Nuclear quantum tunnelling in enzymatic reactions - an enzymologist's perspective.

Linus Johannissen; Sam Hay; NS Scrutton

doi:10.1039/C5CP00614G

Nuclear quantum tunnelling in enzymatic reactions - an enzymologist's perspective.

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

Abstract

Enzyme-catalysed H-transfer reactions are ubiquitous, yet fundamental details of these reactions remain unresolved. In this perspective, we discuss the roles of nuclear quantum tunnelling and (compressive) dynamics during these reactions. Evidence for the coupling of specific substrate and/or protein vibrations to the chemical coordinate is considered and a case is made for the combination of multiple experimental and computational/theoretical approaches when studying these reactions.

Original language	English
Pages (from-to)	30775-30782
Number of pages	8
Journal	Physical Chemistry Chemical Physics
Volume	17
Issue number	46
DOIs	https://doi.org/10.1039/C5CP00614G
Publication status	Published - 18 Nov 2015

Access to Document

10.1039/C5CP00614GLicence: CC BY

Heavy enzymes: Probing fast dynamics in enzyme catalysis by mass modulation
Hay, S. (PI) & Scrutton, N. (CoI)
1/01/15 → 31/12/17
Project: Research
Linking experiment to theory: Quantum entanglement during enzyme catalysis - Dr S Hay fellowship
Hay, S. (PI)
1/09/10 → 31/08/15
Project: Research

Cite this

@article{9bcca5d3493e484a9ed907ebb210a40c,

title = "Nuclear quantum tunnelling in enzymatic reactions - an enzymologist's perspective.",

abstract = "Enzyme-catalysed H-transfer reactions are ubiquitous, yet fundamental details of these reactions remain unresolved. In this perspective, we discuss the roles of nuclear quantum tunnelling and (compressive) dynamics during these reactions. Evidence for the coupling of specific substrate and/or protein vibrations to the chemical coordinate is considered and a case is made for the combination of multiple experimental and computational/theoretical approaches when studying these reactions.",

author = "Linus Johannissen and Sam Hay and NS Scrutton",

year = "2015",

month = nov,

day = "18",

doi = "10.1039/C5CP00614G",

language = "English",

volume = "17",

pages = "30775--30782",

journal = "Physical Chemistry Chemical Physics",

issn = "0300-9599",

publisher = "Royal Society of Chemistry",

number = "46",

}

TY - JOUR

T1 - Nuclear quantum tunnelling in enzymatic reactions - an enzymologist's perspective.

AU - Johannissen, Linus

AU - Hay, Sam

AU - Scrutton, NS

PY - 2015/11/18

Y1 - 2015/11/18

N2 - Enzyme-catalysed H-transfer reactions are ubiquitous, yet fundamental details of these reactions remain unresolved. In this perspective, we discuss the roles of nuclear quantum tunnelling and (compressive) dynamics during these reactions. Evidence for the coupling of specific substrate and/or protein vibrations to the chemical coordinate is considered and a case is made for the combination of multiple experimental and computational/theoretical approaches when studying these reactions.

AB - Enzyme-catalysed H-transfer reactions are ubiquitous, yet fundamental details of these reactions remain unresolved. In this perspective, we discuss the roles of nuclear quantum tunnelling and (compressive) dynamics during these reactions. Evidence for the coupling of specific substrate and/or protein vibrations to the chemical coordinate is considered and a case is made for the combination of multiple experimental and computational/theoretical approaches when studying these reactions.

U2 - 10.1039/C5CP00614G

DO - 10.1039/C5CP00614G

M3 - Article

C2 - 25835565

SN - 0300-9599

SN - 1463-9084

VL - 17

SP - 30775

EP - 30782

JO - Physical Chemistry Chemical Physics

JF - Physical Chemistry Chemical Physics

IS - 46

ER -

Nuclear quantum tunnelling in enzymatic reactions - an enzymologist's perspective.

Abstract

Access to Document

Fingerprint

Projects

Heavy enzymes: Probing fast dynamics in enzyme catalysis by mass modulation

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

Cite this