Tran Rosalie, Kern Jan, Hattne Johan, Koroidov Sergey, Hellmich Julia, Alonso-Mori Roberto, Sauter Nicholas K, Bergmann Uwe, Messinger Johannes, Zouni Athina, Yano Junko, Yachandra Vittal K
Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.
Philos Trans R Soc Lond B Biol Sci. 2014 Jul 17;369(1647):20130324. doi: 10.1098/rstb.2013.0324.
The structure of photosystem II and the catalytic intermediate states of the Mn₄CaO₅ cluster involved in water oxidation have been studied intensively over the past several years. An understanding of the sequential chemistry of light absorption and the mechanism of water oxidation, however, requires a new approach beyond the conventional steady-state crystallography and X-ray spectroscopy at cryogenic temperatures. In this report, we present the preliminary progress using an X-ray free-electron laser to determine simultaneously the light-induced protein dynamics via crystallography and the local chemistry that occurs at the catalytic centre using X-ray spectroscopy under functional conditions at room temperature.
在过去几年里，人们对光系统II的结构以及参与水氧化的Mn₄CaO₅簇的催化中间态进行了深入研究。然而，要理解光吸收的顺序化学过程和水氧化的机制，需要一种超越传统低温稳态晶体学和X射线光谱学的新方法。在本报告中，我们展示了利用X射线自由电子激光在室温功能条件下，通过晶体学同时测定光诱导的蛋白质动力学，并利用X射线光谱学测定催化中心发生的局部化学过程所取得的初步进展。
