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dc.contributor.authorSENGE, MATHIASen
dc.date.accessioned2017-01-18T14:57:40Z
dc.date.available2017-01-18T14:57:40Z
dc.date.created2016en
dc.date.issued2016en
dc.date.submitted2016en
dc.identifier.citationMacGowan S.A, Senge M.O, Contribution of bacteriochlorophyll conformation to the distribution of site-energies in the FMO protein, Biochimica et Biophysica Acta - Bioenergetics, 1857, 4, 2016, 427 - 442en
dc.identifier.otherYen
dc.identifier.urihttp://hdl.handle.net/2262/78919
dc.descriptionPUBLISHEDen
dc.descriptionCited By :4 Export Date: 8 December 2016en
dc.description.abstractThe structural data for the Fenna-Matthews-Olson (FMO) protein indicate that the bacteriochlorophylls (BChls) display a significant degree of conformational heterogeneity of their peripheral substituents and the protein-induced nonplanar skeletal deformations of the tetrapyrrole macrocycle. As electronic properties of chromophores are altered by such differences, a conformational effect may influence the site-energies of specific pigments and thus play a role in mediating the excitation energy transfer dynamics, but this has not yet been established. The difficulty of assessing this question is shown to be partly the result of the inability of the sequential truncation approach usually employed to account for interactions between the conformations of the macrocycle and its substituents and an alternative approach is suggested. By assigning the BChl atoms to meaningful atom groups and performing all possible permutations of partial optimizations in a full-factorial design, where each group is either frozen in the crystal geometry or optimized in vacuo, followed by excited state calculations on each resulting structure (PM6//ZIndo/S), the specific effects of the conformations of each BChl component as well as mutual interactions between the molecular fragments on the site-energy can be delineated. This factorial relaxation procedure gives different estimates of the macrocycle conformational perturbation than the approach of sequentially truncating the BChl periphery. The results were evaluated in the context of published site-energies for the FMO pigments from three species to identify how conformational effects contribute to their distribution and instances of cross-species conservation and functional divergence of the BChl nonplanarity conformational contribution are described.en
dc.description.sponsorshipThis work was supported by Science Foundation Ireland (SFI P.I. 09/IN.1/B2650 and SFI IvP 13/IA/1894). Calculations were performed on the Lonsdale cluster maintained by the Trinity 26 Centre for High Performance Computing. This cluster was funded through grants from Science Foundation Ireland.en
dc.format.extent427en
dc.format.extent442en
dc.relation.ispartofseriesBiochimica et Biophysica Acta - Bioenergeticsen
dc.relation.ispartofseries1857en
dc.relation.ispartofseries4en
dc.rightsYen
dc.subjectFenna-Matthews-Olson (FMO)en
dc.subject.lcshChlorophylls; Factorial Design; Fenna-Matthews-Olson Protein; Light-harvesting; Nonplanar Porphyrins; Partial Optimizations; Photosynthesis; Semi-empirical Quantum Chemistryen
dc.titleContribution of bacteriochlorophyll conformation to the distribution of site-energies in the FMO proteinen
dc.typeJournal Articleen
dc.contributor.sponsorScience Foundation Ireland (SFI)en
dc.contributor.sponsorScience Foundation Ireland (SFI)en
dc.type.supercollectionscholarly_publicationsen
dc.type.supercollectionrefereed_publicationsen
dc.identifier.peoplefinderurlhttp://people.tcd.ie/sengemen
dc.identifier.rssinternalid137600en
dc.identifier.doihttp://dx.doi.org/10.1016/j.bbabio.2016.02.001en
dc.rights.ecaccessrightsopenAccess
dc.contributor.sponsorGrantNumberP.I. 09/IN.1/B2650en
dc.contributor.sponsorGrantNumberIvP 13/IA/1894en
dc.identifier.rssurihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84958781001&doi=10.1016%2fj.bbabio.2016.02.001&partnerID=40&md5=31273a40c8efa8502166abe04b7e03efen


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