Protein motions are coupled to the reaction chemistry in coenzyme B 12-dependent ethanolamine ammonia lyase

Henry J. Russell; Alex Jones; Sam Hay; Gregory M. Greetham; Michael Towrie; Nigel Scrutton

doi:10.1002/anie.201202502

Protein motions are coupled to the reaction chemistry in coenzyme B 12-dependent ethanolamine ammonia lyase

Henry J. Russell, Alex Jones, Sam Hay, Gregory M. Greetham, Michael Towrie, Nigel Scrutton

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

Abstract

The role of protein dynamics in promoting catalysis is hotly debated. Infrared data from both ultrafast flash photolysis and stopped-flow studies show that not only does there appear to be vibrational coupling between the cofactor and protein in B12-dependent ethanolamine ammonia lyase, but also that there are significant protein motions coupled to the reaction that follows substrate binding (see picture). © 2012 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

Original language	English
Pages (from-to)	9306-9310
Number of pages	4
Journal	Angewandte Chemie International Edition
Volume	51
Issue number	37
DOIs	https://doi.org/10.1002/anie.201202502
Publication status	Published - 10 Sept 2012

Keywords

enzymes
infrared spectroscopy
protein dynamics
reaction mechanism
ultrafast spectroscopy

Research Beacons, Institutes and Platforms

Photon Science Institute

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10.1002/anie.201202502

Linking experiment to theory: Quantum entanglement during enzyme catalysis - Dr S Hay fellowship
Hay, S. (PI)
1/09/10 → 31/08/15
Project: Research

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title = "Protein motions are coupled to the reaction chemistry in coenzyme B 12-dependent ethanolamine ammonia lyase",

abstract = "The role of protein dynamics in promoting catalysis is hotly debated. Infrared data from both ultrafast flash photolysis and stopped-flow studies show that not only does there appear to be vibrational coupling between the cofactor and protein in B12-dependent ethanolamine ammonia lyase, but also that there are significant protein motions coupled to the reaction that follows substrate binding (see picture). {\textcopyright} 2012 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.",

keywords = "enzymes, infrared spectroscopy, protein dynamics, reaction mechanism, ultrafast spectroscopy",

author = "Russell, {Henry J.} and Alex Jones and Sam Hay and Greetham, {Gregory M.} and Michael Towrie and Nigel Scrutton",

year = "2012",

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day = "10",

doi = "10.1002/anie.201202502",

language = "English",

volume = "51",

pages = "9306--9310",

journal = "Angewandte Chemie International Edition",

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T1 - Protein motions are coupled to the reaction chemistry in coenzyme B 12-dependent ethanolamine ammonia lyase

AU - Russell, Henry J.

AU - Jones, Alex

AU - Hay, Sam

AU - Greetham, Gregory M.

AU - Towrie, Michael

AU - Scrutton, Nigel

PY - 2012/9/10

Y1 - 2012/9/10

N2 - The role of protein dynamics in promoting catalysis is hotly debated. Infrared data from both ultrafast flash photolysis and stopped-flow studies show that not only does there appear to be vibrational coupling between the cofactor and protein in B12-dependent ethanolamine ammonia lyase, but also that there are significant protein motions coupled to the reaction that follows substrate binding (see picture). © 2012 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

AB - The role of protein dynamics in promoting catalysis is hotly debated. Infrared data from both ultrafast flash photolysis and stopped-flow studies show that not only does there appear to be vibrational coupling between the cofactor and protein in B12-dependent ethanolamine ammonia lyase, but also that there are significant protein motions coupled to the reaction that follows substrate binding (see picture). © 2012 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

KW - enzymes

KW - infrared spectroscopy

KW - protein dynamics

KW - reaction mechanism

KW - ultrafast spectroscopy

U2 - 10.1002/anie.201202502

DO - 10.1002/anie.201202502

M3 - Article

C2 - 22893270

SN - 1521-3773

VL - 51

SP - 9306

EP - 9310

JO - Angewandte Chemie International Edition

JF - Angewandte Chemie International Edition

IS - 37

ER -

Protein motions are coupled to the reaction chemistry in coenzyme B 12-dependent ethanolamine ammonia lyase

Abstract

Keywords

Research Beacons, Institutes and Platforms

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Projects

Linking experiment to theory: Quantum entanglement during enzyme catalysis - Dr S Hay fellowship

Cite this