Direct evidence for interaction between nano-anatase and superoxide dismutase from rat erythrocytes
文献类型：期刊论文
| 作者 | Ma, LL; Ze, YG; Liu, J; Liu, HT; Liu, C; Li, ZR; Zhao, JF; Yan, JY; Duan, YM ; Xie, YN
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| 刊名 | SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
 |
| 出版日期 | 2009 |
| 卷号 | 73期号:2页码:330-335 |
| 关键词 | Nano-anatase TiO(2) Superoxide dismutase Spectral characteristic Coordination Conformation |
| 通讯作者 | [Ma, Linglan ; Ze, Yuguang ; Liu, Jie ; Liu, Huiting ; Liu, Chao ; Yan, Jinying ; Duan, Yanmei ; Hong, Fashui] Soochow Univ, Coll Med, Suzhou 215123, Peoples R China ; [Li, Zhongrui ; Zhao, Jinfang] Univ Arkansas, Nanotechnol Ctr, Little Rock, AR 72204 USA ; [Xie, Yaning] Chinese Acad Sci, Inst High Energy Phys, Synchrotron Radiat Lab, Beijing 100039, Peoples R China |
| 英文摘要 | Nano-TiO(2) and Superoxide dismutase (SOD, EC 1.15.1.1) have been added to cosmetics and used to prevent injury of skin from UV-radiation, which might be rela red to the decrease of oxidative damage of skin. In previous studies we had proven that nano-anatase could increase the activity of SOD and decrease the oxidative damage in vivo. The mechanisms by which nano-anatase promoted SOD activity, however, are still not clearly understood. In the present work, nano-anatase in various concentrations was added to SOD from rat erythrocytes in vitro to gain insight into the mechanism of molecular interactions between nano-anatase and SOD by various spectral methods, suggesting that the reaction between SOD and nano-anatase was two-order. which meant that the SOD activity was greatly increased by low concentration of nano-anatase and inhibited by high concentration of nano-anatase. The spectroscopic assays suggested that the nano-anatase was determined to directly bind to SOD; the binding site of nano-anatase to SOD was 0.256 and the binding constants were 6.54 x 10(5) and 3.6 x 10(5) Lmol(-1); Ti was bound with three oxygen or nitrogen atoms and a Sulfur atoms of amino acid residues at the Ti-O(N) and Ti-S bond lengths of 1.86 and 2.37 angstrom, respectively, the binding nano-anatase entirely altered the secondary structure of SOD. It implied that the nano-anatase coordination created a new metal ion-active site form in SOD, thus leading to an enhancement in SOD activity. (C) 2009 Elsevier B.V. All rights reserved. |
| 学科主题 | Spectroscopy |
| 类目[WOS] | Spectroscopy |
| 研究领域[WOS] | Spectroscopy |
| 原文出处 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000266429700018 |
| 源URL | [http://ir.ihep.ac.cn/handle/311005/237010]  |
| 专题 | 高能物理研究所_实验物理中心 高能物理研究所_多学科研究中心 |
| 作者单位 | 中国科学院高能物理研究所 |
| 推荐引用方式 GB/T 7714 | Ma, LL,Ze, YG,Liu, J,et al. Direct evidence for interaction between nano-anatase and superoxide dismutase from rat erythrocytes[J]. SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY,2009,73(2):330-335. |
| APA | Ma, LL.,Ze, YG.,Liu, J.,Liu, HT.,Liu, C.,...&Hong, FS.(2009).Direct evidence for interaction between nano-anatase and superoxide dismutase from rat erythrocytes.SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY,73(2),330-335. |
| MLA | Ma, LL,et al."Direct evidence for interaction between nano-anatase and superoxide dismutase from rat erythrocytes".SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY 73.2(2009):330-335. |
入库方式： OAI收割
来源：高能物理研究所
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