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利用scifinder搜索 从中挑选数篇如下： NO.1 Bibliographic Information An ONIOM study of the QA site semiquinone in the Rhodobacter sphaeroides photosynthetic reaction centre. Lin, Tzu-Jen; OMalley, Patrick J. School of Chemistry, The University of Manchester Abstract ONIOM (QM/MM) calcns. are performed to investigate the spin d. distribution for the ubisemiquinone anion radical in the QA binding site of the photosynthetic bacterium Rhodobacter sphaeroides. The calcd. spin d. in the QA site model suggests that differential hydrogen bonding strength to the O1 and O4 oxygen atoms of the radical results in an asym. spin d. distribution in the semiquinone anion free radical form. The origin of the spin d. asymmetry is attributed to the presence of the divalent iron or zinc ion situated between the QA and QB sites. Indexing -- Section 11 (Plant Biochemistry) NO.2 Bibliographic Information Three-Layer ONIOM Studies of the Dark State of Rhodopsin: The Protonation State of Glu181. Hall, Katherine F.; Vreven, Thom; Frisch, Michael J.; Bearpark, Michael J. Department of Chemistry, Imperial College Abstract A computational three-layer ONIOM(QM-high:QM-low:MM) hybrid scheme has been applied to analyze the protonation state of the Glu181 amino acid residue in rhodopsin, which is vital to detg. the rhodopsin photoactivation mechanism. Due to conflicting evidence from previous studies, it has yet to be conclusively resolved. In this study, we fully optimize dark-state rhodopsin model structures differing only at the 181-residue site-protonated and unprotonated Glu181-and calc. several exptl. observable properties. Comparison of calcd. structures, excitation energies, and NMR chem. shifts for the two models with values from the literature allows a reevaluation of previously reported conclusions. A key finding is that the S1 ? S2 energy level splitting, previously used as evidence for a neutral Glu181, is found to be almost identical for the two protonation states.