On the modeling of arginine-bound carboxylates: A case study with pyruvate formate-lyase

Condic-Jurkic, Karmen, Tamara Perchyonok, V., Zipse, Hendrik and Smith, David M. (2008) On the modeling of arginine-bound carboxylates: A case study with pyruvate formate-lyase. Journal of Computational Chemistry, 29 14: 2425-2433. doi:10.1002/jcc.20984


Author Condic-Jurkic, Karmen
Tamara Perchyonok, V.
Zipse, Hendrik
Smith, David M.
Title On the modeling of arginine-bound carboxylates: A case study with pyruvate formate-lyase
Journal name Journal of Computational Chemistry   Check publisher's open access policy
ISSN 0192-8651
1096-987X
Publication date 2008-11-15
Sub-type Article (original research)
DOI 10.1002/jcc.20984
Open Access Status
Volume 29
Issue 14
Start page 2425
End page 2433
Total pages 9
Place of publication Hoboken, NJ United States
Publisher John Wiley and Sons, Inc.
Collection year 2008
Language eng
Subject 1600 Chemistry
2605 Computational Mathematics
Abstract High level ab initio and density functional calculations have been employed to determine the most appropriate manner in which to truncate an arginine-bound carboxylate motif, using the substrate mechanism of Pyruvate Formate-Lyase as a case study. The results show that, both qualitatively and quantitatively, a neutral carboxylic acid provides a more realistic approximation to the salt bridge arrangement than does a bare anionic carboxylate substituent.
Keyword Ab initio
Arginine-bound carboxylate
Enzyme mechanism
Pyruvate formate-lyase
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
 
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