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

Single Crystal Diffraction

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

61 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

Access to Document

10.1002/anie.201101753

Cite this

@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",

}

TY - JOUR

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 - http://www.scopus.com/inward/record.url?scp=79961217081&partnerID=8YFLogxK

U2 - 10.1002/anie.201101753

DO - 10.1002/anie.201101753

M3 - Article

C2 - 21604345

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

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this