Institute of Plant Biology and Biotechnology, University of Münster, Münster 48143, Germany.
Department of Biochemistry and Molecular Biology, The George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel.
Plant Cell Physiol. 2021 Oct 29;62(7):1073-1081. doi: 10.1093/pcp/pcab046.
Most of life's energy comes from sunlight, and thus, photosynthesis underpins the survival of virtually all life forms. The light-driven electron transfer at photosystem I (PSI) is certainly the most important generator of reducing power at the cellular level and thereby largely determines the global amount of enthalpy in living systems (Nelson 2011). The PSI is a light-driven plastocyanin:ferredoxin oxidoreductase, which is embedded into thylakoid membranes of cyanobacteria and chloroplasts of eukaryotic photosynthetic organism. Structural determination of complexes of the photosynthetic machinery is vital for the understanding of its mode of action. Here, we describe new structural and functional insights into PSI and associated light-harvesting proteins, with a focus on the plasticity of PSI.
生命所需的能量大多来自阳光，因此光合作用是几乎所有生命形式生存的基础。光合作用系统 I (PSI) 的光驱动电子传递无疑是细胞水平上还原力的最重要产生者，从而在很大程度上决定了生命系统中的焓量（Nelson 2011）。PSI 是一个光驱动的质体蓝素：铁氧还蛋白氧化还原酶，它嵌入蓝藻的类囊体膜和真核光合生物的叶绿体中。对光合作用机制复合物的结构测定对于理解其作用模式至关重要。在这里，我们描述了对 PSI 及其相关光捕获蛋白的新的结构和功能见解，重点是 PSI 的可变性。
