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

Research output: Contribution to journalArticle

19 Citations (Scopus)

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 languageEnglish
Pages (from-to)5873-5875
Number of pages3
JournalChemical Communications
Issue number47
DOIs
Publication statusPublished - 2005

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Proton transfer
Protonation
L-Lactate Dehydrogenase
Hydrides
Chemical reactions
Enzymes
Oxidoreductases

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Dependence of enzyme reaction mechanism on protonation state of titratable residues and QM level description: lactate dehydrogenase. / Ferrer, S; Silla, E; Tunon, I; Oliva, M; Moliner, V; Williams, I H.

In: Chemical Communications, No. 47, 2005, p. 5873-5875.

Research output: Contribution to journalArticle

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AU - Tunon, I

AU - Oliva, M

AU - Moliner, V

AU - Williams, I H

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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.

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