Density functional theory study of proton transfer in carbonic anhydrase

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• 作者：Lidong Zhang (1)
  Daiqian Xie (1)
  
• 关键词：proton transfer ; carbonic anhydrase ; reaction mechanism ; B3LYP
• 刊名：Chinese Science Bulletin
• 出版年：2005
• 出版时间：November 2005
• 年：2005
• 卷：50
• 期：22
• 页码：2557-2559
• 全文大小：456KB
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  5. Duda, D., Tu, C. K., Qian, M. Z. et al., Structural and kinetic analysis of the chemical rescue of the proton transfer function of carbonic anhydrade II, Biochem., 2001, 40(6): 1741-748. CrossRef
  6. Hakansson, K., Carlsson, M., Svensson, L. A. et al., Structure of native and Apro carbonic anhydrase II and structure of some of its anion-ligand complexes, J. Mol. Biol., 1992, 227(4): 1192-204. CrossRef
  7. Chen, H., Li, S. H., Jiang, Y. S., A density functional theory study on the intramolecular proton transfer in the enzyme carbonic anhydrase, J. Phys. Chem. A, 2003, 107(23): 4652-660. CrossRef
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• 作者单位：Lidong Zhang (1)
  Daiqian Xie (1)
  
  1. Department of Chemistry, Institute of Theoretical and Computational Chemistry, Laboratory of Mesoscopic Chemistry, Nanjing University, 210093, Nanjing, China
  
• ISSN：1861-9541

文摘

Proton transfer in carbonic anhydrase II has been studied at the B3LYP/6-31G(D) level. The active site model consists of the zinc ion, four histidine residues, two threonine residues, and three water molecules. Our calculations showed that the proton of the zinc-bound water molecule could be transferred to the nearest water molecule and an intermediate containing H3O+ is then formed. The intermediate is only 1.3 kJ·mol? above the reactant complex, whereas the barrier height for the proton transfer is about 8.1 kJ·mol?.