dc.contributor.authorThellamurege, Nandun
dc.contributor.authorHirao, Hajime
dc.identifier.citationThellamurege, N., & Hirao, H. (2013). Water Complexes of Cytochrome P450: Insights from Energy Decomposition Analysis. Molecules, 18(6), 6782-6791.en_US
dc.description.abstractWater is a small molecule that nevertheless perturbs, sometimes significantly, the electronic properties of an enzyme's active site. In this study, interactions of a water molecule with the ferric heme and the compound I (Cpd I) intermediate of cytochrome P450 are studied. Energy decomposition analysis (EDA) schemes are used to investigate the physical origins of these interactions. Localized molecular orbital EDA (LMOEDA) implemented in the quantum chemistry software GAMESS and the EDA method implemented in the ADF quantum chemistry program are used. EDA reveals that the electrostatic and polarization effects act as the major driving force in both of these interactions. The hydrogen bonding in the Cpd I⋯H2O complex is similar to that in the water dimer; however, the relative importance of the electrostatic effect is somewhat larger in the water dimer.en_US
dc.rights© 2013 The Authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).en_US
dc.titleWater complexes of cytochrome P450 : insights from energy decomposition analysisen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Physical and Mathematical Sciencesen_US
dc.description.versionPublished versionen_US

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