Theoretical study of molecular interaction between tirapazamine enzymatic catalysis metabolites and water |
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| Authors: | Lai‐Cai Li Dong Zha Yan Zheng Xin Wang An‐Min Tian Ning‐Bew Wong |
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| Affiliation: | 1. Department of Chemistry, Sichuan Normal University, Chengdu 610066, People's Republic of ChinaDepartment of Chemistry, Sichuan Normal University, Chengdu 610066, People's Republic of China;2. Department of Chemistry, Sichuan Normal University, Chengdu 610066, People's Republic of China;3. Department of Chemistry, Sichuan University, Chengdu 610064, People's Republic of China;4. Department of Biology and Chemistry, City University of Hong Kong, Kowloon, Hong Kong |
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| Abstract: | The weakly hydrogen‐bonded complexes, between tirapazamine enzymatic catalysis metabolites and water, have been investigated by density functional theory (DFT), using the B3LYP hybrid functional. The geometries of these complexes have been fully optimized at the B3LYP/6‐31G(d) and B3LYP/6‐311+G(d) levels. The stabilization energies and charge changes of some atoms have been calculated and analyzed. The results indicate that the catalysis metabolites and water can form stable hydrogen‐bonded complexes. Nine complexes are identified. It is important and necessary to add zero‐point vibrational energy (ZPVE) and basis set superposition error (BSSE) corrections for calculating stabilization energy. The results also reveal an important relationship between the relative stabilities of hydrogen‐bonded complexes and the final products of tirapazamine medication. © 2006 Wiley Periodicals, Inc. Int J Quantum Chem, 2007 |
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| Keywords: | density functional theory enzymatic catalysis metabolites hydrogen‐bonded complex BSSE stabilization energies |
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