期刊
ACCOUNTS OF CHEMICAL RESEARCH
卷 42, 期 12, 页码 1871-1880出版社
AMER CHEMICAL SOC
DOI: 10.1021/ar900117k
关键词
-
Water oxidation, forming O-2 from water and sunlight, is a fundamental process for life on earth. In nature, the enzyme photosystem II (PSII) catalyzes this reaction. The oxygen evolving complex (OEC) the complex within PSII that catalyzes the actual formation of the O-O bond, contains four manganese atoms and one calcium atom connected by oxo bonds. Seven amino acid side chains in the structure, mostly carboxylates, are ligated to the metal atoms. In the study of many enzyme mechanisms, theoretical modeling using density functional theory has served as an indispensable tool. This Account summarizes theoretical research to elucidate,the mechanism for water oxidation in photosynthesis, including the most recent findings. The development of successively larger models, ranging from 50 atoms in the active site up to the present model size of 170 atoms, has revealed the mechanism Of O-2 formation with increasing detail. The X-ray crystal structures of PSII have provided a framework for optimizing the theoretical models. By constraint of the backbone atoms to be at the same positions as those in the X-ray structures, the theoretical structures are in good agreement with both the measured electron density and extended X-ray absorption fine structure (EXAFS) interpretations. By following the structural and energetic changes in those structures through the different steps in the catalytic process, we have modeled the oxidation of the catalytic complex, the binding of the two substrate water molecules, and the subsequent deprotonations of those substrate molecules. In these models, the OEC forms a basin into which the water molecules naturally fit. These findings demonstrate that the binding of the second water molecule causes a reconstruction, results that are consistent with earlier EXAFS measurements. Most importantly, this Account describes a low-barrier mechanism for formation of the O-O bond, involving an oxygen radical that reacts with a mu-oxo ligand of the OEC. Further research revealed that the oxygen radical is bound in the Mn3Ca cube rather than to the outside manganese. This Account provides detailed diagrams of the energetics of the different S-transitions both without and with a membrane gradient. An interesting detail of these reactions concerns the role of the tyrosine (Tyr(z)), which appears as an intermediate radical in the oxidation of the OEC. By simple electrostatic arguments, these results show that the initial oxidation of Tyr(z) is downhill for the first two transitions but uphill for the final ones. In these later transitions, the oxidation of the OEC is coupled to deprotonations of water.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据