Atomic Structure and Water-splitting Reaction Mechanism of Photosystem II Revealed by X-ray Free Electron Laser

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  • SUGA Michihiro
    Research Institute for Interdisciplinary Science, Okayama University
  • AKITA Fusamichi
    Research Institute for Interdisciplinary Science, Okayama University
  • SHEN Jian-Ren
    Research Institute for Interdisciplinary Science, Okayama University

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  • X線自由電子レーザーを利用した光化学系IIの原子構造と 水分解反応機構の解明
  • Xセン ジユウ デンシ レーザー オ リヨウ シタ コウカガクケイ Ⅱ ノ ゲンシ コウゾウ ト ミズブンカイ ハンノウ キコウ ノ カイメイ

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Abstract

Photosystem II (PSII) is a huge membrane-protein complex which catalyzes light-driven water-oxidation reaction at its catalytic center, the oxygen evolving complex (OEC). The crystal structure of PSII has been determined at 1.9 Å resolution using synchrotron radiation which revealed that the OEC is a Mn4CaO5 cluster. Some of the manganese atoms of the OEC are, however, rapidly reduced by X-ray irradiation which results in slight elongation of the distances between manganese cations. Furthermore, high-resolution 3D structural information is only limited to the dark-stable S1 state and the structures in the other intermediate states are missing. X-ray free electron laser (XFEL) has the potential to address these unsolved problems, and unveil the water-splitting reaction mechanism of PSII. In this review, we will introduce the analyses of the damage-free structure and an intermediate structure of PSII using XFEL, demonstrating the potential to obtain high spatial resolution of biological samples by XFEL.

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