Theoretical studies of the proton transfer behaviors in molecular complexes analogous to catalytic triad of serine protease: Toward understanding the existence and significance of the low-barrier hydrogen-bond in enzymatic catalysis-Reference-Cited by-同舟云学术

Theoretical studies of the proton transfer behaviors in molecular complexes analogous to catalytic triad of serine protease: Toward understanding the existence and significance of the low-barrier hydrogen-bond in enzymatic catalysis

Published:2009-02 Issue:2 Volume:52 Page:131-136
ISSN:1006-9291
Container-title:Science in China Series B: Chemistry
language:en
Short-container-title:Sci. China Ser. B-Chem.

Author:

Li Ping,Wang WeiHua,Bi SiWei,Song Rui,Bu YuXiang

Publisher

Springer Science and Business Media LLC

Subject

General Chemistry

Link

http://link.springer.com/content/pdf/10.1007/s11426-009-0022-2.pdf

Reference16 articles.

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2. Westler W M, Weinhold F, Markley J L. Quantum chemical calculations on structural models of the catalytic site of Chymotrypsin: comparison of calculated results with experimental data from NMR spectroscopy. J Am Chem Soc, 2002, 124(48): 14373–14381

3. Hedstrom L. Serine protease mechanism and specificity. Chem Rev, 2002, 102(12): 4501–4523

4. Pan Y, McAllister M A. Characterization of low-barrier hydrogen bonds. 5. Microsolvation of enol-enolate. An ab initio and DFT investigation. J Org Chem, 1997, 62(23): 8171–8176

5. Frey P A, Whitt S A, Tobin J B. A low-barrier hydrogen bond in the catalytic triad of serine proteases. Science, 1994, 264(5167): 1927–1930

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