期刊
ENERGY & ENVIRONMENTAL SCIENCE
卷 5, 期 7, 页码 7747-7756出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c2ee21210b
关键词
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资金
- Photosynthetic Systems Program, Office of Basic Energy Sciences, United States Department of Energy [DE-FG02-07ER15903]
- U.S. Department of Energy (DOE) [DE-FG02-07ER15903] Funding Source: U.S. Department of Energy (DOE)
- Grants-in-Aid for Scientific Research [24000018, 23657037] Funding Source: KAKEN
The water-splitting protein, photosystem II, catalyzes the light-driven oxidation of water to dioxygen. The solar water oxidation reaction takes place at the catalytic center, referred to as the oxygen-evolving complex, of photosystem II. During the catalytic cycle, the oxygen-evolving complex cycles through five distinct intermediate states, S-0-S-4. In this study, we trap the oxygen-evolving complex in the S-2 intermediate state by low temperature illumination of photosystem II isolated from three different species, Thermosynechococcus vulcanus, the PsbB variant of Synechocystis PCC 6803 and spinach. We apply two-dimensional hyperfine sublevel correlation spectroscopy to detect weak magnetic interactions between the paramagnetic tetra-nuclear manganese cluster of the S-2 state of the OEC and the surrounding protons. We identify five groups of protons that are interacting with the tetra-nuclear manganese cluster. From the values of hyperfine interactions and using the recently reported 1.9 angstrom resolution X-ray structure of the OEC in the S-1 state [Umena et al., Nature, 2011, 473, 55], we discuss the assignments of the five groups of protons and draw important conclusions on the structure of the oxygen-evolving complex in the S-2 state. In addition, we conclude that the structure of OEC is nearly identical in photosystem II from Thermosynechococcus vulcanus, the PsbB variant of Synechocystis PCC 6803 and spinach.
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