Contribution of bacteriochlorophyll conformation to the distribution of site-energies in the FMO protein
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- 作者：Stuart A. MacGowan ; Mathias O. Senge ; sengem@tcd.ie" class="auth_mail" title="E-mail the corresponding author
- 关键词：AHC ; agglomerative hierarchical clustering ; BChl ; bacteriochlorophyll ; Chl ; chlorophyll ; E(BChl)cryst ; in vacuo SPE of BChl in protein bound conformation ; ΔQy[Mac] ; site-energy perturbation due to macrocycle distortion ; dip ; mean absolute deviation of NSD minimum basis model from observed structure for IP normal-modes ; doop ; as previous for OOP modes ; Dip ; NSD total IP distortion ; Doop ; NSD total OOP distortion ; EES ; excited-state energy ; EET ; excitation energy transfer ; EU ; experimental unit (i
- 刊名：Biochimica et Biophysica Acta (BBA) - Bioenergetics
- 出版年：2016
- 出版时间：April 2016
- 年：2016
- 卷：1857
- 期：4
- 页码：427-442
- 全文大小：1393 K
文摘
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The effects of the conformational perturbations of individual moieties of the FMO BChls a on the pigment site-energies are strictly delineated
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The stereoelectronic interplay of BChl molecular constituents are qualitatively described
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A critical comparative analysis of the traditional method employed to delineate competing structural effects versus our new method is provided
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The macrocycle conformational effect may be under evolutionary pressure to afford the observed distribution of site-energies