Dependence of enzyme reaction mechanism on protonation state of titratable residues and QM level description: lactate dehydrogenase

S Ferrer; E Silla; I Tunon; M Oliva; V Moliner; I H Williams

doi:10.1039/b510735k

Dependence of enzyme reaction mechanism on protonation state of titratable residues and QM level description: lactate dehydrogenase

S Ferrer, E Silla, I Tunon, M Oliva, V Moliner, I H Williams

Department of Chemistry

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

20 Citations (SciVal)

Abstract

We have studied the dependence of the chemical reaction mechanism of L-lactate dehydrogenase (LDH) on the protonation state of titratable residues and on the level of the quantum mechanical (QM) description by means of hybrid quantum-mechanical/molecular-mechanical (QM/MM) methods; this methodology has allowed clarification of the timing of the hydride transfer and proton transfer components that hitherto had not been possible to state definitively.

Original language	English
Pages (from-to)	5873-5875
Number of pages	3
Journal	Chemical Communications
Issue number	47
DOIs	https://doi.org/10.1039/b510735k
Publication status	Published - 2005

Bibliographical note

ID number: ISI:000233775600008

Access to Document

10.1039/b510735k

Cite this

@article{0323e61161f041fbb6abd4d3346f52bc,

title = "Dependence of enzyme reaction mechanism on protonation state of titratable residues and QM level description: lactate dehydrogenase",

abstract = "We have studied the dependence of the chemical reaction mechanism of L-lactate dehydrogenase (LDH) on the protonation state of titratable residues and on the level of the quantum mechanical (QM) description by means of hybrid quantum-mechanical/molecular-mechanical (QM/MM) methods; this methodology has allowed clarification of the timing of the hydride transfer and proton transfer components that hitherto had not been possible to state definitively.",

author = "S Ferrer and E Silla and I Tunon and M Oliva and V Moliner and Williams, {I H}",

note = "ID number: ISI:000233775600008",

year = "2005",

doi = "10.1039/b510735k",

language = "English",

pages = "5873--5875",

journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

number = "47",

}

TY - JOUR

T1 - Dependence of enzyme reaction mechanism on protonation state of titratable residues and QM level description: lactate dehydrogenase

AU - Ferrer, S

AU - Silla, E

AU - Tunon, I

AU - Oliva, M

AU - Moliner, V

AU - Williams, I H

N1 - ID number: ISI:000233775600008

PY - 2005

Y1 - 2005

N2 - We have studied the dependence of the chemical reaction mechanism of L-lactate dehydrogenase (LDH) on the protonation state of titratable residues and on the level of the quantum mechanical (QM) description by means of hybrid quantum-mechanical/molecular-mechanical (QM/MM) methods; this methodology has allowed clarification of the timing of the hydride transfer and proton transfer components that hitherto had not been possible to state definitively.

AB - We have studied the dependence of the chemical reaction mechanism of L-lactate dehydrogenase (LDH) on the protonation state of titratable residues and on the level of the quantum mechanical (QM) description by means of hybrid quantum-mechanical/molecular-mechanical (QM/MM) methods; this methodology has allowed clarification of the timing of the hydride transfer and proton transfer components that hitherto had not been possible to state definitively.

U2 - 10.1039/b510735k

DO - 10.1039/b510735k

M3 - Article

SN - 1359-7345

SP - 5873

EP - 5875

JO - Chemical Communications

JF - Chemical Communications

IS - 47

ER -

Dependence of enzyme reaction mechanism on protonation state of titratable residues and QM level description: lactate dehydrogenase

Abstract

Bibliographical note

Access to Document

Fingerprint

Cite this