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Computational Methods for the Study of Enzymic Reaction Mechanisms. 1. Application to the Hydride Transfer Step in the Catalysis of Dihydrofolate Reductase

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Cummins, Peter; Greatbanks, S; Rendell, Alistair; Gready, Jill

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The computational methods for the study of enzymic reaction mechanisms were discussed. High level quantum mechanics cluster calculations and hybrid semiempirical calculations were used for enzymic reactions. The effects of active site protonation on the hydride ion transfer reaction from the nicotinamide adenine dinucleotide phosphate (NADPH) cofactor to the substrate folate and dihydrofolate in the presence of the enzyme, dihydrofolate reductase from Escherichia coli (E.coli) were analyzed. It...[Show more]

dc.contributor.authorCummins, Peter
dc.contributor.authorGreatbanks, S
dc.contributor.authorRendell, Alistair
dc.contributor.authorGready, Jill
dc.date.accessioned2015-12-13T22:24:40Z
dc.identifier.issn1520-6106
dc.identifier.urihttp://hdl.handle.net/1885/72836
dc.description.abstractThe computational methods for the study of enzymic reaction mechanisms were discussed. High level quantum mechanics cluster calculations and hybrid semiempirical calculations were used for enzymic reactions. The effects of active site protonation on the hydride ion transfer reaction from the nicotinamide adenine dinucleotide phosphate (NADPH) cofactor to the substrate folate and dihydrofolate in the presence of the enzyme, dihydrofolate reductase from Escherichia coli (E.coli) were analyzed. It was concluded that the reduction takes place when active site (Asp 27) (E.coli) was protonated.
dc.publisherAmerican Chemical Society
dc.sourceJournal of Physical Chemistry B
dc.subjectKeywords: Activation energy; Catalyst activity; Computation theory; Computer simulation; Escherichia coli; Free energy; Hydrides; Ionization; Molecular dynamics; Nuclear magnetic resonance; Optimization; Probability density function; Density functional theory (DFT)
dc.titleComputational Methods for the Study of Enzymic Reaction Mechanisms. 1. Application to the Hydride Transfer Step in the Catalysis of Dihydrofolate Reductase
dc.typeJournal article
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.citationvolume106
dc.date.issued2002
local.identifier.absfor060107 - Enzymes
local.identifier.absfor030799 - Theoretical and Computational Chemistry not elsewhere classified
local.identifier.ariespublicationMigratedxPub3447
local.type.statusPublished Version
local.contributor.affiliationCummins, Peter, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationGreatbanks, S, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationRendell, Alistair, College of Engineering and Computer Science, ANU
local.contributor.affiliationGready, Jill, College of Medicine, Biology and Environment, ANU
local.description.embargo2037-12-31
local.bibliographicCitation.startpage9934
local.bibliographicCitation.lastpage9944
local.identifier.doi10.1021/jp021070q
dc.date.updated2015-12-11T08:08:33Z
local.identifier.scopusID2-s2.0-0037180004
CollectionsANU Research Publications

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