DOI: 10.1073/pnas.2000895117
论文题名: Acquirement of water-splitting ability and alteration of the charge-separation mechanism in photosynthetic reaction centers
作者: Tamura H. ; Saito K. ; Ishikita H.
刊名: Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
出版年: 2020
卷: 117, 期: 28 起始页码: 16373
结束页码: 16382
语种: 英语
英文关键词: Artificial photosynthesis
; Excitation energy transfer
; Oxygen evolution
; P680
; Unidirectional electron transfer
Scopus关键词: bacteriochlorophyll
; chlorophyll
; cytochrome c2
; water
; amino acid
; bacteriochlorophyll
; oxygen
; Article
; bioenergy
; electron transport
; excitation
; molecular stability
; nonhuman
; photosynthesis
; photosystem II
; polarization
; priority journal
; protein binding
; Proteobacteria
; proton transport
; separation technique
; static electricity
; chemistry
; electron
; electron transport
; metabolism
; photosynthesis
; protein subunit
; Amino Acids
; Bacteriochlorophylls
; Electron Transport
; Electrons
; Oxygen
; Photosynthetic Reaction Center Complex Proteins
; Photosystem II Protein Complex
; Protein Subunits
; Proteobacteria
; Water
英文摘要: In photosynthetic reaction centers from purple bacteria (PbRC) and the water-oxidizing enzyme, photosystem II (PSII), charge separation occurs along one of the two symmetrical electron-transfer branches. Here we report the microscopic origin of the unidirectional charge separation, fully considering electron–hole interaction, electronic coupling of the pigments, and electrostatic interaction with the polarizable entire protein environments. The electronic coupling between the pair of bacteriochlorophylls is large in PbRC, forming a delocalized excited state with the lowest excitation energy (i.e., the special pair). The charge-separated state in the active branch is stabilized by uncharged polar residues in the transmembrane region and charged residues on the cytochrome c2 binding surface. In contrast, the accessory chlorophyll in the D1 protein (ChlD1) has the lowest excitation energy in PSII. The charge-separated state involves ChlD1•+ and is stabilized predominantly by charged residues near the Mn4CaO5 cluster and the proceeding proton-transfer pathway. It seems likely that the acquirement of water-splitting ability makes ChlD1 the initial electron donor in PSII. © 2020 National Academy of Sciences. All rights reserved. Citation statistics:
资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/163438
Appears in Collections: 气候变化与战略
There are no files associated with this item.
作者单位: Tamura, H., Department of Applied Chemistry, University of Tokyo, Tokyo, 113-8654, Japan, Research Center for Advanced Science and Technology, University of Tokyo, Tokyo, 153-8904, Japan; Saito, K., Department of Applied Chemistry, University of Tokyo, Tokyo, 113-8654, Japan, Research Center for Advanced Science and Technology, University of Tokyo, Tokyo, 153-8904, Japan; Ishikita, H., Department of Applied Chemistry, University of Tokyo, Tokyo, 113-8654, Japan, Research Center for Advanced Science and Technology, University of Tokyo, Tokyo, 153-8904, Japan
Recommended Citation:
Tamura H.,Saito K.,Ishikita H.. Acquirement of water-splitting ability and alteration of the charge-separation mechanism in photosynthetic reaction centers[J]. Proceedings of the National Academy of Sciences of the United States of America,2020-01-01,117(28)