塑料醌
P680页
光系统II
化学
叶绿素
光系统I
光合作用
绿色植物采光复合体
光化学
光合反应中心
电子转移
类囊体
叶绿体
生物化学
基因
作者
Dmitriy Shevela,Jan Kern,Govindjee Govindjee,John Whitmarsh,Johannes Messinger
标识
DOI:10.1002/9780470015902.a0029372
摘要
Abstract Photosystem II (PSII) of plants, algae and cyanobacteria is a specialised protein complex that uses light energy to transfer electrons from water to plastoquinone, producing molecular oxygen and reduced plastoquinone. The PSII complex includes a peripheral antenna containing chlorophyll and other pigments to absorb light, a reaction centre that utilises the excitation energy transferred to it for charge separation, cofactors that stabilise the charge pair via electron transfer reactions, a Mn 4 CaO 5 cluster that oxidises water, and a binding pocket where plastoquinone is reduced. The electrons and protons that PSII extracts from water are employed in the overall photosynthetic process for the reduction of CO 2 , which provides the chemical energy for most life on Earth. PSII is the only known biological source of O 2 produced from water and is responsible for the molecular oxygen in the atmosphere. Key Concepts Photosystem II (PSII) is a membrane‐embedded pigment–protein complex, containing more than 20 subunits and approximately 100 cofactors. The PSII antenna and the PSII reaction centre are distinct protein complexes. Light is absorbed by chlorophyll, carotenoid and phycobilin pigments in the antenna and the excitation energy is rapidly transferred to the reaction centre. At the reaction centre, light‐induced charge separation takes place resulting in the formation of a chlorophyll cation and a pheophytin anion that are approximately 10 Å apart; this charge separation is rapidly stabilised by the transfer of the charges to more distant cofactors with smaller differences in redox potentials. The oxidation of water occurs at the Mn 4 CaO 5 cluster, which is embedded in the two protein subunits D1 and CP43 on the luminal side of PSII. To oxidise two molecules of water, four oxidising equivalents must be accumulated in the Mn 4 CaO 5 cluster by four consecutive light‐induced charge separations. Water oxidation by PSII occurs at the Mn 4 CaO 5 cluster, likely via oxo‐oxyl radical coupling in the so‐called S 4 state. Hydrogen‐bonding networks surrounding the Mn 4 CaO 5 cluster are crucial for its catalytic activity, as well as its structural flexibility. Bicarbonate ions play regulatory roles for electron transfer through PSII. The electrons and protons extracted from water by PSII drive the reduction of NADP + via Photosystem I, and the production of ATP, respectively.
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