File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Experimental validation of theoretical potassium and sodium cation affinities of amides by mass spectrometric kinetic method measurements

TitleExperimental validation of theoretical potassium and sodium cation affinities of amides by mass spectrometric kinetic method measurements
Authors
Issue Date2004
PublisherJohn Wiley & Sons Ltd. The Journal's web site is located at http://www.interscience.wiley.com/jpages/0951-4198/
Citation
Rapid Communications In Mass Spectrometry, 2004, v. 18 n. 3, p. 345-355 How to Cite?
AbstractIn this study the theoretical Gaussian-2 K+/Na+ binding affinities (enthalpies) at 0 K (in kJ mol-1) for six amides in the order: formamide (109.2/138.5) < N-methylformamide (117.7/148.6) < acetamide (118.7/149.5) < N,N-dimethylformamide (123.9/156.4) < N-methylacetamide (125.6/157.7) < N,N-dimethylacetamide (129.2/162.6), reported previously (Siu et al., J. Chem. Phys. 2001; 114: 7045-7051), were validated experimentally by mass spectrometric kinetic method measurements. By monitoring the collision-induced dissociation (CID) of K+/Na +-bound heterodimers of the amides, the relative affinities were shown to be accurate to within ±2 kJ mol-1. With these six theoretical K+/Na+ binding affinities as reference values, the absolute K+/Na+ affinities of imidazole, 1-methylimidazole, pyridazine and 1,2-dimethoxyethane were determined by the extended kinetic method, and found to be consistent (to within ±9 kJ mol-1) with literature experimental values obtained by threshold-CID, equilibrium high-pressure mass spectrometry, and Fourier transform ion cyclotron resonance/ligand-exchange equilibrium methods. A self-consistent resolution is proposed for the inconsistencies in the relative order of K +/Na+ affinities of amides reported in the literature. These two sets of validated K+ and Na+ affinity values are useful as reference values in kinetic method measurements of K +/Na+ affinity of model biological ligands, such as the K+ affinities of aliphatic amino acids. Copyright © 2004 John Wiley & Sons, Ltd.
Persistent Identifierhttp://hdl.handle.net/10722/167873
ISSN
2015 Impact Factor: 2.226
2015 SCImago Journal Rankings: 0.819
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorTsang, Yen_US
dc.contributor.authorSiu, FMen_US
dc.contributor.authorHo, CSen_US
dc.contributor.authorMa, NLen_US
dc.contributor.authorTsang, CWen_US
dc.date.accessioned2012-10-08T03:12:23Z-
dc.date.available2012-10-08T03:12:23Z-
dc.date.issued2004en_US
dc.identifier.citationRapid Communications In Mass Spectrometry, 2004, v. 18 n. 3, p. 345-355en_US
dc.identifier.issn0951-4198en_US
dc.identifier.urihttp://hdl.handle.net/10722/167873-
dc.description.abstractIn this study the theoretical Gaussian-2 K+/Na+ binding affinities (enthalpies) at 0 K (in kJ mol-1) for six amides in the order: formamide (109.2/138.5) < N-methylformamide (117.7/148.6) < acetamide (118.7/149.5) < N,N-dimethylformamide (123.9/156.4) < N-methylacetamide (125.6/157.7) < N,N-dimethylacetamide (129.2/162.6), reported previously (Siu et al., J. Chem. Phys. 2001; 114: 7045-7051), were validated experimentally by mass spectrometric kinetic method measurements. By monitoring the collision-induced dissociation (CID) of K+/Na +-bound heterodimers of the amides, the relative affinities were shown to be accurate to within ±2 kJ mol-1. With these six theoretical K+/Na+ binding affinities as reference values, the absolute K+/Na+ affinities of imidazole, 1-methylimidazole, pyridazine and 1,2-dimethoxyethane were determined by the extended kinetic method, and found to be consistent (to within ±9 kJ mol-1) with literature experimental values obtained by threshold-CID, equilibrium high-pressure mass spectrometry, and Fourier transform ion cyclotron resonance/ligand-exchange equilibrium methods. A self-consistent resolution is proposed for the inconsistencies in the relative order of K +/Na+ affinities of amides reported in the literature. These two sets of validated K+ and Na+ affinity values are useful as reference values in kinetic method measurements of K +/Na+ affinity of model biological ligands, such as the K+ affinities of aliphatic amino acids. Copyright © 2004 John Wiley & Sons, Ltd.en_US
dc.languageengen_US
dc.publisherJohn Wiley & Sons Ltd. The Journal's web site is located at http://www.interscience.wiley.com/jpages/0951-4198/en_US
dc.relation.ispartofRapid Communications in Mass Spectrometryen_US
dc.subject.meshAmides - Chemistryen_US
dc.subject.meshCations, Monovalenten_US
dc.subject.meshKineticsen_US
dc.subject.meshMass Spectrometry - Methodsen_US
dc.subject.meshPotassium - Chemistryen_US
dc.subject.meshReproducibility Of Resultsen_US
dc.subject.meshSodium - Chemistryen_US
dc.subject.meshSpectroscopy, Fourier Transform Infrared - Methodsen_US
dc.titleExperimental validation of theoretical potassium and sodium cation affinities of amides by mass spectrometric kinetic method measurementsen_US
dc.typeArticleen_US
dc.identifier.emailSiu, FM:fmsiu@hku.hken_US
dc.identifier.authoritySiu, FM=rp00776en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1002/rcm.1325-
dc.identifier.pmid14755622-
dc.identifier.scopuseid_2-s2.0-0842327470en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0842327470&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume18en_US
dc.identifier.issue3en_US
dc.identifier.spage345en_US
dc.identifier.epage355en_US
dc.identifier.isiWOS:000188695200017-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridTsang, Y=7007101142en_US
dc.identifier.scopusauthoridSiu, FM=6701518489en_US
dc.identifier.scopusauthoridHo, CS=7404653591en_US
dc.identifier.scopusauthoridMa, NL=7103357185en_US
dc.identifier.scopusauthoridTsang, CW=7202935952en_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats