proton in an enzyme at lower pH values

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Keywords

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