Positive charges on lysine residues of the extrinsic 18 kDa protein are important to its electrostatic interaction with spinach photosystem II membranes
文献类型：期刊论文
| 作者 | Gao, JP; Yong, ZH; Zhang, F; Ruan, KC; Xu, CH; Chen, GY |
| 刊名 | ACTA BIOCHIMICA ET BIOPHYSICA SINICA
 |
| 出版日期 | 2005 |
| 卷号 | 37期号:11页码:737-742 |
| 关键词 | extrinsic 18 kDa protein circular dichroism electrostatic interaction chemical modification |
| 通讯作者 | Ruan, KC (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Plant Physiol & Ecol, 345 Lingling Lu, Shanghai 200032, Peoples R China.,kcruan@sibs.ac.cn ; chenggy@sippe.ac.cn |
| 英文摘要 | To determine the contribution of charged amino acids to binding with the photosystem II complex (PSII), the amino or carboxyl groups of the extrinsic 18 kDa protein were modified with N-succinimidyl propionate (NSP) or glycine methyl ester (GME) in the presence of a water-soluble carbodiimide, respectively. Based on isoelectric point shift, 4-10 and 10-14 amino groups were modified in the presence of 2 and 4 mM NSP, respectively. Similarly, 3-4 carboxyl groups were modified by reaction with 100 mM GME. Neutralization of negatively charged carboxyl groups with GME did not alter the binding activity of the extrinsic 18 kDa protein. However, the NSP-modified 18 kDa protein, in which the positively charged amino groups had been modified to uncharged methyl esters, failed to bind with the PSII membrane in the presence of the extrinsic 23 kDa protein. This defect can not be attributed to structural or conformational alterations imposed by chemical modification, as the fluorescence and circular dichroism spectra among native, GME-and NSP-modified extrinsic 18 kDa proteins were similar. Thus, we have concluded that the positive charges of lysyl residues in the extrinsic 18 kDa protein are important for its interaction with PSII membranes in the presence of the extrinsic 23 kDa protein. Furthermore, it was found that the negative charges of carboxyl groups of this protein did not participate in binding with the extrinsic 23 kDa protein associated with PSII membranes. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 关键词[WOS] | OXYGEN-EVOLVING COMPLEX ; HIGHER-PLANTS ; PSBQ PROTEIN ; POLYPEPTIDES ; IDENTIFICATION ; RECONSTITUTION ; SPECTROSCOPY ; EVOLUTION ; RELEASE ; DOMAINS |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000233539600003 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/1961]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Gao, JP,Yong, ZH,Zhang, F,et al. Positive charges on lysine residues of the extrinsic 18 kDa protein are important to its electrostatic interaction with spinach photosystem II membranes[J]. ACTA BIOCHIMICA ET BIOPHYSICA SINICA,2005,37(11):737-742. |
| APA | Gao, JP,Yong, ZH,Zhang, F,Ruan, KC,Xu, CH,&Chen, GY.(2005).Positive charges on lysine residues of the extrinsic 18 kDa protein are important to its electrostatic interaction with spinach photosystem II membranes.ACTA BIOCHIMICA ET BIOPHYSICA SINICA,37(11),737-742. |
| MLA | Gao, JP,et al."Positive charges on lysine residues of the extrinsic 18 kDa protein are important to its electrostatic interaction with spinach photosystem II membranes".ACTA BIOCHIMICA ET BIOPHYSICA SINICA 37.11(2005):737-742. |
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