高等学校化学学报

高等学校化学学报 ›› 1994, Vol. 15 ›› Issue (6): 903.

• 论文 • 上一篇    下一篇

氧络血红素模型的量子化学计算研究(Ⅰ)─氧络的几何与氢键

林大威, 王志中   

  1. 吉林大学理论化学研究所, 理论化学计算国家重点实验室, 长春, 130023
  • 收稿日期:1993-05-29 修回日期:1994-04-10 出版日期:1994-06-24 发布日期:1994-06-24
  • 通讯作者: 王志中.
  • 作者简介:林大威,男,25岁,博士研究生.
  • 基金资助:

    国家自然科学基金

Quantum-Chemical Calculation Studies on Model Oxyheme(Ⅰ)─Oxygen Geometry and Hydrogen Bond

LIN Da-Wei, WANG Zhi-Zhong   

  1. Institute of Theoretical Chemistry and National Key Laboratory of Computational Theoretical Chemistry, Jilin University, Changchun, 130023
  • Received:1993-05-29 Revised:1994-04-10 Online:1994-06-24 Published:1994-06-24

PDF (PC)

摘要： 用CNDO/2方法计算了氧络血红素中O2与铁卟啉的键合,优化得到的O2与Fe络合的几何与实验结果相符合,同时研究了氧络肌红蛋白与略远组氨酸E7上氢的氢键作用,得到氢键能为10.5kJ/mol,计算了CO与铁卟啉的络合几何。

关键词: 氧络血红素, 电子结构, 氧络几何, 氢键

Abstract: In this paper the CNDO/2 method was used to investigate the bonding between dioxygen and Fe-porphyrin in oxyheme.Optimized Fe-O2 complexing geometry is in good agreement with experimental results.At the same time, the hydrogen bond between oxymyoglobin and distal histidine E7 is studied and the liydrogen bond energy 10.5kJ/mol is obtained.For comparison the Fe-COcomplexing geometry is also studied and the result is coincided with experimental measurement.

Key words: Oxyheme, Electronic structure, Fe-O2 geometry, Hydrogen bond

TrendMD: