Effect of dielectric medium on angiotensin converting enzyme inhibitors binding to Zn2+

[1] Andújar-Sánchez, M., Cámara-Artigas, A., & Jara-Pérez, V. (2004). A calorimetric study of the binding of lisinopril, enalaprilat and captopril to angiotensin-converting enzyme. Biophysical Chemistry, 111, 183–189. DOI: 10.1016/j.bpc.2004.05.011. http://dx.doi.org/10.1016/j.bpc.2004.05.01110.1016/j.bpc.2004.05.011Suche in Google Scholar PubMed

[2] Barone, V., & Cossi, M. (1998). Quantum calculation of molecular energies and energy gradients in solution by a conductor solvent model. The Journal of Physical Chemistry A, 102, 1995–2001. DOI: 10.1021/jp9716997. http://dx.doi.org/10.1021/jp971699710.1021/jp9716997Suche in Google Scholar

[3] Barone, V., Cossi, M., & Tomasi, J. (1997). A new definition of cavities for the computation of solvation free energies by the polarizable continuum model. The Journal of Chemical Physics, 107, 3210–3221. DOI: 10.1063/1.474671. http://dx.doi.org/10.1063/1.47467110.1063/1.474671Suche in Google Scholar

[4] Becke, A. D. (1993). Density-functional thermochemistry. III. The role of exact exchange. The Journal of Chemical Physics, 98, 5648–5652. DOI: 10.1063/1.464913. http://dx.doi.org/10.1063/1.46491310.1063/1.464913Suche in Google Scholar

[5] Becke, A. D. (1988). Density-functional exchange-energy approximation with correct asymptotic behaviour. Physical Review A, 38, 3098–3100. DOI: 10.1103/PhysRevA.38.3098. http://dx.doi.org/10.1103/PhysRevA.38.309810.1103/PhysRevA.38.3098Suche in Google Scholar

[6] Berman, H., Henrick, K., & Nakamura, H. (2003). Announcing the worldwide Protein Data Bank. Nature Structural Biology, 10, 980. DOI: 10.1038/nsb1203-980. http://dx.doi.org/10.1038/nsb1203-98010.1038/nsb1203-980Suche in Google Scholar PubMed

[7] Bock, C. W., Katz, A. K., & Glusker, J. P. (1995). Hydration of zinc ions: A comparison with magnesium and beryllium ions. Journal of the American Chemical Society, 117, 3754–3765. DOI: 10.1021/ja00118a012. http://dx.doi.org/10.1021/ja00118a01210.1021/ja00118a012Suche in Google Scholar

[8] Bock, C. W., Katz, A. K., Markham, G. D., & Glusker, J. P. (1999). Manganese as a replacement for magnesium and zinc: Functional comparison of the divalent ions. Journal of the American Chemical Society, 121, 7360–7372. DOI: 10.1021/ja9906960. http://dx.doi.org/10.1021/ja990696010.1021/ja9906960Suche in Google Scholar

[9] Cheng, F., Zhang, R., Luo, X., Shen, J., Li, X., Gu, J., Zhu, W., Shen, J., Sagi, I., Ji, R., Chen, K., & Jiang, H. (2002). Quantum chemistry study on the interaction of the exogenous ligands and the catalytic zinc ion in matrix metalloproteinases. The Journal of Physical Chemistry B, 106, 4552–4559. DOI: 10.1021/jp013336j. http://dx.doi.org/10.1021/jp013336j10.1021/jp013336jSuche in Google Scholar

[10] Cini, R. (1999). Molecular orbital study of complexes of zinc(II) with sulphide, thiomethanolate, thiomethanol, dimethylthioether, thiophenolate, formiate, acetate, carbonate, hydrogen carbonate, iminomethane and imidazole: Relationships with structural and catalytic zinc in some metallo-enzymes. Journal of Biomolecular Structure and Dynamics, 16, 1225–1237. 10.1080/07391102.1999.10508330Suche in Google Scholar PubMed

[11] Corradi, H. R., Chitapi, I., Sewell, B. T., Georgiadis, D., Dive, V., Sturrock, E. D., & Acharya, K. R. (2007). The structure of testis angiotensin-converting enzyme in complex with the C domain-specific inhibitor RXPA380. Biochemistry, 46, 5473–5478. DOI: 10.1021/bi700275e. http://dx.doi.org/10.1021/bi700275e10.1021/bi700275eSuche in Google Scholar

[12] Corradi, H. R., Schwager, S. L. U., Nchinda, A. T., Sturrock, E. D., & Acharya, K. R. (2006). Crystal structure of the N domain of human somatic angiotensin I-converting enzyme provides a structural basis for domain-specific inhibitor design. Journal of Molecular Biology, 357, 964–974. DOI: 10.1016/j.jmb.2006.01.048. http://dx.doi.org/10.1016/j.jmb.2006.01.04810.1016/j.jmb.2006.01.048Suche in Google Scholar

[13] Deerfield, D. W., Carter, C. W., Jr., & Pedersen, L. G. (2001). Models for protein-zinc ion binding sites. II: The catalytic sites. International Journal of Quantum Chemistry, 83, 150–165. DOI: 10.1002/qua.1207. http://dx.doi.org/10.1002/qua.120710.1002/qua.1207Suche in Google Scholar

[14] Dudev, T., & Lim, C. (2003). Principles governing Mg, Ca, and Zn binding and selectivity in proteins. Chemical Reviews, 103, 773–788. DOI: 10.1021/cr020467n. http://dx.doi.org/10.1021/cr020467n10.1021/cr020467nSuche in Google Scholar

[15] Dudev, T., & Lim, C. (2000a). Tetrahedral vs octahedral zinc complexes with ligands of biological interest: A DFT/CDM study. Journal of the American Chemical Society, 122, 11146–11153. DOI: 10.1021/ja0010296. http://dx.doi.org/10.1021/ja001029610.1021/ja0010296Suche in Google Scholar

[16] Dudev, T., & Lim, C. (2000b). Metal binding in proteins: The effect of the dielectric medium. The Journal of Physical Chemistry B, 104, 3692–3694. DOI: 10.1021/jp9941559. http://dx.doi.org/10.1021/jp994155910.1021/jp9941559Suche in Google Scholar

[17] Fernandez, M., Liu, X., Wouters, M. A., Heyberger, S., & Husain, A. (2001). Angiotensin I-converting enzyme transition state stabilization by His1089. Evidence for a catalytic mechanism distinct from other gluzincin metalloproteinases. The Journal of Biological Chemistry, 276, 4998–5004. DOI: 10.1074/jbc.M009009200. http://dx.doi.org/10.1074/jbc.M00900920010.1074/jbc.M009009200Suche in Google Scholar

[18] Frisch, M. J., Trucks, G. W., Schlegel, H. B., Scuseria, G. E., Robb, M. A., Cheeseman, J. R., Montgomery, J. A., Jr., Vreven, T., Kudin, K. N., Burant, J. C., Millam, J. M., Iyengar, S. S., Tomasi, J., Barone, V., Mennucci, B., Cossi, M., Scalmani, G., Rega, N., Petersson, G. A., Nakatsuji, H., Hada, M., Ehara, M., Toyota, K., Fukuda, R., Hasegawa, J., Ishida, M., Nakajima, T., Honda, Y., Kitao, O., Nakai, H., Klene, M., Li, X., Knox, J. E., Hratchian, H. P., Cross, J. B., Bakken, V., Adamo, C., Jaramillo, J., Gomperts, R., Stratmann, R. E., Yazyev, O., Austin, A. J., Cammi, R., Pomelli, C., Ochterski, J. W., Ayala, P. Y., Morokuma, K., Voth, G. A., Salvador, P., Dannenberg, J. J., Zakrzewski, V. G., Dapprich, S., Daniels, A. D., Strain, M. C., Farkas, O., Malick, D. K., Rabuck, A. D., Raghavachari, K., Foresman, J. B., Ortiz, J. V., Cui, Q., Baboul, A. G., Clifford, S., Cioslowski, J., Stefanov, B. B., Liu, G., Liashenko, A., Piskorz, P., Komaromi, I., Martin, R. L., Fox, D. J., Keith, T., Al-Laham, M. A., Peng, C. Y., Nanayakkara, A., Challacombe, M., Gill, P. M. W., Johnson, B., Chen, W., Wong, M. W., Gonzalez, C., & Pople, J. A. (2004). Gaussian 03, Revision D.01. Wallingford, CT, USA: Gaussian, Inc. Suche in Google Scholar

[19] Garmer, D. R., Gresh, N., & Roques, B.-P. (1998). Modeling of inhibitor-metalloenzyme interactions and selectivity using molecular mechanics grounded in quantum chemistry. Proteins: Structure, Function, and Genetics, 31, 42–60. DOI: 10.1002/(SICI)1097-0134(19980401)31:1〈42. http://dx.doi.org/10.1002/(SICI)1097-0134(19980401)31:1<42::AID-PROT5>3.0.CO;2-J10.1002/(SICI)1097-0134(19980401)31:1<42::AID-PROT5>3.0.CO;2-JSuche in Google Scholar

[20] Gilson, M. K., & Honig, B. H. (1986). The dielectric constant of a folded protein. Biopolymers, 25, 2097–2119. DOI: 10.1002/bip.360251106. http://dx.doi.org/10.1002/bip.36025110610.1002/bip.360251106Suche in Google Scholar

[21] Hartmann, M., Clark, T., & van Eldik, R. (1997). Hydration and water exchange of zinc(II) ions. Application of density functional theory. Journal of the American Chemical Society, 119, 7843–7850. DOI: 10.1021/ja970483f. 10.1021/ja970483fSuche in Google Scholar

[22] Hasegawa, K., Ono, T.-a., & Noguchi, T. (2002). Ab initio density functional theory calculations and vibrational analysis of zinc-bound 4-methylimidazole as a model of a histidine ligand in metalloenzymes. The Journal of Physical Chemistry A, 106, 3377–3390. DOI: 10.1021/jp012251f. http://dx.doi.org/10.1021/jp012251f10.1021/jp012251fSuche in Google Scholar

[23] James, M. N. G., & Sielecki, A. R. (1983). Structure and refinement of penicillopepsin at 1.8 Å resolution. Journal of Molecular Biology, 163, 299–361. DOI: 10.1016/0022-2836(83)90008-6. http://dx.doi.org/10.1016/0022-2836(83)90008-610.1016/0022-2836(83)90008-6Suche in Google Scholar

[24] Karplus, M., McCammon, J. A., & Peticolas, W. L. (1981). The internal dynamics of globular proteins. Critical Reviews in Biochemistry and Molecular Biology, 9, 293–349. DOI: 10.3109/10409238109105437. http://dx.doi.org/10.3109/1040923810910543710.3109/10409238109105437Suche in Google Scholar PubMed

[25] Katz, A. K., Glusker, J. P., Beebe, S. A., & Bock, C. W. (1996). Calcium ion coordination: A comparison with that of beryllium, magnesium, and zinc. Journal of the American Chemical Society, 118, 5752–5763. DOI: 10.1021/ja953943i. http://dx.doi.org/10.1021/ja953943i10.1021/ja953943iSuche in Google Scholar

[26] Kimura, E. (2001). Model studies for molecular recognition of carbonic anhydrase and carboxypeptidase. Accounts of Chemical Research, 34, 171–179. DOI: 10.1021/ar000001w. http://dx.doi.org/10.1021/ar000001w10.1021/ar000001wSuche in Google Scholar PubMed

[27] Lee, C., Yang, W., & Paar, R. G. (1988). Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density. Physical Review B, 37, 785–789. DOI: 10.1103/PhysRevB.37.785. http://dx.doi.org/10.1103/PhysRevB.37.78510.1103/PhysRevB.37.785Suche in Google Scholar

[28] Lee, S., Kim, J., Park, J. K., & Kim, K. S. (1996). Ab initio study of the structures, energetics, and spectra of Aquazinc(II). The Journal of Physical Chemistry, 100, 14329–14338. DOI: 10.1021/jp960714p. http://dx.doi.org/10.1021/jp960714p10.1021/jp960714pSuche in Google Scholar

[29] McCall, K. A., Huang, C.-c., & Fierke, C. A. (2000). Function and mechanism of zinc metalloenzymes. Journal of Nutrition, 130, 1437S–1446S. 10.1093/jn/130.5.1437SSuche in Google Scholar PubMed

[30] Menziani, M. C., De Benedetti, P. G., Gago, F., & Richards, W. G. (1989). The binding of benzenesulfonamides to carbonic anhydrase enzyme. A molecular mechanics study and quantitative structure-activity relationships. Journal of Medicinal Chemistry, 32, 951–956. DOI: 10.1021/jm00125a005. http://dx.doi.org/10.1021/jm00125a00510.1021/jm00125a005Suche in Google Scholar PubMed

[31] Mertz, E. L., & Krishtalik, L. I. (2000). Low dielectric response in enzyme active site. Proceedings of the National Academy of Sciences of the USA, 97, 2081–2086. DOI: 10.1073/pnas.050316997. http://dx.doi.org/10.1073/pnas.05031699710.1073/pnas.050316997Suche in Google Scholar PubMed PubMed Central

[32] Nakamura, H., Sakamoto, T., & Wada, A. (1988). A theoretical study of the dielectric constant of protein. Protein Engineering, 2, 177–183. DOI: 10.1093/protein/2.3.177. http://dx.doi.org/10.1093/protein/2.3.17710.1093/protein/2.3.177Suche in Google Scholar PubMed

[33] Natesh, R., Schwager, S. L. U., Evans, H. R., Sturrock, E. D., & Acharya, K. R. (2004). Structural details on the binding of antihypertensive drugs captopril and enalaprilat to human testicular angiotensin I-converting enzyme. Biochemistry, 43, 8718–8724. DOI: 10.1021/bi049480n. http://dx.doi.org/10.1021/bi049480n10.1021/bi049480nSuche in Google Scholar PubMed

[34] Natesh, R., Schwager, S. L. U., Sturrock, E. D., & Acharya, K. R. (2003). Crystal structure of the human angiotensinconverting enzyme-lisinopril complex. Nature, 421, 551–554. DOI: 10.1038/nature01370. http://dx.doi.org/10.1038/nature0137010.1038/nature01370Suche in Google Scholar PubMed

[35] Nchinda, A. T., Chibale, K., Redelinghuys, P., & Sturrock, E. D. (2006). Synthesis of novel keto-ACE analogues as domain-selective angiotensin-I converting enzyme inhibitors. Bioorganic & Medicinal Chemistry Letters, 16, 4612–4615. DOI: 10.1016/j.bmcl.2006.06.003. http://dx.doi.org/10.1016/j.bmcl.2006.06.00310.1016/j.bmcl.2006.06.003Suche in Google Scholar PubMed

[36] Opie, L. H. (1994). Angiotensin converting enzyme inhibitors (2nd ed.). New York, NY, USA: Wiley-Liss. Suche in Google Scholar

[37] Pavlov, M., Siegbahn, P. E. M., & Sandström, M. (1998). Hydration of beryllium, magnesium, calcium, and zinc ions using density functional theory. The Journal of Physical Chemistry A, 102, 219–228. DOI: 10.1021/jp972072r. http://dx.doi.org/10.1021/jp972072r10.1021/jp972072rSuche in Google Scholar

[38] Peschke, M., Blades, A. T., & Kebarle, P. (2000). Binding energies for doubly-charged ions M2+ = Mg2+, Ca2+ and Zn2+ with the ligands L = H2O, acetone and N-methylacetamide in complexes: M L n2+ for n = 1 to 7 from gas phase equilibria determinations and theoretical calculations. Journal of the American Chemical Society, 122, 10440–10449. DOI: 10.1021/ja002021z. http://dx.doi.org/10.1021/ja002021z10.1021/ja002021zSuche in Google Scholar

[39] Pethig, R. (1979). Dielectric and electronic properties of biological materials. New York, NY, USA: Wiley. Suche in Google Scholar

[40] Redelinghuys, P., Nchinda, A. T., & Sturrock, E. D. (2005). Development of domain-selective angiotensin I-converting enzyme inhibitors. Annals of the New York Academy of Sciences, 1056, 160–175. DOI: 10.1196/annals.1352.035. http://dx.doi.org/10.1196/annals.1352.03510.1196/annals.1352.035Suche in Google Scholar PubMed

[41] Remko, M. (2007). Acidity, lipophilicity, solubility, absorption, and polar surface area of some ACE inhibitors. Chemical Papers, 61, 133–141. DOI: 10.2478/s11696-007-0010-y. http://dx.doi.org/10.2478/s11696-007-0010-y10.2478/s11696-007-0010-ySuche in Google Scholar

[42] Remko, M., & Garaj, V. (2003). Thermodynamics of binding of Zn2+ to carbonic anhydrase inhibitors. Molecular Physics, 101, 2357–2368. DOI: 10.1080/0026897031000716583. http://dx.doi.org/10.1080/002689703100071658310.1080/0026897031000716583Suche in Google Scholar

[43] Remko, M., & Rode, B. M. (2006). Effect of metal ions (Li+, Na+, K+, Mg2+, Ca2+, Ni2+, Cu2+, and Zn2+) and water coordination on the structure of glycine and zwitterionic glycine. The Journal of Physical Chemistry A, 110, 1960–1967. DOI: 10.1021/jp054119b. http://dx.doi.org/10.1021/jp054119b10.1021/jp054119bSuche in Google Scholar PubMed

[44] Remko, M., & Rode, B. M. (2000). Thermodynamics of binding of Li+, Na+, Mg2+ and Zn2+ to Lewis bases in the gas phase. Journal of Molecular Structure: Theochem, 505, 269–281. DOI: 10.1016/S0166-1280(99)00381-4. http://dx.doi.org/10.1016/S0166-1280(99)00381-410.1016/S0166-1280(99)00381-4Suche in Google Scholar

[45] Rogalewicz, F., Ohanessian, G., & Gresh, N. (2000). Interaction of neutral and zwitterionic glycine with Zn2+ in gas phase: ab initio and SIBFA molecular mechanics calculations. Journal of Computational Chemistry, 21, 963–973. DOI: 10.1002/1096-987X(200008)21:11〈963::AIDJCC6〉3.0.CO;2–3. http://dx.doi.org/10.1002/1096-987X(200008)21:11<963::AID-JCC6>3.0.CO;2-310.1002/1096-987X(200008)21:11<963::AID-JCC6>3.0.CO;2-3Suche in Google Scholar

[46] Ryde, U. (1999). Carboxylate binding modes in zinc proteins: A theoretical study. Biophysical Journal, 77, 2777–2787. DOI: 10.1016/S0006-3495(99)77110-9. http://dx.doi.org/10.1016/S0006-3495(99)77110-910.1016/S0006-3495(99)77110-9Suche in Google Scholar

[47] Simonson, T., & Perahia, D. (1995). Internal and interfacial dielectric properties of cytochrome c from molecular dynamics in aqueous solution. Proceedings of the National Academy of Sciences of the USA, 92, 1082–1086. http://dx.doi.org/10.1073/pnas.92.4.108210.1073/pnas.92.4.1082Suche in Google Scholar

[48] Smieško, M., & Remko, M. (2005). Structure and gas-phase stability of Zn(II)—molecule complexes. Chemical Papers, 59, 310–315. Suche in Google Scholar

[49] Smieško, M., & Remko, M. (2004). Two-layer ONIOM calculation of gas-phase acidities of selected ACE inhibitors. Chemical Papers, 58, 71–78. Suche in Google Scholar

[50] Smieško, M., & Remko, M. (2003). Coordination and thermodynamics of stable Zn(II) complexes in the gas phase. Journal of Biomolecular Structure and Dynamics, 20, 759–770. 10.1080/07391102.2003.10506893Suche in Google Scholar

[51] Smieško, M., & Remko, M. (2002). Preferred conformation of selected ACE inhibitors for interaction with ACE active site. Chemical Papers, 56, 138–143. Suche in Google Scholar

[52] Smith, P. E., Brunne, R. M., Mark, A. E., & van Gunsteren, W. F. (1993). Dielectric properties of trypsin inhibitor and lysozyme calculated from molecular dynamics simulations. The Journal of Physical Chemistry, 97, 2009–2014. DOI: 10.1021/j100111a046. http://dx.doi.org/10.1021/j100111a04610.1021/j100111a046Suche in Google Scholar

[53] Spyroulias, G. A., & Cordopatis, P. (2005). Current inhibition concepts of zinc metallopeptidases involved in blood pressure regulation. Current Enzyme Inhibition, 1, 29–42. DOI: 10.2174/1573408052952702. http://dx.doi.org/10.2174/157340805295270210.2174/1573408052952702Suche in Google Scholar

[54] Šramko, M., Garaj, V., & Remko, M. (2008). Thermodynamics of binding of angiotensin-converting enzyme inhibitors to enzyme active site model. Journal of Molecular Structure: Theochem, 869, 19–28. DOI: 10.1016/j.theochem.2008.08.018. http://dx.doi.org/10.1016/j.theochem.2008.08.01810.1016/j.theochem.2008.08.018Suche in Google Scholar

[55] Šramko, M., Remko, M., & Garaj, V. (2005). Theoretical study of gas-phase acidities of selected angiotensin-converting enzyme inhibitors. Structural Chemistry, 16, 391–399. DOI: 10.1007/s11224-005-6348-2. http://dx.doi.org/10.1007/s11224-005-6348-210.1007/s11224-005-6348-2Suche in Google Scholar

[56] Strömberg, D., Sandström, M., & Wahlgren, U. (1990). Theoretical calculations on the structure of the hexahydrated divalent zinc, cadmium and mercury ions. Chemical Physics Letters, 172, 49–54. DOI: 10.1016/0009-2614(90)87215-D. http://dx.doi.org/10.1016/0009-2614(90)87215-D10.1016/0009-2614(90)87215-DSuche in Google Scholar

[57] Swamy, K. M. K., Lin, M.-J., & Sun, C.-M. (2003). Advances in angiotensin converting enzyme inhibitors (ACEIs) and angiotensin receptor blockers (ARBs). Mini-Reviews in Medicinal Chemistry, 3, 621–631. DOI: 10.2174/1389557033487944. http://dx.doi.org/10.2174/138955703348794410.2174/1389557033487944Suche in Google Scholar

[58] Tanaka, A., & Ishida, Y. (1973). Relation between dielectric behavior and structure in some solid polypeptides. Journal of Polymer Science: Polymer Physics Edition, 11, 1117–1138. DOI: 10.1002/pol.1973.180110607. http://dx.doi.org/10.1002/pol.1973.18011100410.1002/pol.1973.180110607Suche in Google Scholar

[59] Tiraboschi, G., Fournié-Zaluski, M.-C., Roques, B.-P., & Gresh, N. (2001). Intramolecular chelation of Zn2+ by α- and β-mercaptocarboxamides. A parallel ab initio and polarizable molecular mechanics investigation. Assessment of the role of multipole transferability. Journal of Computational Chemistry, 22, 1038–1047. DOI: 10.1002/jcc.1064. http://dx.doi.org/10.1002/jcc.106410.1002/jcc.1064Suche in Google Scholar

[60] Tiraboschi, G., Gresh, N., Giessner-Prettre, C., Pedersen, L. G., & Deerfield, D. W. (2000). Parallel ab initio and molecular mechanics investigation of polycoordinated Zn(II) complexes with model hard and soft ligands: Variations of the binding energy and of its components with number and charges of ligands. Journal of Computational Chemistry, 21, 1011–1039. DOI: 10.1002/1096-987X(200009)21:12〈1011. http://dx.doi.org/10.1002/1096-987X(200009)21:12<1011::AID-JCC1>3.0.CO;2-B10.1002/1096-987X(200009)21:12<1011::AID-JCC1>3.0.CO;2-BSuche in Google Scholar

[61] Wyvratt, M. J., & Patchett, A. A. (1985). Recent developments in the design of angiotensin-converting enzyme inhibitors. Medicinal Research Reviews, 5, 483–531. DOI: 10.1002/med.2610050405. http://dx.doi.org/10.1002/med.261005040510.1002/med.2610050405Suche in Google Scholar

[62] Yazal, J. E., & Pang, Y.-P. (2000). Proton dissociation energies of zinc-coordinated hydroxamic acids and their relative affinities for zinc: Insights into design inhibitors of zinccontaining proteinases. The Journal of Physical Chemistry B, 104, 6499–6504. DOI: 10.1021/jp0012707. http://dx.doi.org/10.1021/jp001270710.1021/jp0012707Suche in Google Scholar

[63] Yazal, J. E., & Pang, Y.-P. (1999). Ab initio calculations of proton dissociation energies of zinc ligands: Hypothesis of imidazolate as zinc ligand in proteins. The Journal of Physical Chemistry B, 103, 8773–8779. DOI: 10.1021/jp991787m. http://dx.doi.org/10.1021/jp991787m10.1021/jp991787mSuche in Google Scholar

[64] Yazal, J. E., Roe, R. R., & Pang, Y.-P. (2000). Zincșs affect on proton transfer between imidazole and acetate predicted by ab initio calculations. The Journal of Physical Chemistry B, 104, 6662–6667. DOI: 10.1021/jp994283x. http://dx.doi.org/10.1021/jp994283x10.1021/jp994283xSuche in Google Scholar