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Volumn 110, Issue 28, 2013, Pages

Quantitative dissection of hydrogen bond-mediated proton transfer in the ketosteroid isomerase active site

Author keywords

Active site environment; Computational modeling; Enzyme catalysis; Protein electrostatics; Protein semisynthesis

Indexed keywords

ANION; PHENOL; STEROID DELTA ISOMERASE; TYROSINE;

EID: 84879908394     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1302191110     Document Type: Article
Times cited : (38)

References (62)
  • 3
    • 0036099192 scopus 로고    scopus 로고
    • a) values of buried residues: Analysis with continuum methods and role of water penetration
    • a) values of buried residues: Analysis with continuum methods and role of water penetration. Biophys J 82(6):3289-3304.
    • (2002) Biophys J , vol.82 , Issue.6 , pp. 3289-3304
    • Fitch, C.A.1
  • 5
    • 33947683393 scopus 로고    scopus 로고
    • High apparent dielectric constant inside a protein reflects structural reorganization coupled to the ionization of an internal Asp
    • DOI 10.1529/biophysj.106.090266
    • Karp DA, et al. (2007) High apparent dielectric constant inside a protein reflects structural reorganization coupled to the ionization of an internal Asp. Biophys J 92(6):2041-2053. (Pubitemid 46495267)
    • (2007) Biophysical Journal , vol.92 , Issue.6 , pp. 2041-2053
    • Karp, D.A.1    Gittis, A.G.2    Stahley, M.R.3    Fitch, C.A.4    Stites, W.E.5    Garcia-Moreno, E.B.6
  • 6
    • 0032512414 scopus 로고    scopus 로고
    • 5-steroid isomerase. A probe for the nature of hydrogen bonding to the intermediate
    • DOI 10.1021/bi972262s
    • Petrounia IP, Pollack RM (1998) Substituent effects on the binding of phenols to the D38N mutant of 3-oxo-delta5-steroid isomerase. A probe for the nature of hydrogen bonding to the intermediate. Biochemistry 37(2):700-705. (Pubitemid 28123805)
    • (1998) Biochemistry , vol.37 , Issue.2 , pp. 700-705
    • Petrounia, I.P.1    Pollack, R.M.2
  • 7
    • 0034635151 scopus 로고    scopus 로고
    • 5-steroid isomerase: Variation of ligand ionization state with the nature of the electrophilic component
    • DOI 10.1021/bi9917838
    • Petrounia IP, Blotny G, Pollack RM (2000) Binding of 2-naphthols to D38E mutants of 3-oxo-Delta 5-steroid isomerase: Variation of ligand ionization state with the nature of the electrophilic component. Biochemistry 39(1):110-116. (Pubitemid 30033325)
    • (2000) Biochemistry , vol.39 , Issue.1 , pp. 110-116
    • Petrounia, I.P.1    Blotny, G.2    Pollack, R.M.3
  • 8
    • 33646262869 scopus 로고    scopus 로고
    • Testing electrostatic complementarity in enzyme catalysis: Hydrogen bonding in the ketosteroid isomerase oxyanion hole
    • Kraut DA, et al. (2006) Testing electrostatic complementarity in enzyme catalysis: Hydrogen bonding in the ketosteroid isomerase oxyanion hole. PLoS Biol 4(4):e99.
    • (2006) PLoS Biol , vol.4 , Issue.4
    • Kraut, D.A.1
  • 9
    • 53849096731 scopus 로고    scopus 로고
    • Testing geometrical discrimination within an enzyme active site: Constrained hydrogen bonding in the ketosteroid isomerase oxyanion hole
    • Sigala PA, et al. (2008) Testing geometrical discrimination within an enzyme active site: Constrained hydrogen bonding in the ketosteroid isomerase oxyanion hole. J Am Chem Soc 130(41):13696-13708.
    • (2008) J Am Chem Soc , vol.130 , Issue.41 , pp. 13696-13708
    • Sigala, P.A.1
  • 11
    • 78650899625 scopus 로고    scopus 로고
    • Hydrogen bonding in the active site of ketosteroid isomerase: Electronic inductive effects and hydrogen bond coupling
    • Hanoian P, Sigala PA, Herschlag D, Hammes-Schiffer S (2010) Hydrogen bonding in the active site of ketosteroid isomerase: Electronic inductive effects and hydrogen bond coupling. Biochemistry 49(48):10339-10348.
    • (2010) Biochemistry , vol.49 , Issue.48 , pp. 10339-10348
    • Hanoian, P.1    Sigala, P.A.2    Herschlag, D.3    Hammes-Schiffer, S.4
  • 12
    • 0030819258 scopus 로고    scopus 로고
    • 5-3-ketosteroid isomerase
    • DOI 10.1021/bi971549m
    • Zhao Q, Abeygunawardana C, Gittis AG, Mildvan AS (1997) Hydrogen bonding at the active site of delta 5-3-ketosteroid isomerase. Biochemistry 36(48):14616-14626. (Pubitemid 27524381)
    • (1997) Biochemistry , vol.36 , Issue.48 , pp. 14616-14626
    • Zhao, Q.1    Abeygunawardana, C.2    Gittis, A.G.3    Mildvan, A.S.4
  • 13
    • 77949824987 scopus 로고    scopus 로고
    • Proton affinity of the oxyanion hole in the active site of ketosteroid isomerase
    • Childs W, Boxer SG (2010) Proton affinity of the oxyanion hole in the active site of ketosteroid isomerase. Biochemistry 49(12):2725-2731.
    • (2010) Biochemistry , vol.49 , Issue.12 , pp. 2725-2731
    • Childs, W.1    Boxer, S.G.2
  • 14
    • 0024585879 scopus 로고
    • 5-3-ketosteroid isomerase
    • DOI 10.1021/bi00427a022
    • Kuliopulos A,Mildvan AS, Shortle D, Talalay P (1989) Kinetic and ultraviolet spectroscopic studies of active-site mutants of delta 5-3-ketosteroid isomerase. Biochemistry 28(1):149-159. (Pubitemid 19046732)
    • (1989) Biochemistry , vol.28 , Issue.1 , pp. 149-159
    • Kuliopulos, A.1    Mildvan, A.S.2    Shortle, D.3    Talalay, P.4
  • 16
    • 0035890870 scopus 로고    scopus 로고
    • a of phenol
    • DOI 10.1002/qua.1525, International Symposium on Atomic, Molecular, and Condensed Matter Theory
    • Gross KC, Seybold PG (2001) Substituent effects on the physical properties and pKa of phenol. Int J Quantum Chem 85:569-579. (Pubitemid 33105805)
    • (2001) International Journal of Quantum Chemistry , vol.85 , Issue.4-5 , pp. 569-579
    • Gross, K.C.1    Seybold, P.G.2
  • 17
    • 0032860508 scopus 로고    scopus 로고
    • Hydrogen bonding in enzymatic catalysis: Analysis of energetic contributions
    • Shan SO, Herschlag D (1999) Hydrogen bonding in enzymatic catalysis: Analysis of energetic contributions. Methods Enzymol 308:246-276.
    • (1999) Methods Enzymol , vol.308 , pp. 246-276
    • Shan, S.O.1    Herschlag, D.2
  • 18
    • 0029926948 scopus 로고    scopus 로고
    • The energetics of hydrogen bonds in model systems: Implications for enzymatic catalysis
    • Shan SO, Loh S, Herschlag D (1996) The energetics of hydrogen bonds in model systems: Implications for enzymatic catalysis. Science 272(5258):97-101. (Pubitemid 26110758)
    • (1996) Science , vol.272 , Issue.5258 , pp. 97-101
    • Shan, S.-O.1    Loh, S.2    Herschlag, D.3
  • 19
    • 84989060629 scopus 로고
    • 13C NMR studies of the proton transfer in complexes of substituted phenols with trimethylamine N-oxide
    • 13C NMR studies of the proton transfer in complexes of substituted phenols with trimethylamine N-oxide. Magn Reson Chem 30(6):507-510.
    • (1992) Magn Reson Chem , vol.30 , Issue.6 , pp. 507-510
    • Brycki, B.1    Brzezinski, B.2    Zundel, G.3    Keil, T.4
  • 20
    • 84857125236 scopus 로고    scopus 로고
    • Quantitative, directional measurement of electric field heterogeneity in the active site of ketosteroid isomerase
    • Fafarman AT, et al. (2012) Quantitative, directional measurement of electric field heterogeneity in the active site of ketosteroid isomerase. Proc Natl Acad Sci USA 109(6):E299-E308.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.6
    • Fafarman, A.T.1
  • 21
    • 80053641898 scopus 로고    scopus 로고
    • Direct measurement of the protein response to an electrostatic perturbation that mimics the catalytic cycle in ketosteroid isomerase
    • Jha SK, Ji M, Gaffney KJ, Boxer SG (2011) Direct measurement of the protein response to an electrostatic perturbation that mimics the catalytic cycle in ketosteroid isomerase. Proc Natl Acad Sci USA 108(40):16612-16617.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.40 , pp. 16612-16617
    • Jha, S.K.1    Ji, M.2    Gaffney, K.J.3    Boxer, S.G.4
  • 22
    • 84855827272 scopus 로고    scopus 로고
    • Evaluation of the energetics of the concerted acid-base mechanism in enzymatic catalysis: The case of ketosteroid isomerase
    • Fried SD, Boxer SG (2012) Evaluation of the energetics of the concerted acid-base mechanism in enzymatic catalysis: The case of ketosteroid isomerase. J Phys Chem B 116(1):690-697.
    • (2012) J Phys Chem B , vol.116 , Issue.1 , pp. 690-697
    • Fried, S.D.1    Boxer, S.G.2
  • 23
    • 0024850562 scopus 로고
    • Fluorine nuclear magnetic resonance of fluorinated ligands
    • Gerig JT (1989) Fluorine nuclear magnetic resonance of fluorinated ligands. Methods Enzymol 177:3-23.
    • (1989) Methods Enzymol , vol.177 , pp. 3-23
    • Gerig, J.T.1
  • 24
    • 0018118592 scopus 로고
    • Carbon-13 NMR chemical shifts of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH
    • Richarz R, Wuthrich K (1978) Carbon-13 NMR chemical shifts of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH. Biopolymers 17(9):2133-2141. (Pubitemid 9015225)
    • (1978) Biopolymers , vol.17 , Issue.9 , pp. 2133-2141
    • Richarz, R.1    Wuthrich, K.2
  • 25
    • 0000346064 scopus 로고    scopus 로고
    • Solution structure of 3-oxo-delta5-steroid isomerase
    • Wu ZR, et al. (1997) Solution structure of 3-oxo-delta5-steroid isomerase. Science 276(5311):415-418.
    • (1997) Science , vol.276 , Issue.5311 , pp. 415-418
    • Wu, Z.R.1
  • 28
    • 0034731147 scopus 로고    scopus 로고
    • a perturbations of an inhibitor and a catalytic group at an enzyme active site, a mechanistic basis for catalytic power of many enzymes
    • DOI 10.1074/jbc.M007561200
    • Ha NC, Kim MS, Lee W, Choi KY, Oh BH (2000) Detection of large pKa perturbations of an inhibitor and a catalytic group at an enzyme active site, a mechanistic basis for catalytic power of many enzymes. J Biol Chem 275(52):41100-41106. (Pubitemid 32054939)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.52 , pp. 41100-41106
    • Ha, N.-C.1    Kim, M.-S.2    Lee, W.3    Choi, K.Y.4    Oh, B.-H.5
  • 29
    • 35048844134 scopus 로고    scopus 로고
    • Do ligand binding and solvent exclusion alter the electrostatic character within the oxyanion hole of an enzymatic active site?
    • DOI 10.1021/ja075605a
    • Sigala PA, Fafarman AT, Bogard PE, Boxer SG, Herschlag D (2007) Do ligand binding and solvent exclusion alter the electrostatic character within the oxyanion hole of an enzymatic active site? J Am Chem Soc 129(40):12104-12105. (Pubitemid 47556841)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.40 , pp. 12104-12105
    • Sigala, P.A.1    Fafarman, A.T.2    Bogard, P.E.3    Boxer, S.G.4    Herschlag, D.5
  • 32
    • 0029905014 scopus 로고    scopus 로고
    • The change in hydrogen bond strength accompanying charge rearrangement: Implications for enzymatic catalysis
    • Shan SO, Herschlag D (1996) The change in hydrogen bond strength accompanying charge rearrangement: Implications for enzymatic catalysis. Proc Natl Acad Sci USA 93(25):14474-14479.
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.25 , pp. 14474-14479
    • Shan, S.O.1    Herschlag, D.2
  • 33
    • 33746007568 scopus 로고
    • Lengthening of the covalent O-H bond in O-H-O hydrogen bonds re-examined from low-temperature neutron diffraction data of organic compounds
    • Steiner T, Saenger W (1994) Lengthening of the covalent O-H bond in O-H-O hydrogen bonds re-examined from low-temperature neutron diffraction data of organic compounds. Acta Crystallogr B 50:348-357.
    • (1994) Acta Crystallogr B , vol.50 , pp. 348-357
    • Steiner, T.1    Saenger, W.2
  • 34
    • 33845374118 scopus 로고
    • Hydrogen bonding between solutes in aqueous solution
    • Stahl N, Jencks WP (1986) Hydrogen bonding between solutes in aqueous solution. J Am Chem Soc 108(14):4196-4205.
    • (1986) J Am Chem Soc , vol.108 , Issue.14 , pp. 4196-4205
    • Stahl, N.1    Jencks, W.P.2
  • 35
    • 37049073393 scopus 로고
    • Hydrogen bonding. Part 10. A scale of solute hydrogen-bond basicity using log K values for complexation in tetrachloromethane
    • Abraham MH, Grellier PL, Prior DV, Morris JJ, Taylor PJ (1990) Hydrogen bonding. Part 10. A scale of solute hydrogen-bond basicity using log K values for complexation in tetrachloromethane. J Chem Soc Perkin Trans 2:521-529.
    • (1990) J Chem Soc Perkin Trans , vol.2 , pp. 521-529
    • Abraham, M.H.1    Grellier, P.L.2    Prior, D.V.3    Morris, J.J.4    Taylor, P.J.5
  • 36
    • 0142072231 scopus 로고    scopus 로고
    • Vibrational Stark Effects Calibrate the Sensitivity of Vibrational Probes for Electric Fields in Proteins
    • DOI 10.1021/bi0352926
    • Suydam IT, Boxer SG (2003) Vibrational Stark effects calibrate the sensitivity of vibrational probes for electric fields in proteins. Biochemistry 42(41):12050-12055. (Pubitemid 37280655)
    • (2003) Biochemistry , vol.42 , Issue.41 , pp. 12050-12055
    • Suydam, I.T.1    Boxer, S.G.2
  • 37
    • 77956634583 scopus 로고    scopus 로고
    • Decomposition of vibrational shifts of nitriles into electrostatic and hydrogen-bonding effects
    • Fafarman AT, Sigala PA, Herschlag D, Boxer SG (2010) Decomposition of vibrational shifts of nitriles into electrostatic and hydrogen-bonding effects. J Am Chem Soc 132(37):12811-12813.
    • (2010) J Am Chem Soc , vol.132 , Issue.37 , pp. 12811-12813
    • Fafarman, A.T.1    Sigala, P.A.2    Herschlag, D.3    Boxer, S.G.4
  • 39
    • 0032475836 scopus 로고    scopus 로고
    • The low barrier hydrogen bond in enzymatic catalysis
    • DOI 10.1074/jbc.273.40.25529
    • Cleland WW, Frey PA, Gerlt JA (1998) The low barrier hydrogen bond in enzymatic catalysis. J Biol Chem 273(40):25529-25532. (Pubitemid 28475766)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.40 , pp. 25529-25532
    • Cleland, W.W.1    Frey, P.A.2    Gerlt, J.A.3
  • 40
  • 41
    • 0040765445 scopus 로고
    • Role of symmetry in the tunneling of the proton in double minimum potentials
    • de la Vega JR (1982) Role of symmetry in the tunneling of the proton in double minimum potentials. Acc Chem Res 15(41):185-191.
    • (1982) Acc Chem Res , vol.15 , Issue.41 , pp. 185-191
    • De La Vega, J.R.1
  • 42
    • 79957744586 scopus 로고    scopus 로고
    • Reaction pathways of proton transfer in hydrogen-bonded phenol-carboxylate complexes explored by combined UV-vis and NMR spectroscopy
    • Koeppe B, Tolstoy PM, Limbach HH (2011) Reaction pathways of proton transfer in hydrogen-bonded phenol-carboxylate complexes explored by combined UV-vis and NMR spectroscopy. J Am Chem Soc 133(20):7897-7908.
    • (2011) J Am Chem Soc , vol.133 , Issue.20 , pp. 7897-7908
    • Koeppe, B.1    Tolstoy, P.M.2    Limbach, H.H.3
  • 43
    • 78650460393 scopus 로고    scopus 로고
    • Are short, low-barrier hydrogen bonds unusually strong?
    • Perrin CL (2010) Are short, low-barrier hydrogen bonds unusually strong? Acc Chem Res 43(12):1550-1557.
    • (2010) Acc Chem Res , vol.43 , Issue.12 , pp. 1550-1557
    • Perrin, C.L.1
  • 44
    • 33746017658 scopus 로고    scopus 로고
    • Electric fields at the active site of an enzyme: Direct comparison of experiment with theory
    • DOI 10.1126/science.1127159
    • Suydam IT, Snow CD, Pande VS, Boxer SG (2006) Electric fields at the active site of an enzyme: Direct comparison of experiment with theory. Science 313(5784):200-204. (Pubitemid 44066246)
    • (2006) Science , vol.313 , Issue.5784 , pp. 200-204
    • Suydam, I.T.1    Snow, C.D.2    Pande, V.S.3    Boxer, S.G.4
  • 45
    • 77958474269 scopus 로고    scopus 로고
    • Nitrile bonds as infrared probes of electrostatics in ribonuclease S
    • Fafarman AT, Boxer SG (2010) Nitrile bonds as infrared probes of electrostatics in ribonuclease S. J Phys Chem B 114(42):13536-13544.
    • (2010) J Phys Chem B , vol.114 , Issue.42 , pp. 13536-13544
    • Fafarman, A.T.1    Boxer, S.G.2
  • 46
    • 76549252207 scopus 로고
    • The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain
    • Pauling L, Corey RB, Branson HR (1951) The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain. Proc Natl Acad Sci USA 37(4):205-211.
    • (1951) Proc Natl Acad Sci USA , vol.37 , Issue.4 , pp. 205-211
    • Pauling, L.1    Corey, R.B.2    Branson, H.R.3
  • 47
    • 33947451575 scopus 로고
    • Two hydrogen-bonded spiral configurations of the polypeptide chain
    • Pauling L, Corey RB (1950) Two hydrogen-bonded spiral configurations of the polypeptide chain. J Am Chem Soc 72(11):5349.
    • (1950) J Am Chem Soc , vol.72 , Issue.11 , pp. 5349
    • Pauling, L.1    Corey, R.B.2
  • 48
    • 67249133227 scopus 로고    scopus 로고
    • Hydrogen bond dynamics in the active site of photoactive yellow protein
    • Sigala PA, Tsuchida MA, Herschlag D (2009) Hydrogen bond dynamics in the active site of photoactive yellow protein. Proc Natl Acad Sci USA 106(23):9232-9237.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.23 , pp. 9232-9237
    • Sigala, P.A.1    Tsuchida, M.A.2    Herschlag, D.3
  • 49
    • 0041989850 scopus 로고    scopus 로고
    • Challenges in enzyme mechanism and energetics
    • DOI 10.1146/annurev.biochem.72.121801.161617
    • Kraut DA, Carroll KS, Herschlag D (2003) Challenges in enzyme mechanism and energetics. Annu Rev Biochem 72:517-571. (Pubitemid 36934521)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 517-571
    • Kraut, D.A.1    Carroll, K.S.2    Herschlag, D.3
  • 50
    • 76649126435 scopus 로고    scopus 로고
    • Dissecting the paradoxical effects of hydrogen bond mutations in the ketosteroid isomerase oxyanion hole
    • Kraut DA, Sigala PA, Fenn TD, Herschlag D (2010) Dissecting the paradoxical effects of hydrogen bond mutations in the ketosteroid isomerase oxyanion hole. Proc Natl Acad Sci USA 107(5):1960-1965.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.5 , pp. 1960-1965
    • Kraut, D.A.1    Sigala, P.A.2    Fenn, T.D.3    Herschlag, D.4
  • 51
    • 0028930478 scopus 로고
    • Site-directed mutagenesis: A tool for studying enzyme catalysis
    • Plapp BV (1995) Site-directed mutagenesis: A tool for studying enzyme catalysis. Methods Enzymol 249:91-119.
    • (1995) Methods Enzymol , vol.249 , pp. 91-119
    • Plapp, B.V.1
  • 52
    • 0024281312 scopus 로고
    • Relationships between apparent binding energies measured in site-directed mutagenesis experiments and energetics of binding and catalysis
    • Fersht AR (1988) Relationships between apparent binding energies measured in site-directed mutagenesis experiments and energetics of binding and catalysis. Biochemistry 27(5):1577-1580.
    • (1988) Biochemistry , vol.27 , Issue.5 , pp. 1577-1580
    • Fersht, A.R.1
  • 54
    • 33947547892 scopus 로고
    • Molecular architecture and biological reactions
    • Pauling L (1946) Molecular architecture and biological reactions. Chem Eng News 24(10):1375-1377.
    • (1946) Chem Eng News , vol.24 , Issue.10 , pp. 1375-1377
    • Pauling, L.1
  • 55
    • 0024713705 scopus 로고
    • Enzymes work by solvation substitution rather than by desolvation
    • Warshel A, Aqvist J, Creighton S (1989) Enzymes work by solvation substitution rather than by desolvation. Proc Natl Acad Sci USA 86(15):5820-5824.
    • (1989) Proc Natl Acad Sci USA , vol.86 , Issue.15 , pp. 5820-5824
    • Warshel, A.1    Aqvist, J.2    Creighton, S.3
  • 56
    • 77952020160 scopus 로고    scopus 로고
    • Solvation response along the reaction coordinate in the active site of ketosteroid isomerase
    • Childs W, Boxer SG (2010) Solvation response along the reaction coordinate in the active site of ketosteroid isomerase. J Am Chem Soc 132(18):6474-6480.
    • (2010) J Am Chem Soc , vol.132 , Issue.18 , pp. 6474-6480
    • Childs, W.1    Boxer, S.G.2
  • 57
    • 38949205622 scopus 로고    scopus 로고
    • Electrostatic fields near the active site of human aldose reductase: 1. New inhibitors and vibrational stark effect measurements
    • DOI 10.1021/bi701708u
    • Webb LJ, Boxer SG (2008) Electrostatic fields near the active site of human aldose reductase: 1. New inhibitors and vibrational stark effect measurements. Biochemistry 47(6):1588-1598. (Pubitemid 351231209)
    • (2008) Biochemistry , vol.47 , Issue.6 , pp. 1588-1598
    • Webb, L.J.1    Boxer, S.G.2
  • 58
    • 80053392716 scopus 로고    scopus 로고
    • Electrostatic fields near the active site of human aldose reductase: 2. New inhibitors and complications caused by hydrogen bonds
    • Xu L, Cohen AE, Boxer SG (2011) Electrostatic fields near the active site of human aldose reductase: 2. New inhibitors and complications caused by hydrogen bonds. Biochemistry 50(39):8311-8322.
    • (2011) Biochemistry , vol.50 , Issue.39 , pp. 8311-8322
    • Xu, L.1    Cohen, A.E.2    Boxer, S.G.3
  • 59
    • 22844455879 scopus 로고    scopus 로고
    • Hydrogen bonds with large proton polarizability and proton transfer processes in electrochemistry and biology
    • Zundel G (2000) Hydrogen bonds with large proton polarizability and proton transfer processes in electrochemistry and biology. Adv Chem Phys 111:1-217.
    • (2000) Adv Chem Phys , vol.111 , pp. 1-217
    • Zundel, G.1
  • 60
    • 0001125401 scopus 로고
    • Hydrogen-bonded intermediates and stepwise mechanisms for proton-exchange reactions between oxygen atoms in hydroxylic solvents
    • Hine J (1972) Hydrogen-bonded intermediates and stepwise mechanisms for proton-exchange reactions between oxygen atoms in hydroxylic solvents. J Am Chem Soc 94(16):5766-5771.
    • (1972) J Am Chem Soc , vol.94 , Issue.16 , pp. 5766-5771
    • Hine, J.1
  • 61
    • 61849159407 scopus 로고    scopus 로고
    • Predicting hydrogen-bond strengths from acid-base molecular properties. The pK(a) slide rule: Toward the solution of a long-lasting problem
    • Gilli P, Pretto L, Bertolasi V, Gilli G (2009) Predicting hydrogen-bond strengths from acid-base molecular properties. The pK(a) slide rule: Toward the solution of a long-lasting problem. Acc Chem Res 42(1):33-44.
    • (2009) Acc Chem Res , vol.42 , Issue.1 , pp. 33-44
    • Gilli, P.1    Pretto, L.2    Bertolasi, V.3    Gilli, G.4
  • 62
    • 84988087911 scopus 로고
    • Calculating the electrostatic potential of molecules in solution - Method and error assessment
    • Gilson MK, Sharp K, Honig B (1988) Calculating the electrostatic potential of molecules in solution - Method and error assessment. J Comput Chem 9(4):327-335.
    • (1988) J Comput Chem , vol.9 , Issue.4 , pp. 327-335
    • Gilson, M.K.1    Sharp, K.2    Honig, B.3


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