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Volumn 117, Issue 22, 2013, Pages 6635-6645

Catalytic mechanism of angiotensin-converting enzyme and effects of the chloride ion

Author keywords

[No Author keywords available]

Indexed keywords

AMIDES; CATALYSIS; CHLORINE COMPOUNDS; ENZYMES; MOLECULAR DYNAMICS; MOLECULES; QUANTUM CHEMISTRY; QUANTUM THEORY; REACTION KINETICS;

EID: 84879149902     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp400974n     Document Type: Article
Times cited : (41)

References (67)
  • 1
    • 0038163054 scopus 로고
    • The Preparation and Function of the Hypertension-Converting Enzyme
    • Skeggs, L. T. J.; Kahn, J. R.; Shuway, N. P. The Preparation and Function of the Hypertension-Converting Enzyme J. Exp. Med. 1956, 103, 295-299
    • (1956) J. Exp. Med. , vol.103 , pp. 295-299
    • Skeggs, L.T.J.1    Kahn, J.R.2    Shuway, N.P.3
  • 2
    • 0014217361 scopus 로고
    • Conversion of Angiotensin i to Angiotensin II
    • Ng, K. K. F.; Vane, J. R. Conversion of Angiotensin I to Angiotensin II Nature 1967, 216, 762-766
    • (1967) Nature , vol.216 , pp. 762-766
    • Ng, K.K.F.1    Vane, J.R.2
  • 3
    • 1442313018 scopus 로고    scopus 로고
    • ACE Inhibition and Bradykinin-Mediated Renal Vascular Responses: EDHF Invovement
    • Imig, J. D. ACE Inhibition and Bradykinin-Mediated Renal Vascular Responses: EDHF Invovement Hypertension 2004, 43, 533-535
    • (2004) Hypertension , vol.43 , pp. 533-535
    • Imig, J.D.1
  • 5
    • 0029925360 scopus 로고    scopus 로고
    • Mice Lacking Angiotensin-Converting Enzyme Have Low Blood Pressure, Renal Pathology and Reduced Fertility
    • Esther, C. R.; Howard, T. E., Jr.; Marino, E. M.; Goddard, J. M.; Capecchi, M. R.; Bernstein, K. E. Mice Lacking Angiotensin-Converting Enzyme Have Low Blood Pressure, Renal Pathology and Reduced Fertility Lab. Invest. 1996, 74, 953-965
    • (1996) Lab. Invest. , vol.74 , pp. 953-965
    • Esther, C.R.1    Howard Jr., T.E.2    Marino, E.M.3    Goddard, J.M.4    Capecchi, M.R.5    Bernstein, K.E.6
  • 7
    • 0035042245 scopus 로고    scopus 로고
    • RXP 407, a Selective Inhibitor of the N-Domain of Angiotensin I-Converting Enzyme, Blocks in vivo the Degradation of Hemoregulatory Peptide Acetyl-Ser-Asp-Lys-Pro with No Effect on Angiotensin i Hydrolysis
    • Junot, C.; Gonzales, M. F.; Ezan, E.; Cotton, J.; Vazeux, G.; Michaud, A.; Azizi, M.; Vassiliou, S.; Yiotakis, A.; Corvol, P.; Dive, V. RXP 407, a Selective Inhibitor of the N-Domain of Angiotensin I-Converting Enzyme, Blocks in vivo the Degradation of Hemoregulatory Peptide Acetyl-Ser-Asp-Lys-Pro with No Effect on Angiotensin I Hydrolysis J. Pharmacol. Exp. Ther. 2001, 297, 606-611
    • (2001) J. Pharmacol. Exp. Ther. , vol.297 , pp. 606-611
    • Junot, C.1    Gonzales, M.F.2    Ezan, E.3    Cotton, J.4    Vazeux, G.5    Michaud, A.6    Azizi, M.7    Vassiliou, S.8    Yiotakis, A.9    Corvol, P.10    Dive, V.11
  • 8
    • 0017584729 scopus 로고
    • Design of Potent Competitive Inhibitors of Angiotensin-Converting Enzyme. Carboxyalkanoyl and Mercaptoalkanoyl Amino Acids
    • Cushman, D. W.; Cheung, H. S.; Sabo, E. F.; Ondetti, M. A. Design of Potent Competitive Inhibitors of Angiotensin-Converting Enzyme. Carboxyalkanoyl and Mercaptoalkanoyl Amino Acids Biochemistry 1977, 16, 5484-5491
    • (1977) Biochemistry , vol.16 , pp. 5484-5491
    • Cushman, D.W.1    Cheung, H.S.2    Sabo, E.F.3    Ondetti, M.A.4
  • 9
    • 0346195665 scopus 로고    scopus 로고
    • Crystal Structure of the Human Angiotensin-Converting Enzyme-Lisinopril Complex
    • Natesh, R.; Schwager, S. L. U.; Sturrock, E. D.; Acharya, K. R. Crystal Structure of the Human Angiotensin-Converting Enzyme-Lisinopril Complex Nature 2003, 421, 551-554
    • (2003) Nature , vol.421 , pp. 551-554
    • Natesh, R.1    Schwager, S.L.U.2    Sturrock, E.D.3    Acharya, K.R.4
  • 10
    • 3042732126 scopus 로고    scopus 로고
    • Structural Details on the Binding of Antihypertensive Drugs Captopril and Enalaprilat to Human Testicular Angiotensin I-Converting Enzyme
    • Natesh, R.; Schwager, S. L. U.; Evans, H. R.; Sturrock, E. D.; Acharya, K. R. Structural Details on the Binding of Antihypertensive Drugs Captopril and Enalaprilat to Human Testicular Angiotensin I-Converting Enzyme Biochemistry 2004, 43, 8718-8724
    • (2004) Biochemistry , vol.43 , pp. 8718-8724
    • Natesh, R.1    Schwager, S.L.U.2    Evans, H.R.3    Sturrock, E.D.4    Acharya, K.R.5
  • 11
    • 44449140132 scopus 로고    scopus 로고
    • Probing the Basis of Domain-Dependent Inhibition Using Novel ketone Inhibitors of Angiotensin-Converting Enzyme
    • Watermeyer, J. M.; Kroger, W. L.; O'Neil, H. G.; Sewell, B. T.; Sturrock, E. D. Probing the Basis of Domain-Dependent Inhibition Using Novel ketone Inhibitors of Angiotensin-Converting Enzyme Biochemistry 2008, 47, 5942-5950
    • (2008) Biochemistry , vol.47 , pp. 5942-5950
    • Watermeyer, J.M.1    Kroger, W.L.2    O'Neil, H.G.3    Sewell, B.T.4    Sturrock, E.D.5
  • 12
    • 84860997466 scopus 로고    scopus 로고
    • Inhibition Mechansim and Model of an Angiotensin I-Converting Enzyme (ACE)-Inhibitory Hexapeptide from Yeast (Saccharomyces cerevisiae)
    • Ni, H.; Li, L.; Liu, G.; Hu, S. Inhibition Mechansim and Model of an Angiotensin I-Converting Enzyme (ACE)-Inhibitory Hexapeptide from Yeast (Saccharomyces cerevisiae) Plos One 2012, 7, e37077
    • (2012) Plos One , vol.7 , pp. 37077
    • Ni, H.1    Li, L.2    Liu, G.3    Hu, S.4
  • 14
    • 0021780973 scopus 로고
    • The Design and Properties of N-Carboxyalkyl-Depeptide Inhibitors of Angiotensin-Converting Enzyme
    • Patchett, A. A.; Cordes, E. H. The Design and Properties of N-Carboxyalkyl-Depeptide Inhibitors of Angiotensin-Converting Enzyme Adv. Enzymol. Relat. Areas Mol. Biol. 1985, 57, 1-84
    • (1985) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.57 , pp. 1-84
    • Patchett, A.A.1    Cordes, E.H.2
  • 15
    • 84864350421 scopus 로고    scopus 로고
    • Activity-Guided Discovery of (S)-Malic Acid 1′-O-β- Gentiobioside as an Angiotensin I-Converting Enzyme Inhibitor in Lettuce (Lactuca sativa)
    • Lagemann, A.; Dunkel, A.; Hofmann, T. Activity-Guided Discovery of (S)-Malic Acid 1′-O-β-Gentiobioside as an Angiotensin I-Converting Enzyme Inhibitor in Lettuce (Lactuca sativa) J. Agr. Food Chem. 2012, 60, 7211-7217
    • (2012) J. Agr. Food Chem. , vol.60 , pp. 7211-7217
    • Lagemann, A.1    Dunkel, A.2    Hofmann, T.3
  • 16
    • 84867364818 scopus 로고    scopus 로고
    • Purification and Characterization of a Novel Angiotensin i Converting Enzyme Inhibitory Peptide Derived from an Enzymatic Hydrolysate of Duck Skin Byproducts
    • Lee, S.; Kim, Y.; Kim, E.; Hwang, J.; Park, T.; Kim, B.; Moon, S.; Jeon, B.; Jeon, Y.; Ahn, Y.; Ahn, C.; Je, J.; Park, P. Purification and Characterization of a Novel Angiotensin I Converting Enzyme Inhibitory Peptide Derived from an Enzymatic Hydrolysate of Duck Skin Byproducts J. Agr. Food Chem. 2012, 60, 10035-10040
    • (2012) J. Agr. Food Chem. , vol.60 , pp. 10035-10040
    • Lee, S.1    Kim, Y.2    Kim, E.3    Hwang, J.4    Park, T.5    Kim, B.6    Moon, S.7    Jeon, B.8    Jeon, Y.9    Ahn, Y.10    Ahn, C.11    Je, J.12    Park, P.13
  • 17
    • 84857382200 scopus 로고    scopus 로고
    • Targeted Catalytic Inactivation of Angiotensin Converting Enzyme by Lisinopril-Coupled Transition-Metal Chelates
    • Joyner, J. C.; Hocharoen, L.; Cowan, J. A. Targeted Catalytic Inactivation of Angiotensin Converting Enzyme by Lisinopril-Coupled Transition-Metal Chelates J. Am. Chem. Soc. 2012, 134, 3396-3410
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 3396-3410
    • Joyner, J.C.1    Hocharoen, L.2    Cowan, J.A.3
  • 18
    • 34248221658 scopus 로고    scopus 로고
    • The Structure of Testis Angiotensin-Converting Enzyme in Complex with the C Domain-Specific Inhibitor RXPA380
    • Corradi, H. R.; Chitapi, I.; Sewell, T.; Georgiadis, D.; Dive, V.; Sturrock, E. D.; Acharya, K. R. The Structure of Testis Angiotensin-Converting Enzyme in Complex with the C Domain-Specific Inhibitor RXPA380 Biochem. 2007, 46, 5473-5478
    • (2007) Biochem. , vol.46 , pp. 5473-5478
    • Corradi, H.R.1    Chitapi, I.2    Sewell, T.3    Georgiadis, D.4    Dive, V.5    Sturrock, E.D.6    Acharya, K.R.7
  • 19
    • 0042490795 scopus 로고    scopus 로고
    • Roles of the Two Active Sites of Somatic Angiotensin-Converting Enzyme in the Cleavage of Angiotensin i and Bradykinin: Insights from Selective Inhibitors
    • Georgiadis, D.; Beau, F.; Czarny, B.; Cotton, J.; Yiotakis, A.; Dive, V. Roles of the Two Active Sites of Somatic Angiotensin-Converting Enzyme in the Cleavage of Angiotensin I and Bradykinin: Insights from Selective Inhibitors Circ. Res. 2003, 93, 148-154
    • (2003) Circ. Res. , vol.93 , pp. 148-154
    • Georgiadis, D.1    Beau, F.2    Czarny, B.3    Cotton, J.4    Yiotakis, A.5    Dive, V.6
  • 20
    • 33644945546 scopus 로고    scopus 로고
    • Crystal Structure of the N Domain of Human Somatic Angiotensin I-Converting Enzyme Provides a Structural Basis for Domain-Specific Inhibitor Design
    • Corradi, H. R.; Schwager, S. L. U.; Nchinda, A. T.; Sturrock, E. D.; Acharya, K. R. Crystal Structure of the N Domain of Human Somatic Angiotensin I-Converting Enzyme Provides a Structural Basis for Domain-Specific Inhibitor Design J. Mol. Biol. 2006, 357, 964-974
    • (2006) J. Mol. Biol. , vol.357 , pp. 964-974
    • Corradi, H.R.1    Schwager, S.L.U.2    Nchinda, A.T.3    Sturrock, E.D.4    Acharya, K.R.5
  • 21
    • 34547635443 scopus 로고    scopus 로고
    • Simulated Interactions between Angiotensin-Converting Enzyme and Substrate Gonadotropin-Releasing Hormone: Novel Insights into Domain Selectivity
    • Papakyriakou, A.; Spyroulias, G. A.; Sturrock, E. D.; Manessi-Zoupa, E.; Cordopatis, P. Simulated Interactions between Angiotensin-Converting Enzyme and Substrate Gonadotropin-Releasing Hormone: Novel Insights into Domain Selectivity Biochem. 2007, 46, 8753-8765
    • (2007) Biochem. , vol.46 , pp. 8753-8765
    • Papakyriakou, A.1    Spyroulias, G.A.2    Sturrock, E.D.3    Manessi-Zoupa, E.4    Cordopatis, P.5
  • 22
    • 79960262561 scopus 로고    scopus 로고
    • Inhibitor and Substrate Binding by Angiotensin-Converting Enzyme: Quantum Mechanical/Molecular Mechanical Molecular Dynamics Studies
    • Wang, X.; Wu, S.; Xu, D.; Xie, D.; Guo, H. Inhibitor and Substrate Binding by Angiotensin-Converting Enzyme: Quantum Mechanical/Molecular Mechanical Molecular Dynamics Studies J. Chem. Inf. Model. 2011, 51, 1074-1082
    • (2011) J. Chem. Inf. Model. , vol.51 , pp. 1074-1082
    • Wang, X.1    Wu, S.2    Xu, D.3    Xie, D.4    Guo, H.5
  • 24
    • 67650504166 scopus 로고    scopus 로고
    • Quantum Mechanical/Molecular Mechanical and Density Functional Theory Studies of a Prototypical Zinc Peptidase (Carboxypeptidase A) Suggest a General Acid-General Base Mechanism
    • Xu, D.; Guo, H. Quantum Mechanical/Molecular Mechanical and Density Functional Theory Studies of a Prototypical Zinc Peptidase (Carboxypeptidase A) Suggest a General Acid-General Base Mechanism J. Am. Chem. Soc. 2009, 131, 9780-9788
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 9780-9788
    • Xu, D.1    Guo, H.2
  • 25
    • 35948980030 scopus 로고    scopus 로고
    • Peptide Hydrolysis in Thermolysin; Ab Initio QM/MM Investigation of the Glu143-Assisted Water Addition Mechanism
    • Blumberger, J.; Lamoureux, G.; Klein, M. L. Peptide Hydrolysis in Thermolysin; Ab Initio QM/MM Investigation of the Glu143-Assisted Water Addition Mechanism J. Chem. Theor. Comput. 2007, 3, 1837-1850
    • (2007) J. Chem. Theor. Comput. , vol.3 , pp. 1837-1850
    • Blumberger, J.1    Lamoureux, G.2    Klein, M.L.3
  • 26
    • 0020678693 scopus 로고
    • Activation of Angiotensin Converting Enzyme by Monovalent Anions
    • Bunning, P.; Riordan, J. F. Activation of Angiotensin Converting Enzyme by Monovalent Anions Biochemistry 1983, 22, 110-116
    • (1983) Biochemistry , vol.22 , pp. 110-116
    • Bunning, P.1    Riordan, J.F.2
  • 27
    • 0020593991 scopus 로고
    • Anion Activation of Angiotensin Converting Enzyme: Dependence on Nature of Substrate
    • Shapiro, R.; Holmquist, B.; Riordan, J. F. Anion Activation of Angiotensin Converting Enzyme: Dependence on Nature of Substrate Biochem. 1983, 22, 3850-3857
    • (1983) Biochem. , vol.22 , pp. 3850-3857
    • Shapiro, R.1    Holmquist, B.2    Riordan, J.F.3
  • 28
    • 0027175193 scopus 로고
    • Differences in the Properties and Enzymatic Specificities of the Two Active Sites of Angiotensin I-Converting Enzyme (Kininase II)
    • Jaspard, E.; Wei, L.; Alhenc-Gelas, F. Differences in the Properties and Enzymatic Specificities of the Two Active Sites of Angiotensin I-Converting Enzyme (Kininase II) J. Biol. Chem. 1993, 268, 9496-9503
    • (1993) J. Biol. Chem. , vol.268 , pp. 9496-9503
    • Jaspard, E.1    Wei, L.2    Alhenc-Gelas, F.3
  • 29
    • 0035823581 scopus 로고    scopus 로고
    • Arg(1098) is Critical for the Chloride Dependence of Human Angiotensin I-Converting C-Domain Catalytic Activity
    • Liu, X.; Fernandez, A.; Wouters, M. A.; Heyberger, S.; Husain, A. Arg(1098) is Critical for the Chloride Dependence of Human Angiotensin I-Converting C-Domain Catalytic Activity J. Biol. Chem. 2001, 276, 33518-33525
    • (2001) J. Biol. Chem. , vol.276 , pp. 33518-33525
    • Liu, X.1    Fernandez, A.2    Wouters, M.A.3    Heyberger, S.4    Husain, A.5
  • 30
    • 0019332139 scopus 로고
    • Binding of Peptide Substrates and Inhibitors of Angiotensin-Converting Enzyme
    • Cheung, H.-S.; Wang, F.-L.; Ondetti, M. A.; Sabo, E. F.; Cushman, D. W. Binding of Peptide Substrates and Inhibitors of Angiotensin-Converting Enzyme J. Biol. Chem. 1980, 255, 401-407
    • (1980) J. Biol. Chem. , vol.255 , pp. 401-407
    • Cheung, H.-S.1    Wang, F.-L.2    Ondetti, M.A.3    Sabo, E.F.4    Cushman, D.W.5
  • 31
    • 0030148967 scopus 로고    scopus 로고
    • Hippuryl-L-Histidyl-L-leucine, a Substrate for Angiotensin Converting Enzyme
    • Vrielink, A.; Obel-Jorgensen, A.; Codding, P. W. Hippuryl-L-Histidyl-L- leucine, a Substrate for Angiotensin Converting Enzyme Acta Crystallogr. 1996, C52, 1300-1302
    • (1996) Acta Crystallogr. , vol.52 , pp. 1300-1302
    • Vrielink, A.1    Obel-Jorgensen, A.2    Codding, P.W.3
  • 32
    • 77954386602 scopus 로고    scopus 로고
    • High Resolution Crystal Structures of Drosophila melanogaster Angiotensin-Converting Enzyme in Complex with Novel Inhibitors and Antihypertensive Drugs
    • Akif, M.; Georgiadis, D.; Mahajan, A.; Dive, V.; Sturrock, E. D.; Isaac, R. E.; Acharya, K. R. High Resolution Crystal Structures of Drosophila melanogaster Angiotensin-Converting Enzyme in Complex with Novel Inhibitors and Antihypertensive Drugs J. Mol. Biol. 2010, 400, 502-517
    • (2010) J. Mol. Biol. , vol.400 , pp. 502-517
    • Akif, M.1    Georgiadis, D.2    Mahajan, A.3    Dive, V.4    Sturrock, E.D.5    Isaac, R.E.6    Acharya, K.R.7
  • 33
    • 0037434846 scopus 로고    scopus 로고
    • Crystal Structure of Drosophila Angiotensin I-Converting Enzyme Bound to Captopril and Lisinopril
    • Kim, H. M.; Shin, D. R.; Yoo, O. J.; Lee, H.; Lee, J. O. Crystal Structure of Drosophila Angiotensin I-Converting Enzyme Bound to Captopril and Lisinopril FEBS Lett. 2003, 538, 65-70
    • (2003) FEBS Lett. , vol.538 , pp. 65-70
    • Kim, H.M.1    Shin, D.R.2    Yoo, O.J.3    Lee, H.4    Lee, J.O.5
  • 34
    • 0017100947 scopus 로고
    • Theoretical Studies of Enzymatic Reactions: Dielectric, Electrostatic and Steric Stabilization of Carbonium Ion in the Reaction of Lysozyme
    • Warshel, A.; Levitt, M. Theoretical Studies of Enzymatic Reactions: Dielectric, Electrostatic and Steric Stabilization of Carbonium Ion in the Reaction of Lysozyme J. Mol. Biol. 1976, 103, 227-249
    • (1976) J. Mol. Biol. , vol.103 , pp. 227-249
    • Warshel, A.1    Levitt, M.2
  • 35
    • 84986513644 scopus 로고
    • A Combined Quantum Mechanical and Molecular Mechanical Potential for Molecular Dynamics Simulations
    • Field, M. J.; Bash, P. A.; Karplus, M. A Combined Quantum Mechanical and Molecular Mechanical Potential for Molecular Dynamics Simulations J. Comput. Chem. 1990, 11, 700-733
    • (1990) J. Comput. Chem. , vol.11 , pp. 700-733
    • Field, M.J.1    Bash, P.A.2    Karplus, M.3
  • 36
    • 84962367344 scopus 로고    scopus 로고
    • Methods and Applications of Combined Quantum Mechanical and Molecular Mechanical Potentials
    • Lipkowitz, K. B. Boyd, D. B. VCH: New York
    • Gao, J. Methods and Applications of Combined Quantum Mechanical and Molecular Mechanical Potentials. In Reviews in Computational Chemistry; Lipkowitz, K. B.; Boyd, D. B., Eds.; VCH: New York, 1996; Vol. 7, pp 119-185.
    • (1996) Reviews in Computational Chemistry , vol.7 , pp. 119-185
    • Gao, J.1
  • 37
    • 1542779956 scopus 로고    scopus 로고
    • Self-Consistent-Charge Density-Functional Tight-Binding Method for Simulations of Complex Materials Properties
    • Elstner, M.; Porezag, D.; Jungnickel, G.; Elsner, J.; Haugk, M.; Frauenheim, T.; Suhai, S.; Seigert, G. Self-Consistent-Charge Density-Functional Tight-Binding Method for Simulations of Complex Materials Properties Phys. Rev. 1998, B58, 7260-7268
    • (1998) Phys. Rev. , vol.58 , pp. 7260-7268
    • Elstner, M.1    Porezag, D.2    Jungnickel, G.3    Elsner, J.4    Haugk, M.5    Frauenheim, T.6    Suhai, S.7    Seigert, G.8
  • 38
    • 0033633272 scopus 로고    scopus 로고
    • A Self-Consistent Charge Density-Functional Based Tight-Binding Scheme for Large Biomolecules
    • Elstner, M.; Frauenheim, T.; Kaxiras, E.; Seifert, G.; Suhai, S. A Self-Consistent Charge Density-Functional Based Tight-Binding Scheme for Large Biomolecules Phys. Status Solidi 2000, B217, 357
    • (2000) Phys. Status Solidi , vol.217 , pp. 357
    • Elstner, M.1    Frauenheim, T.2    Kaxiras, E.3    Seifert, G.4    Suhai, S.5
  • 39
    • 0035138648 scopus 로고    scopus 로고
    • A QM/MM Implementation of the Self Consistent Charge Density Functional Tight Binding (SCC-DFTB) Method
    • Cui, Q.; Elstner, M.; Kaxiras, E.; Frauenheim, T.; Karplus, M. A QM/MM Implementation of the Self Consistent Charge Density Functional Tight Binding (SCC-DFTB) Method J. Phys. Chem. B 2001, 105, 569-585
    • (2001) J. Phys. Chem. B , vol.105 , pp. 569-585
    • Cui, Q.1    Elstner, M.2    Kaxiras, E.3    Frauenheim, T.4    Karplus, M.5
  • 40
    • 0141566583 scopus 로고    scopus 로고
    • Modeling Zinc in Biomolecules with the Self Consistent Charge Density Functional Tight Binding (SCC-DFTB) Method: Applications to Structure and Energetic Analysis
    • Elstner, M.; Cui, Q.; Munih, P.; Kaxiras, E.; Frauenheim, T.; Karplus, M. Modeling Zinc in Biomolecules with the Self Consistent Charge Density Functional Tight Binding (SCC-DFTB) Method: Applications to Structure and Energetic Analysis J. Comput. Chem. 2003, 24, 565
    • (2003) J. Comput. Chem. , vol.24 , pp. 565
    • Elstner, M.1    Cui, Q.2    Munih, P.3    Kaxiras, E.4    Frauenheim, T.5    Karplus, M.6
  • 42
    • 39749169756 scopus 로고    scopus 로고
    • Proton Transfer in Carbonic Anhydrase is Controlled by Electrostatics Rather Than Orientation of the Acceptor
    • Riccardi, D.; Konig, P.; Guo, H.; Cui, Q. Proton Transfer in Carbonic Anhydrase is Controlled by Electrostatics Rather Than Orientation of the Acceptor Biochemistry 2008, 47, 2369-2378
    • (2008) Biochemistry , vol.47 , pp. 2369-2378
    • Riccardi, D.1    Konig, P.2    Guo, H.3    Cui, Q.4
  • 43
    • 34547480925 scopus 로고    scopus 로고
    • PKa Analysis for the Zinc-Bound Water in Human Carbonic Anhydrase II: Benchmark for "multi-Scale" QM/MM Simulations and Mechanistic Implications
    • Riccardi, D.; Cui, Q. pKa Analysis for the Zinc-Bound Water in Human Carbonic Anhydrase II: Benchmark for "Multi-Scale" QM/MM Simulations and Mechanistic Implications J. Phys. Chem. A 2007, 111, 5703-5711
    • (2007) J. Phys. Chem. A , vol.111 , pp. 5703-5711
    • Riccardi, D.1    Cui, Q.2
  • 44
    • 80052206792 scopus 로고    scopus 로고
    • PH-Dependent Reactivity for Glycyl-l-tyrosine in Carboxypeptidase-A- Catalyzed Hydrolysis
    • Wu, S.; Zhang, C.; Xu, D.; Guo, H. pH-Dependent Reactivity for Glycyl-l-tyrosine in Carboxypeptidase-A-Catalyzed Hydrolysis J. Phys. Chem. B 2011, 115, 10360-10367
    • (2011) J. Phys. Chem. B , vol.115 , pp. 10360-10367
    • Wu, S.1    Zhang, C.2    Xu, D.3    Guo, H.4
  • 45
    • 34848849542 scopus 로고    scopus 로고
    • Antibiotic Deactivation by a Dizinc -Lactamase: Mechanistic Insights from QM/MM and DFT Studies
    • Xu, D.; Guo, H.; Cui, Q. Antibiotic Deactivation by a Dizinc -Lactamase: Mechanistic Insights from QM/MM and DFT Studies J. Am. Chem. Soc. 2007, 129, 10814-10822
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 10814-10822
    • Xu, D.1    Guo, H.2    Cui, Q.3
  • 46
    • 33646855255 scopus 로고    scopus 로고
    • Catalytic Mechanism of Class B2Metallo-β-Lactamase
    • Xu, D.; Xie, D.; Guo, H. Catalytic Mechanism of Class B2Metallo-β-Lactamase J. Biol. Chem. 2006, 281, 8740-8747
    • (2006) J. Biol. Chem. , vol.281 , pp. 8740-8747
    • Xu, D.1    Xie, D.2    Guo, H.3
  • 47
    • 78650620354 scopus 로고    scopus 로고
    • QM/MM Studies of Mono-Zinc Beta-Lactamase CphA Suggest that the Crystal Structure of an Enzyme-Intermediate Complex Represents a Minor Pathway
    • Wu, S.; Xu, D.; Guo, H. QM/MM Studies of Mono-Zinc Beta-Lactamase CphA Suggest that the Crystal Structure of an Enzyme-Intermediate Complex Represents a Minor Pathway J. Am. Chem. Soc. 2010, 132, 17986-17988
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 17986-17988
    • Wu, S.1    Xu, D.2    Guo, H.3
  • 50
    • 0022068152 scopus 로고
    • Active Site Dynamics in Protein Molecules: A Stochastic Boundary Molecular-Dynamics Approach
    • Brooks, C. L., III; Brunger, A.; Karplus, M. Active Site Dynamics in Protein Molecules: A Stochastic Boundary Molecular-Dynamics Approach Biopolymers 1985, 24, 843
    • (1985) Biopolymers , vol.24 , pp. 843
    • Brooks III, C.L.1    Brunger, A.2    Karplus, M.3
  • 51
    • 84986534166 scopus 로고
    • New Spherical-Cutoff Methods for Long-Range Forces in Macromolecular Simulations
    • Steinbach, P. J.; Brooks, B. R. New Spherical-Cutoff Methods for Long-Range Forces in Macromolecular Simulations J. Comput. Chem. 1994, 15, 667
    • (1994) J. Comput. Chem. , vol.15 , pp. 667
    • Steinbach, P.J.1    Brooks, B.R.2
  • 53
    • 0342929614 scopus 로고
    • Non-Physical Sampling Distributions in Monte Carlo Free Energy Estimation: Umbrella Sampling
    • Torrie, G. M.; Valleau, J. P. Non-Physical Sampling Distributions in Monte Carlo Free Energy Estimation: Umbrella Sampling J. Comput. Phys. 1977, 23, 187-199
    • (1977) J. Comput. Phys. , vol.23 , pp. 187-199
    • Torrie, G.M.1    Valleau, J.P.2
  • 54
    • 84986519238 scopus 로고
    • The Weighted Histogram Analysis Method for Free Energy Calculations on Biomolecules. 1. The Method
    • Kumar, S.; Bouzida, D.; Swendsen, R. H.; Kollman, P. A.; Rosenberg, J. M. The Weighted Histogram Analysis Method for Free Energy Calculations on Biomolecules. 1. The Method J. Comput. Chem. 1992, 13, 1011-1021
    • (1992) J. Comput. Chem. , vol.13 , pp. 1011-1021
    • Kumar, S.1    Bouzida, D.2    Swendsen, R.H.3    Kollman, P.A.4    Rosenberg, J.M.5
  • 55
    • 33646940952 scopus 로고
    • Numerical Integration of the Cartesian of Motion of a System with Constraints: Molecular Dynamics of n -Alkanes
    • Ryckaert, J.-P.; Ciccotti, G.; Berendsen, H. J. C. Numerical Integration of the Cartesian of Motion of a System with Constraints: Molecular Dynamics of n -Alkanes J. Comput. Phys. 1977, 23, 327-341
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 56
    • 0037087047 scopus 로고    scopus 로고
    • Performance of the Am1, PM3, and SCC-DFTB Methods in the Study of Conjugated Schiff Base Molecules
    • Zhou, H.; Tajkhorshid, E.; Frauenheim, T.; Suhai, S.; Elstner, M. Performance of the Am1, PM3, and SCC-DFTB Methods in the Study of Conjugated Schiff Base Molecules Chem. Phys. 2002, 277, 91-103
    • (2002) Chem. Phys. , vol.277 , pp. 91-103
    • Zhou, H.1    Tajkhorshid, E.2    Frauenheim, T.3    Suhai, S.4    Elstner, M.5
  • 57
    • 78549236130 scopus 로고    scopus 로고
    • Accurate Proton Affinity and Gas-Phase Basicity Values for Molecules Importance in Biocatalysis
    • Moser, A.; Range, K.; York, D. M. Accurate Proton Affinity and Gas-Phase Basicity Values for Molecules Importance in Biocatalysis J. Phys. Chem. B 2010, 114, 13911-13921
    • (2010) J. Phys. Chem. B , vol.114 , pp. 13911-13921
    • Moser, A.1    Range, K.2    York, D.M.3
  • 58
    • 7744244599 scopus 로고    scopus 로고
    • Recent Advances in Zinc Enzymology
    • Lipscomb, W. M.; Strater, N. Recent Advances in Zinc Enzymology Chem. Rev. 1996, 96, 2375-2433
    • (1996) Chem. Rev. , vol.96 , pp. 2375-2433
    • Lipscomb, W.M.1    Strater, N.2
  • 59
    • 34547414525 scopus 로고    scopus 로고
    • Exploring SCC-DFTB Paths for Mapping QM/MM Reaction Mechanisms
    • Woodcock, H. L.; Hodoscek, M.; Brooks, B. R. Exploring SCC-DFTB Paths for Mapping QM/MM Reaction Mechanisms J. Phys. Chem. A 2007, 111, 5720-5728
    • (2007) J. Phys. Chem. A , vol.111 , pp. 5720-5728
    • Woodcock, H.L.1    Hodoscek, M.2    Brooks, B.R.3
  • 60
    • 0000231955 scopus 로고
    • Conjugate Peak Refinement: An Algorithm for Finding Reaction Paths and Accurate Transition State in Systems with Many Degrees of Freedom
    • Fischer, S.; Karplus, M. Conjugate Peak Refinement: an Algorithm for Finding Reaction Paths and Accurate Transition State in Systems with Many Degrees of Freedom Chem. Phys. Lett. 1992, 194, 252-261
    • (1992) Chem. Phys. Lett. , vol.194 , pp. 252-261
    • Fischer, S.1    Karplus, M.2
  • 61
    • 84961973449 scopus 로고    scopus 로고
    • Minimum Energy Pathways for Proton Transfer between Adjacent Sites Exposed to Water
    • Friedman, R.; Fischer, S.; Nachliel, E.; Scheiner, S.; Gutman, M. Minimum Energy Pathways for Proton Transfer between Adjacent Sites Exposed to Water J. Phys. Chem. B 2007, 111, 6059-6070
    • (2007) J. Phys. Chem. B , vol.111 , pp. 6059-6070
    • Friedman, R.1    Fischer, S.2    Nachliel, E.3    Scheiner, S.4    Gutman, M.5
  • 62
    • 0021744255 scopus 로고
    • An Interactive Computer Graphics Study of Thermolysin-Catalyzed Peptide Cleavage and Inhibition by N-Carboxymethyl Dipeptides
    • Hangauer, D. G.; Mozingo, A. F.; Matthews, B. W. An Interactive Computer Graphics Study of Thermolysin-Catalyzed Peptide Cleavage and Inhibition by N-Carboxymethyl Dipeptides Biochem 1984, 23, 5730-5741
    • (1984) Biochem , vol.23 , pp. 5730-5741
    • Hangauer, D.G.1    Mozingo, A.F.2    Matthews, B.W.3
  • 63
    • 0027970068 scopus 로고
    • Identification of Two Active Site Residues in Human Angiotensin I-converting Enzyme
    • Williams, T. A.; Corvol, P.; Soubrier, F. Identification of Two Active Site Residues in Human Angiotensin I-converting Enzyme J. Biol. Chem. 1994, 269, 29430-29434
    • (1994) J. Biol. Chem. , vol.269 , pp. 29430-29434
    • Williams, T.A.1    Corvol, P.2    Soubrier, F.3
  • 64
    • 84874167691 scopus 로고    scopus 로고
    • Charging Free Energy Calculations Using the Generalized Solvent Boundary Potential (GSBP) and Periodic Boundary Condition: A Comparative Analysis Using Ion Solvation and Oxidation Free Energy in Proteins
    • Lu, X.; Cui, Q. Charging Free Energy Calculations Using the Generalized Solvent Boundary Potential (GSBP) and Periodic Boundary Condition: A Comparative Analysis Using Ion Solvation and Oxidation Free Energy in Proteins J. Phys. Chem. B 2013, 117, 2005-2018
    • (2013) J. Phys. Chem. B , vol.117 , pp. 2005-2018
    • Lu, X.1    Cui, Q.2
  • 65
    • 34548059996 scopus 로고    scopus 로고
    • Reliable Treatment of Electrostatics in Combined QM/MM Simulation of Macromolecules
    • Schaefer, P.; Riccardi, D.; Cui, Q. Reliable Treatment of Electrostatics in Combined QM/MM Simulation of Macromolecules J. Chem. Phys. 2005, 123, 014905
    • (2005) J. Chem. Phys. , vol.123 , pp. 014905
    • Schaefer, P.1    Riccardi, D.2    Cui, Q.3
  • 66
    • 0031167555 scopus 로고    scopus 로고
    • Atomic Raddi for Continuum Electrostatics Calculations Based on Molecular Dynamics Free Energy Simulations
    • Nina, M.; Beglov, D.; Roux, B. Atomic Raddi for Continuum Electrostatics Calculations Based on Molecular Dynamics Free Energy Simulations J. Phys. Chem. B 1997, 101, 5239-5248
    • (1997) J. Phys. Chem. B , vol.101 , pp. 5239-5248
    • Nina, M.1    Beglov, D.2    Roux, B.3
  • 67
    • 0003464216 scopus 로고    scopus 로고
    • NIST Standard Reference Database Number 69
    • Standard Reference Data Program: Gaithersbug, MD
    • Linstrom, P.; Mallard, W. NIST Chemistry WebBook, NIST Standard Reference Database Number 69; Standard Reference Data Program: Gaithersbug, MD, 2003.
    • (2003) NIST Chemistry WebBook
    • Linstrom, P.1    Mallard, W.2


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