期刊
BIOCHEMISTRY
卷 57, 期 33, 页码 4997-5004出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.biochem.8b00574
关键词
-
资金
- JST CREST [JPMJCR1656]
- JSPS KAKENHI [JP26800224, JP16H06560, JP26105012, JP18H05155]
- Japan Agency for Medical Research and Development (AMED)
- Materials Integration for engineering polymers of Cross-ministerial Strategic Innovation Promotion Program (SIP)
- Interdisciplinary Computational Science Program in CCS, University of Tsukuba
In photosystem II (PSII), redox-active tyrosine Z (TyrZ) forms a low-barrier H-bond with N epsilon of D1-His190. The PSII crystal structures show that N delta of D1-His190 donates an H-bond to the carbonyl O of D1-Asn298. However, at a level of similar to 2 angstrom resolution, a clear discrimination between the -NH2 and -C=O groups of the asparagine side chain may not be possible based on the electron density map. Using quantum mechanical/molecular mechanical calculations, we investigated the energetics of the D1-Asn298 conformations. In the D1-Asn298-rotated conformation, where the amide N group donates an H-bond to deprotonated NS of D1-His190, oxidation of S 2 resulted in formation of a neutral radical, either TyrZ(center dot) or D1-His190(center dot). This suggests that in the D1-Asn298-rotated conformation, the redox potential (E-m) values of TyrZ/D1-His190 are lower than the E-m of the Mn4CaO5 cluster due to deprotonated D1-His190. The large disorder of a water molecule (water 1117A) at D1-Asn298 in the crystal structure as well as the absence of water 1117A in the Sr2+-substituted crystal structure may be associated with coexistence of the two D1-Asn298 conformations in the crystals.
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