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Acid-base thermochemistry of gaseous aliphatic α-aminoacids.
MedLine Citation:
PMID:  21038045     Owner:  NLM     Status:  In-Process    
Abstract/OtherAbstract:
Acid-base thermochemistry of isolated aliphatic amino acids (denoted AAA): glycine, alanine, valine, leucine, isoleucine and proline has been examined theoretically by quantum chemical computations at the G3MP2B3 level. Conformational analysis on neutral, protonated and deprotonated species has been used to identify the lowest energy conformers and to estimate the population of conformers expected to be present at thermal equilibrium at 298 K. Comparison of the G3MP2B3 theoretical proton affinities, PA, and ΔH(acid) with experimental results is shown to be correct if experimental thermochemistry is re-evaluated and adapted to the most recent acidity-basicity scales. From this point of view, a set of evaluated proton affinities of 887, 902, 915, 916, 919 and 941 kJ mol(-1), and a set of evaluated ΔH(acid) of 1433, 1430, 1423, 1423, 1422 and 1426 kJ mol(-1), is proposed for glycine, alanine, valine, leucine, isoleucine and proline, respectively. Correlations with structural parameters (Taft's σ(α) polarizability parameter and molecular size) suggest that polarizability of the side chain is the major origin of the increase in PA and decrease in ΔH(acid) along the homologous series glycine, alanine, valine and leucine/isoleucine. Heats of formation of gaseous species AAA, AAAH(+) and [AAA-H](-) were computed at the G3MP2B3 level. The present study provides previously unavailable Δ(f)H°(298) for the ionized species AAAH(+) and [AAA-H](-). Comparison with Benson's estimate, and correlation with molecular size, show that several experimental Δ(f)H°(298) values of neutral or gaseous AAA might be erroneous.
Authors:
Guy Bouchoux; Sihua Huang; Bhawani Singh Inda
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Publication Detail:
Type:  Journal Article     Date:  2010-10-29
Journal Detail:
Title:  Physical chemistry chemical physics : PCCP     Volume:  13     ISSN:  1463-9084     ISO Abbreviation:  Phys Chem Chem Phys     Publication Date:  2011 Jan 
Date Detail:
Created Date:  2010-12-17     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100888160     Medline TA:  Phys Chem Chem Phys     Country:  England    
Other Details:
Languages:  eng     Pagination:  651-68     Citation Subset:  IM    
Affiliation:
Laboratoire des Mécanismes Réactionnels, UMR CNRS 7651, Département de Chimie, Ecole Polytechnique, F-91128 Palaiseau cedex, France. bouchoux@dcmr.polytechnique.fr
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