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

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21 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

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ID number: ISI:000233775600008

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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\}",

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year = "2005",

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language = "English",

pages = "5873--5875",

journal = "Chemical Communications",

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publisher = "Royal Society of Chemistry",

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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.

UR - https://www.scopus.com/pages/publications/29644432365

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

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