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Volumn 110, Issue 40, 2006, Pages 11501-11508

Proton affinity of canavanine and canaline, oxyanalogues of arginine and ornithine, from the extended kinetic method

Author keywords

[No Author keywords available]

Indexed keywords

CANAVANINE; ELECTROSPRAY IONIZATION; ION TRAP INSTRUMENTS; PROTON AFFINITY;

EID: 33750366599     PISSN: 10895639     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp063081f     Document Type: Article
Times cited : (13)

References (65)
  • 2
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons
    • Karas, M.; Hillenkamp, F. Laser Desorption Ionization of Proteins with Molecular Masses Exceeding 10,000 Daltons. Anal. Chem. 1988, 60, 2299.
    • (1988) Anal. Chem. , vol.60 , pp. 2299
    • Karas, M.1    Hillenkamp, F.2
  • 4
    • 0023228195 scopus 로고
    • The order of proton affinities of the 20 common 1-α-amino acids
    • Bojesen, G. The Order of Proton Affinities of the 20 Common 1-α-Amino Acids. J. Am. Chem. Soc. 1987, 109, 5557.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 5557
    • Bojesen, G.1
  • 5
    • 37049082684 scopus 로고
    • On the proton affinity of some α-amino acids and the theory of the kinetic method
    • Bojesen, G.; Breindahl, T. On the Proton Affinity of Some α-Amino Acids and the Theory of the Kinetic Method. J. Chem. Soc., Perkins Trans. 2 1994, 2, 1029.
    • (1994) J. Chem. Soc., Perkins Trans. 2 , vol.2 , pp. 1029
    • Bojesen, G.1    Breindahl, T.2
  • 6
    • 84989085622 scopus 로고
    • A kinetic approach to the proton affinity of amine bases
    • Li, X.; Harrison, A. G. A Kinetic Approach to the Proton Affinity of Amine Bases. Org. Mass Spectrom. 1993, 28, 366.
    • (1993) Org. Mass Spectrom. , vol.28 , pp. 366
    • Li, X.1    Harrison, A.G.2
  • 7
    • 0001588558 scopus 로고    scopus 로고
    • The gas-phase basicities and proton affinities of amino acids and peptides
    • Harrison, A. G. The Gas-Phase Basicities and Proton Affinities of Amino Acids and Peptides. Mass Spectrom. Rev. 1997, 16, 201.
    • (1997) Mass Spectrom. Rev. , vol.16 , pp. 201
    • Harrison, A.G.1
  • 8
    • 0034963024 scopus 로고    scopus 로고
    • Estimation of proton affinity of proline and tryptophan under electrospray ionization conditions using the extended kinetic method
    • Mirza, S. P.; Prabhakar, S.; Vairamani, M. Estimation of Proton Affinity of Proline and Tryptophan Under Electrospray Ionization Conditions Using the Extended Kinetic Method. Rapid Comm. Mass Spectrom. 2001, 15, 957.
    • (2001) Rapid Comm. Mass Spectrom. , vol.15 , pp. 957
    • Mirza, S.P.1    Prabhakar, S.2    Vairamani, M.3
  • 9
    • 0346678656 scopus 로고    scopus 로고
    • Proton affinities of the commonly occurring L-amino acids by using electro-spray ionization-ion trap mass spectrometry
    • Afonso, C.; Modeste, F.; Breton, P.; Fournier, F.; Tabet, J. C. Proton Affinities of the Commonly Occurring L-Amino Acids by Using Electro-spray Ionization-Ion Trap Mass Spectrometry. Eur. J. Mass Spectrom. 2000, 6, 443.
    • (2000) Eur. J. Mass Spectrom. , vol.6 , pp. 443
    • Afonso, C.1    Modeste, F.2    Breton, P.3    Fournier, F.4    Tabet, J.C.5
  • 11
    • 0024017498 scopus 로고
    • Models for strong interactions in proteins and enzymes. 1. Enhanced acidities of principal biological hydrogen donors
    • Meot-Ner (Mautner), M. Models for Strong Interactions in Proteins and Enzymes. 1. Enhanced Acidities of Principal Biological Hydrogen Donors. J. Am. Chem. Soc. 1988, 110, 3071.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 3071
    • Meot-Ner, M.1
  • 12
    • 0020764887 scopus 로고
    • Effect of solvation on the acid/base properties of glycine
    • Locke, M. J.; McIver, R. T., Jr. Effect of Solvation on the Acid/Base Properties of Glycine. J. Am. Chem. Soc. 1983, 105, 4226.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 4226
    • Locke, M.J.1    McIver Jr., R.T.2
  • 13
    • 0000718491 scopus 로고
    • Decompositions of cationized heterodimers of amino acids in relation to charge location in peptide ions
    • Burlet, O.; Gaskell, S. J. Decompositions of Cationized Heterodimers of Amino Acids in Relation to Charge Location in Peptide Ions. J. Am. Soc. Mass Spectrom. 1993, 4, 461.
    • (1993) J. Am. Soc. Mass Spectrom. , vol.4 , pp. 461
    • Burlet, O.1    Gaskell, S.J.2
  • 15
    • 84865899847 scopus 로고
    • On the sodium and lithium ion affinties of some α-amino acids
    • Nojesen, G.; Breindal, T.; Andersen, U. On the Sodium and Lithium Ion Affinties of Some α-Amino Acids. Org. Mass Spectrom. 1993, 28, 1448.
    • (1993) Org. Mass Spectrom. , vol.28 , pp. 1448
    • Nojesen, G.1    Breindal, T.2    Andersen, U.3
  • 16
    • 0002776721 scopus 로고    scopus 로고
    • The order of lithium ion affmtites for the 20 common α-amino acids. Caluclation of energy well-depth of ion-bound dimers
    • Andersen, U. N.; Bojesen, G. The Order of Lithium Ion Affmtites for the 20 Common α-Amino Acids. Caluclation of Energy Well-Depth of Ion-Bound Dimers. J. Chem. Soc., Perkin Trans. 2 1997, 2, 323.
    • (1997) J. Chem. Soc., Perkin Trans. 2 , vol.2 , pp. 323
    • Andersen, U.N.1    Bojesen, G.2
  • 17
    • 0029959473 scopus 로고    scopus 로고
    • + binding to the DNA and RNA nucleobases. Bond energies and attachment sites from the dissociation of metal ion-bound heterodimers
    • + Binding to the DNA and RNA Nucleobases. Bond Energies and Attachment Sites from the Dissociation of Metal Ion-Bound Heterodimers. J. Am. Chem. Soc. 1996, 118, 11884.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11884
    • Cerda, B.A.1    Wesdemiotis, C.2
  • 19
    • 0034704866 scopus 로고    scopus 로고
    • An absolute sodium cation affinity scale: Threshold collision-induced dissociation experiments and ab initio theory
    • Armentrout, P. B.; Rodgers, M. T. An Absolute Sodium Cation Affinity Scale: Threshold Collision-Induced Dissociation Experiments and ab Initio Theory. J. Phys. Chem. A 2000, 104, 2238.
    • (2000) J. Phys. Chem. A , vol.104 , pp. 2238
    • Armentrout, P.B.1    Rodgers, M.T.2
  • 20
    • 0034351714 scopus 로고    scopus 로고
    • 2+ affinities of peptides: Application of the kinetic method to analogues of calcium-binding site III of rabbit skeletal troponin C
    • 2+ Affinities of Peptides: Application of the Kinetic Method to Analogues of Calcium-Binding Site III of Rabbit Skeletal Troponin C. J. Am. Soc. Mass Spectrom. 2000, 11, 770.
    • (2000) J. Am. Soc. Mass Spectrom. , vol.11 , pp. 770
    • Nemirovskiy, O.V.1    Gross, M.L.2
  • 23
    • 7744232158 scopus 로고    scopus 로고
    • + with the aromatic amino acids, phenylalanine, tyrosine, and tryptophan
    • + with the Aromatic Amino Acids, Phenylalanine, Tyrosine, and Tryptophan. J. Am. Chem. Soc 2004, 126, 14600.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 14600
    • Ruan, C.1    Rodgers, M.T.2
  • 24
    • 0043208673 scopus 로고    scopus 로고
    • + affinities of gas-phase amino acids by ligand exchange equilibrium
    • + affinities of gas-phase amino acids by ligand exchange equilibrium. Int. J. Mass Spectrom. 2003, 228, 825.
    • (2003) Int. J. Mass Spectrom. , vol.228 , pp. 825
    • Gapeev, A.1    Dunbar, R.C.2
  • 25
    • 3042606432 scopus 로고    scopus 로고
    • An experimental and theoretical dissection of potassium cation/glycine interactions
    • Moision, R. M.; Armentrout, P. B. An Experimental and Theoretical Dissection of Potassium Cation/Glycine Interactions. Phys. Chem. Chem. Phys. 2004, 6, 2588.
    • (2004) Phys. Chem. Chem. Phys. , vol.6 , pp. 2588
    • Moision, R.M.1    Armentrout, P.B.2
  • 26
    • 33645669352 scopus 로고    scopus 로고
    • The special five-membered ring of proline: An experimental and theoretical investigation of alkali metal cation interactions with proline and its four- and six-membered ring analogues
    • Moision, R. M.; Armentrout, P. B. The Special Five-Membered Ring of Proline: An Experimental and Theoretical Investigation of Alkali Metal Cation Interactions with Proline and its Four- and Six-Membered Ring Analogues. J. Phys Chem. A 2006, 110, 3933.
    • (2006) J. Phys Chem. A , vol.110 , pp. 3933
    • Moision, R.M.1    Armentrout, P.B.2
  • 27
    • 0000855019 scopus 로고
    • The relative copper(I) ion affinities of amino acids in the gas phase
    • Cerda, B. A.; Wesdemiotis, C. The Relative Copper(I) Ion Affinities of Amino Acids in the Gas Phase. J. Am. Chem. Soc. 1995, 117, 9734.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 9734
    • Cerda, B.A.1    Wesdemiotis, C.2
  • 29
    • 1642444692 scopus 로고    scopus 로고
    • The proton affinity of lysine analogues using the extended kinetic method
    • Schroeder, O. E.; Andriole, E. J.: Carver, K. L.; Poutsma, J. C. The Proton Affinity of Lysine Analogues Using the Extended Kinetic Method. J. Phys. Chem. A 2004, 108, 326.
    • (2004) J. Phys. Chem. A , vol.108 , pp. 326
    • Schroeder, O.E.1    Andriole, E.J.2    Carver, K.L.3    Poutsma, J.C.4
  • 30
    • 20444464495 scopus 로고    scopus 로고
    • Proton affinity of β-oxalylaminoalanine (BOAA). Incorporation of direct entropy correction into the single reference kinetic method
    • Wind, J. J.; Papp, L. D.; Happel, M.; Hahn, K.; Poutsma, J. C. Proton Affinity of β-Oxalylaminoalanine (BOAA). Incorporation of Direct Entropy Correction into the Single Reference Kinetic Method. J. Am. Soc. Mass Spectrom. 2005, 16, 1151.
    • (2005) J. Am. Soc. Mass Spectrom. , vol.16 , pp. 1151
    • Wind, J.J.1    Papp, L.D.2    Happel, M.3    Hahn, K.4    Poutsma, J.C.5
  • 32
    • 0013395549 scopus 로고
    • Non-protein amino acids in plants
    • Bell, E. A. Non-Protein Amino Acids in Plants. Encylc. Plant. Phys. 1975, 403.
    • (1975) Encylc. Plant. Phys. , pp. 403
    • Bell, E.A.1
  • 33
    • 38249028033 scopus 로고
    • The effect of nonprotein amino acids from Calliandra plants on the aphid, Aphis fabae
    • Simmonds, M. S. J.; Romeo, J. T.; Blaney, W. M. The Effect of Nonprotein Amino Acids from Calliandra Plants on the Aphid, Aphis fabae. Biochem. System. Ecol. 1988, 16 (7/8), 623.
    • (1988) Biochem. System. Ecol. , vol.16 , Issue.7-8 , pp. 623
    • Simmonds, M.S.J.1    Romeo, J.T.2    Blaney, W.M.3
  • 34
    • 2142733891 scopus 로고
    • Avoidance of non-protein amino acid incorporation into protein by the seed predator Caryede brasiliensis (Bruchidae)
    • Rosenthal, G. A.; Janzen, D. H. Avoidance of Non-Protein Amino Acid Incorporation into Protein by the Seed Predator Caryede brasiliensis (Bruchidae). J. Chem. Ecol. 1983, 9 (9), 1353.
    • (1983) J. Chem. Ecol. , vol.9 , Issue.9 , pp. 1353
    • Rosenthal, G.A.1    Janzen, D.H.2
  • 35
    • 0017497959 scopus 로고
    • The biological effects and mode of action of 1-canavanine, a structural analogue of L-arginine
    • Rosenthal, G. A. The Biological Effects and Mode of Action of 1-Canavanine, a Structural Analogue of L-Arginine. Qu. Rev. Biol. 1977, 52, 155.
    • (1977) Qu. Rev. Biol. , vol.52 , pp. 155
    • Rosenthal, G.A.1
  • 36
    • 0001077363 scopus 로고
    • L-Canavanine, a paradigm for the structures of substituted guanidines
    • Boyar, A.; Marsh, R. E. L-Canavanine, a Paradigm for the Structures of Substituted Guanidines. J. Am. Chem. Soc. 1982, 104, 1995.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 1995
    • Boyar, A.1    Marsh, R.E.2
  • 37
    • 0029121270 scopus 로고
    • Interaction of arginase with metal ions: Studies of the enzyme from human liver and comparison with other arginases
    • Carvajal, N.; Torres, C.; Uribe, E.; Salas, M. Interaction of Arginase with Metal Ions: Studies of the Enzyme From Human Liver and Comparison With Other Arginases. Comp. Biochem. Physiol. 1995, 112, (1), 153.
    • (1995) Comp. Biochem. Physiol. , vol.112 , Issue.1 , pp. 153
    • Carvajal, N.1    Torres, C.2    Uribe, E.3    Salas, M.4
  • 38
    • 0025332527 scopus 로고
    • Endothelia nitric oxide generating enzyme(s) in the bovine aorta: Subcellular location and metabolic characterization
    • Boje, K. M.; Fung, H.-L. Endothelia Nitric Oxide Generating Enzyme(s) in the Bovine Aorta: Subcellular Location and Metabolic Characterization. J. Pharmocol. Exp. Therapeutics 1990, 253 (1), 20.
    • (1990) J. Pharmocol. Exp. Therapeutics , vol.253 , Issue.1 , pp. 20
    • Boje, K.M.1    Fung, H.-L.2
  • 40
    • 0000801562 scopus 로고
    • The biochemical basis for the deleterious effects of L-Canavanine
    • Rosenthal, G. A. The Biochemical Basis for the Deleterious Effects of L-Canavanine. Phytochemistry 1991, 30, 1055.
    • (1991) Phytochemistry , vol.30 , pp. 1055
    • Rosenthal, G.A.1
  • 41
    • 0030989518 scopus 로고    scopus 로고
    • The biochemical basis for L-Canavanine tolerance by the tobacco budworm Heliothis virescens (Noctuidae)
    • Melangeli, C.; Rosenthal, G. A.; Dalman, D. L. The Biochemical Basis for L-Canavanine Tolerance by the Tobacco Budworm Heliothis virescens (Noctuidae). Proc. Nat. Acad. Sci., U.S.A. 1997, 94, 2255.
    • (1997) Proc. Nat. Acad. Sci., U.S.A. , vol.94 , pp. 2255
    • Melangeli, C.1    Rosenthal, G.A.2    Dalman, D.L.3
  • 42
    • 0141649430 scopus 로고    scopus 로고
    • The mechanism of L-canavanine cytotoxicity: Arginyl tRNA synthetase as a novel target for anticancer drug discovery
    • Bence, A. K.; Crooks, P. A. The Mechanism of L-Canavanine Cytotoxicity: Arginyl tRNA Synthetase as a Novel Target for Anticancer Drug Discovery. J. Enzymol. Inhib. Med. Chem. 2003, 18, 383.
    • (2003) J. Enzymol. Inhib. Med. Chem. , vol.18 , pp. 383
    • Bence, A.K.1    Crooks, P.A.2
  • 43
    • 0036245198 scopus 로고    scopus 로고
    • The antiproliferative and immunotoxic effects of L-canavanine and L-canaline
    • Bence, A. K.; Worthen, D. R.; Adams, V. R.; Crooks, P. A. The antiproliferative and immunotoxic effects of L-canavanine and L-canaline. Anti-Cancer Drug 2002, 13, 313.
    • (2002) Anti-Cancer Drug , vol.13 , pp. 313
    • Bence, A.K.1    Worthen, D.R.2    Adams, V.R.3    Crooks, P.A.4
  • 45
    • 84990637902 scopus 로고
    • Proton affinity of arginine measured by the kinetic approach
    • Wu, Z.; Fenselau, C. Proton Affinity of Arginine Measured by the Kinetic Approach. Rapid Comm. Mass Spectrom. 1992, 6, 403.
    • (1992) Rapid Comm. Mass Spectrom. , vol.6 , pp. 403
    • Wu, Z.1    Fenselau, C.2
  • 46
    • 0030915618 scopus 로고    scopus 로고
    • L-Canaline: A potent antimetabolite and anti-cancer agent from leguminous plants
    • Rosenthal, G. A. L-Canaline: A Potent Antimetabolite and Anti-Cancer Agent from Leguminous Plants. Life Sci. 1997, 60, 1635.
    • (1997) Life Sci. , vol.60 , pp. 1635
    • Rosenthal, G.A.1
  • 47
    • 84990637897 scopus 로고
    • Gas-phase basicities and proton affinities of lysine and histidine measured from the dissociation of proton-bound dimers
    • Wu, Z.; Fenselau, C. Gas-Phase Basicities and Proton Affinities of Lysine and Histidine Measured from the Dissociation of Proton-Bound Dimers. Rapid Commun. Mass Spectrom. 1994, 8, 777.
    • (1994) Rapid Commun. Mass Spectrom. , vol.8 , pp. 777
    • Wu, Z.1    Fenselau, C.2
  • 48
    • 0034478481 scopus 로고    scopus 로고
    • Entropy measurements and the kinetic method: A statistically meaningful approach
    • Armentrout, P. B. Entropy Measurements and the Kinetic Method: A Statistically Meaningful Approach. J. Am. Soc. Mass Spectrom. 2000, 11, 371.
    • (2000) J. Am. Soc. Mass Spectrom. , vol.11 , pp. 371
    • Armentrout, P.B.1
  • 49
    • 0037168351 scopus 로고    scopus 로고
    • Thermochemical determinations by the kinetic method with direct entropy corrections
    • Zheng, X.; Cooks, R. G. Thermochemical Determinations by the Kinetic Method with Direct Entropy Corrections. J. Phys. Chem. A 2002, 106, 9939.
    • (2002) J. Phys. Chem. A , vol.106 , pp. 9939
    • Zheng, X.1    Cooks, R.G.2
  • 50
    • 0000222120 scopus 로고    scopus 로고
    • Microcanonical analysis of the kinetic method. The meaning of apparent entropy
    • Ervin, K. M. Microcanonical Analysis of the Kinetic Method. The Meaning of Apparent Entropy. J. Am. Soc. Mass Spectrom. 2002, 13, 435.
    • (2002) J. Am. Soc. Mass Spectrom. , vol.13 , pp. 435
    • Ervin, K.M.1
  • 51
    • 0242410117 scopus 로고    scopus 로고
    • Entropy evaluation using the kinetic method: Is it feasible
    • Drahos, L.; Vekey, K. Entropy Evaluation using the Kinetic Method: Is it Feasible. J. Mass Spectrom. 2003, 38, 1025.
    • (2003) J. Mass Spectrom. , vol.38 , pp. 1025
    • Drahos, L.1    Vekey, K.2
  • 52
    • 4544352935 scopus 로고    scopus 로고
    • Obtaining thermochemical data by the extended kinetic method
    • Bouchoux, G.; Sablier, M.; Berruyer-Penaud, F. Obtaining Thermochemical Data by the Extended Kinetic Method. J. Mass Spectrom. 2004, 39, 986.
    • (2004) J. Mass Spectrom. , vol.39 , pp. 986
    • Bouchoux, G.1    Sablier, M.2    Berruyer-Penaud, F.3
  • 53
    • 4544324083 scopus 로고    scopus 로고
    • Systematic and random errors in ion affinities and activation entropies from the extended kinetic method
    • Ervin, K. M.; Armentrout, P. B. Systematic and Random Errors in Ion Affinities and Activation Entropies from the Extended Kinetic Method. J. Mass Spectrom. 2004, 39, 1004.
    • (2004) J. Mass Spectrom. , vol.39 , pp. 1004
    • Ervin, K.M.1    Armentrout, P.B.2
  • 54
    • 4544357155 scopus 로고    scopus 로고
    • Entropy considerations in kinetic method experiments
    • Wesdemiotis, C. Entropy Considerations in Kinetic Method Experiments. J. Mass Spectrom. 2004, 39, 998.
    • (2004) J. Mass Spectrom. , vol.39 , pp. 998
    • Wesdemiotis, C.1
  • 55
    • 4544248417 scopus 로고    scopus 로고
    • Accuracy of enthalpy and entropy determination using the kinetic method: Are we approaching a consensus?
    • Drahos, L.; Peltz, C.; Vekey, K. Accuracy of Enthalpy and Entropy Determination Using the Kinetic Method: Are We Approaching a Consensus? J. Mass Spectrom. 2004, 39, 1016.
    • (2004) J. Mass Spectrom. , vol.39 , pp. 1016
    • Drahos, L.1    Peltz, C.2    Vekey, K.3
  • 56
    • 0037213122 scopus 로고    scopus 로고
    • Protonation thermochemistry of β-alanine. An evaluation of the proton affinities and entropies determined by the extended kinetic method
    • Hahn, I. S.; Wesdemiotis, C. Protonation Thermochemistry of β-Alanine. An Evaluation of the Proton Affinities and Entropies Determined by the Extended Kinetic Method. Int. J. Mass Spectrom. 2003, 222, 465.
    • (2003) Int. J. Mass Spectrom. , vol.222 , pp. 465
    • Hahn, I.S.1    Wesdemiotis, C.2
  • 57
    • 0038517827 scopus 로고    scopus 로고
    • Application of the kinetic method to bifunctional bases. MIKE and CID-MIKE test cases
    • Bouchoux, G.; Djazi, F.; Gaillard, F.; Vierezet, D. Application of the Kinetic Method to Bifunctional Bases. MIKE and CID-MIKE Test Cases. Int. J. Mass Spectrom. 2003, 227, 479.
    • (2003) Int. J. Mass Spectrom. , vol.227 , pp. 479
    • Bouchoux, G.1    Djazi, F.2    Gaillard, F.3    Vierezet, D.4
  • 58
    • 0042744896 scopus 로고    scopus 로고
    • Application of the kinetic method to bifunctional bases. ESI tandem quadrupole experiments
    • Bouchoux, G.; Buisson, D.-A.; Bourcier, S.; Sablier, M. Application of the Kinetic Method to Bifunctional Bases. ESI Tandem Quadrupole Experiments. Int. J. Mass Spectrom 2003, 228, 1035.
    • (2003) Int. J. Mass Spectrom , vol.228 , pp. 1035
    • Bouchoux, G.1    Buisson, D.-A.2    Bourcier, S.3    Sablier, M.4
  • 59
    • 0034322926 scopus 로고    scopus 로고
    • Proton affinities of simple amine: Entropies and enthalpies of activation and their effect on the kinetic method for evaluating proton affinities
    • Cao, J. C.; Aubry, C.; Holmes, J. L. Proton Affinities of Simple Amine: Entropies and Enthalpies of Activation and Their Effect on the Kinetic Method for Evaluating Proton Affinities. J. Phys. Chem. A 2000, 104, 10045.
    • (2000) J. Phys. Chem. A , vol.104 , pp. 10045
    • Cao, J.C.1    Aubry, C.2    Holmes, J.L.3
  • 60
    • 0000189651 scopus 로고
    • Density functional thermochemistry. III. The role of exact exchange
    • Becke, A. D. Density Functional Thermochemistry. III. The Role of Exact Exchange. J. Chem. Phys. 1993, 98, 5648.
    • (1993) J. Chem. Phys. , vol.98 , pp. 5648
    • Becke, A.D.1
  • 61
    • 0345491105 scopus 로고
    • Development of the Colle-Salvetti correlation energy formula into a functional of the electron density
    • Lee. C.; Yang, W.; Parr, R. G. Development of the Colle-Salvetti Correlation Energy Formula into a Functional of the Electron Density. Phys. Rev. B 1988, 37, 785.
    • (1988) Phys. Rev. B , vol.37 , pp. 785
    • Lee, C.1    Yang, W.2    Parr, R.G.3
  • 63
    • 0011083273 scopus 로고    scopus 로고
    • Harmonic vibrational frequencies: An evaluation of Hartree-Fock, Moeller-Plesset, quadratic configuration interaction, density functional theory, and semiempirical scale factors
    • Scott, A. P.; Radom, L. Harmonic Vibrational Frequencies: An Evaluation of Hartree-Fock, Moeller-Plesset, Quadratic Configuration Interaction, Density Functional Theory, and Semiempirical Scale Factors. J. Phys. Chem. 1996, 100, 16502.
    • (1996) J. Phys. Chem. , vol.100 , pp. 16502
    • Scott, A.P.1    Radom, L.2
  • 64
    • 0032366914 scopus 로고    scopus 로고
    • Evaluated gas-phase basicities and proton affinities of molecules: An update
    • Hunter, E. P.; Lias, S. G. Evaluated Gas-Phase Basicities and Proton Affinities of Molecules: An Update. J. Phys. Chem. Ref. Data 1998, 27, 3.
    • (1998) J. Phys. Chem. Ref. Data , vol.27 , pp. 3
    • Hunter, E.P.1    Lias, S.G.2
  • 65
    • 28444435875 scopus 로고    scopus 로고
    • L-Canavanine is a time-controlled mechanism-based inhibitor of Pseudomonas aeruginosa arginine deiminase
    • Lu, X.; Li, L.; Feng, X.; Wu, Y.; Dunaway-Mariano, D.; Engen, J. R.; Mariano, P. S. L-Canavanine is a Time-Controlled Mechanism-Based Inhibitor of Pseudomonas aeruginosa Arginine Deiminase. J. Am. Chem. Soc 2005, 127, 16412.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 16412
    • Lu, X.1    Li, L.2    Feng, X.3    Wu, Y.4    Dunaway-Mariano, D.5    Engen, J.R.6    Mariano, P.S.7


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