| 固氮酶底物络合活化模式的量子化学计算 |
| |
| 引用本文： | 刘爱民,周泰锦,张鸿图,万惠霖,蔡启瑞. 固氮酶底物络合活化模式的量子化学计算[J]. 生物化学与生物物理进展, 1994, 21(2): 171-172 |
| |
| 作者姓名： | 刘爱民 周泰锦 张鸿图 万惠霖 蔡启瑞 |
| |
| 作者单位： | 厦门大学化学系、物理化学研究所;厦门大学化学系、物理化学研究所;厦门大学化学系、物理化学研究所;厦门大学化学系、物理化学研究所;厦门大学化学系、物理化学研究所 |
| |
| 基金项目： | 国家基础性研究重大关键项目(攀登计划)子课题及固体表面物理化学国家重点实验室开放课题基金资助. |
| |
| 摘 要： | 用改进的EHMO方法对分子氮和乙炔作为固氮酶底物时的络合活化模式进行了总能量及电荷分布的量化近似计算.结果表明固氮酶底物活性中心(FeMo-co)对于分子氮和其它底物在络合活化时是区别对待的.
|
| 关 键 词： | 固氮酶 铁钼辅基 EHMO方法 配位 |
| 收稿时间： | 1993-10-19 |
| 修稿时间： | 1993-12-09 |
Quantum Calculation for the Coordination Modes of Substrates Binding on Nitrogenase Active-Center |
| |
| Liu Aimin,Zhou Taijin,Zhang Hongtu,Wan Huilin and Cai Qirui. Quantum Calculation for the Coordination Modes of Substrates Binding on Nitrogenase Active-Center[J]. Progress In Biochemistry and Biophysics, 1994, 21(2): 171-172 |
| |
| Authors: | Liu Aimin Zhou Taijin Zhang Hongtu Wan Huilin Cai Qirui |
| |
| Affiliation: | Department of Chemistry and Institute of Physical Chemistry, Xiamen University;Department of Chemistry and Institute of Physical Chemistry, Xiamen University;Department of Chemistry and Institute of Physical Chemistry, Xiamen University;Department of Chemistry and Institute of Physical Chemistry, Xiamen University;Department of Chemistry and Institute of Physical Chemistry, Xiamen University |
| |
| Abstract: | EHMO studies of N_2 and C_2H_2 coordination-ac-tivation led to the conclusion that the iron-molybdenum cofactor of nitrogenase might beable to give a special treat to its special sub-strate, i. e. NN. The exogenous substratesexcept N_2 are apparently not to get into thecage of the active-center and/or to manoeuvreas freely as NN inside the cage with the pro-posed structural settings. |
| |
| Keywords: | nitrogenase FeMo-cofactor EHMO approach coordination |
| 本文献已被 CNKI 维普 等数据库收录！ |
| 点击此处可从《生物化学与生物物理进展》浏览原始摘要信息 |
|
点击此处可从《生物化学与生物物理进展》下载全文 |
