Quantum chemistry study of proteins in bacterial photosynthetic reaction center

	Quantum chemistry study of proteins in bacterial photosynthetic reaction center
	Shen, LL; Zhang, XD; Zhang, QY
刊名	INTERNATIONAL JOURNAL OF QUANTUM CHEMISTRY
	2001-05-15
卷号	83 期号:1 页码:30-40
关键词	electronic structure of protein photosynthetic reaction center (PRC) HF ab initio overlapping-dimer approximation (ODA) extended negative factor counter (ENFC) method
ISSN号	0020-7608
文献子类	Article
英文摘要	Quantum chemistry study on proteins L and M in the Rhodopseudomononas viridis (Rh. viridis) photosynthetic reaction center (PRC) are presented. The calculations were performed at ab initio level with Clementi minimal basis set by means of the overlapping-dimer approximation (ODA)-extended negative factor counting (ENFC) method. Additional point charges were added to individual residues to simulated ionized aqueous environment of the proteins in the calculations. Meanwhile, the electronic structure of protein complex MH (protein M plus the alpha -helix segment of protein H) was studied as well to examine the weak interaction between proteins M and H. As the first case of global quantum chemistry calculation for proteins in PRC, details of the electronic structure and the influence of proteins on the electron transfer process (ET) were studied. Moreover, new three-dimensional structure plots of subunit L and M were given based on the distribution of the components of frontier orbitals in order to more clearly understand the structure-function relationship of the proteins in electron transfer reactions. Calculation results indicated that the components of frontier orbitals are extremely localized at individual residues. Amino acid residues, having contributed to the frontier orbitals of protein L, are located at the flexible random area of L, while those having contributed to the frontier orbitals of protein M are located at the rigid alpha -helix area. This asymmetry of proteins L, and M provides new understanding the ET reaction that takes place mainly along branch L in the PRC of Rh. viridis. Meanwhile, there is frontier orbital localized amino acid distribution around the V-shaped pocket areas of protein L (M) that were expected to have an important interaction with Q(A) (Q(B)) All results indicate that protein provided a heterogeneous environment for pigment molecules and some important interaction between protein residues and pigment molecules are worthy of further investigation. (C) 2001 John Wiley & Sons, Inc.
WOS关键词	BACTERIOCHLOROPHYLL-B DIMER ; ELECTRON-TRANSFER REACTIONS ; INDUCED STRUCTURAL-CHANGES ; RHODOPSEUDOMONAS-VIRIDIS ; HOPPING CONDUCTIVITY ; RHODOBACTER-SPHAEROIDES ; PROTON-TRANSFER ; PIG INSULIN ; ENERGY ; DONOR
WOS研究方向	Chemistry ; Mathematics ; Physics
语种	英语
出版者	JOHN WILEY & SONS INC
WOS记录号	WOS:000168573800004
内容类型	期刊论文
源URL	[http://119.78.100.183/handle/2S10ELR8/274491]
专题	中国科学院上海药物研究所
通讯作者	Shen, LL
作者单位	Chinese Acad Sci, Inst Chem, State Key Lab Struct Chem Unstable & Stable Speci, Ctr Mol Sci, Beijing 100080, Peoples R China
推荐引用方式 GB/T 7714	Shen, LL,Zhang, XD,Zhang, QY. Quantum chemistry study of proteins in bacterial photosynthetic reaction center[J]. INTERNATIONAL JOURNAL OF QUANTUM CHEMISTRY,2001,83(1):30-40.
APA	Shen, LL,Zhang, XD,&Zhang, QY.(2001).Quantum chemistry study of proteins in bacterial photosynthetic reaction center.INTERNATIONAL JOURNAL OF QUANTUM CHEMISTRY,83(1),30-40.
MLA	Shen, LL,et al."Quantum chemistry study of proteins in bacterial photosynthetic reaction center".INTERNATIONAL JOURNAL OF QUANTUM CHEMISTRY 83.1(2001):30-40.