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Volumn 87, Issue 4, 2004, Pages 2221-2239

Studies of proton translocations in biological systems: Simulating proton transport in carbonic anhydrase by EVB-based models

Author keywords

[No Author keywords available]

Indexed keywords

CARBONATE DEHYDRATASE; WATER; CARBONATE DEHYDRATASE III; PROTON; PROTON PUMP;

EID: 12344266417     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.043257     Document Type: Article
Times cited : (83)

References (90)
  • 1
    • 11744384413 scopus 로고
    • The Grotthuss mechanism
    • Agmon, N. 1995. The Grotthuss mechanism. Chem. Phys. Lett. 244:456-462.
    • (1995) Chem. Phys. Lett. , vol.244 , pp. 456-462
    • Agmon, N.1
  • 2
    • 0026504259 scopus 로고
    • Computer simulation of the initial proton transfer step in human carbonic anhydrase I
    • Åqvist, J., and A. Warshel. 1992. Computer simulation of the initial proton transfer step in human carbonic anhydrase I. J. Mol. Biol. 224:7-14.
    • (1992) J. Mol. Biol. , vol.224 , pp. 7-14
    • Åqvist, J.1    Warshel, A.2
  • 3
    • 4243810035 scopus 로고
    • Simulation of enzyme reactions using valence bond force fields and other hybrid quantum/classical approaches
    • Åqvist, J., and A. Warshel. 1993. Simulation of enzyme reactions using valence bond force fields and other hybrid quantum/classical approaches. Chem. Rev. 93:2523-2544.
    • (1993) Chem. Rev. , vol.93 , pp. 2523-2544
    • Åqvist, J.1    Warshel, A.2
  • 5
    • 0035861430 scopus 로고    scopus 로고
    • Reality simulation: Observe while it happens
    • Berendsen, H. J. C. 2001. Reality simulation: observe while it happens. Science. 294:2304-2305.
    • (2001) Science , vol.294 , pp. 2304-2305
    • Berendsen, H.J.C.1
  • 6
    • 0035861065 scopus 로고    scopus 로고
    • Hydride transfer in liver alcohol dehydrogenase: Quantum dynamics, kinetic isotope effects, and role of enzyme motion
    • Billeter, S. R., S. P. Webb, P. K. Agarwal, T. Iordanov, and S. Hammes-Schiffer. 2001. Hydride transfer in liver alcohol dehydrogenase: quantum dynamics, kinetic isotope effects, and role of enzyme motion. J. Am. Chem. Soc. 123:11262-11272.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 11262-11272
    • Billeter, S.R.1    Webb, S.P.2    Agarwal, P.K.3    Iordanov, T.4    Hammes-Schiffer, S.5
  • 7
    • 0344825877 scopus 로고    scopus 로고
    • What really prevents proton transport through aquaporin? Charge self-energy versus proton wire proposals
    • Burykin, A., and A. Warshel. 2003. What really prevents proton transport through aquaporin? Charge self-energy versus proton wire proposals. Biophys. J. 85:3696-3706.
    • (2003) Biophys. J. , vol.85 , pp. 3696-3706
    • Burykin, A.1    Warshel, A.2
  • 9
    • 0037473097 scopus 로고    scopus 로고
    • Is a "proton wire" concerted or stepwise? A model study of proton transfer in carbonic anhydrase
    • Cui, Q., and M. Karplus. 2003. Is a "proton wire" concerted or stepwise? A model study of proton transfer in carbonic anhydrase. J. Phys. Chem. B. 107:1071-1078.
    • (2003) J. Phys. Chem. B. , vol.107 , pp. 1071-1078
    • Cui, Q.1    Karplus, M.2
  • 10
    • 0035967378 scopus 로고    scopus 로고
    • A multi-state empirical valence bond model for weak acid dissociation in aqueous solution
    • Cuma, M., U. W. Schmitt, and G. A. Voth. 2001. A multi-state empirical valence bond model for weak acid dissociation in aqueous solution. Journal of Physical Chemistry A. 105:2814-2823.
    • (2001) Journal of Physical Chemistry A , vol.105 , pp. 2814-2823
    • Cuma, M.1    Schmitt, U.W.2    Voth, G.A.3
  • 11
    • 84931510416 scopus 로고
    • Adiabatic electron transfer in polar media quantum transition state theory
    • Dakhnovskii, Y. I., and A. A. Ovchinnikov. 1986. Adiabatic electron transfer in polar media quantum transition state theory. Mol. Phys. 58:237-252.
    • (1986) Mol. Phys. , vol.58 , pp. 237-252
    • Dakhnovskii, Y.I.1    Ovchinnikov, A.A.2
  • 12
    • 0037379781 scopus 로고    scopus 로고
    • Voltage-gated proton channels and other proton transfer pathways
    • Decoursey, T. E. 2003. Voltage-gated proton channels and other proton transfer pathways. Physiol. Rev. 83:475-579.
    • (2003) Physiol. Rev. , vol.83 , pp. 475-579
    • Decoursey, T.E.1
  • 13
    • 0141534474 scopus 로고    scopus 로고
    • The mechanism of proton exclusion in the aquaporin-1 water channel
    • de Groot, B. L., T. Frigato, V. Helms, and H. Grubmuller. 2003. The mechanism of proton exclusion in the aquaporin-1 water channel. J. Mol. Biol. 333:279-293.
    • (2003) J. Mol. Biol. , vol.333 , pp. 279-293
    • De Groot, B.L.1    Frigato, T.2    Helms, V.3    Grubmuller, H.4
  • 14
    • 0035861454 scopus 로고    scopus 로고
    • Water permeation across biological membranes: Mechanism and dynamics of aquaporin-1 and GlpF
    • de Groot, B., and H. Grubmuller. 2001. Water permeation across biological membranes: mechanism and dynamics of aquaporin-1 and GlpF. Science. 294:2353-2357.
    • (2001) Science , vol.294 , pp. 2353-2357
    • De Groot, B.1    Grubmuller, H.2
  • 15
    • 0001957354 scopus 로고
    • Proton transfer, acid-base catalysis, and enzymatic hydrolysis. Part I: Elementary processes
    • Eigen, M. 1964. Proton transfer, acid-base catalysis, and enzymatic hydrolysis. Part I: Elementary processes. Angew. Chem. Int. Ed. Engl. 3:1-19.
    • (1964) Angew. Chem. Int. Ed. Engl. , vol.3 , pp. 1-19
    • Eigen, M.1
  • 16
    • 0028774335 scopus 로고
    • Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution: Cofactors and protein-cofactor interactions
    • Ermler, U., G. Fritzsch, S. K. Buchanan, and H. Michel. 1994. Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution: cofactors and protein-cofactor interactions. Structure. 2:925-936.
    • (1994) Structure , vol.2 , pp. 925-936
    • Ermler, U.1    Fritzsch, G.2    Buchanan, S.K.3    Michel, H.4
  • 17
    • 0037207102 scopus 로고    scopus 로고
    • The catalytic power of ketosteroid isomerase investigated by computer simulation
    • Feierberg, I., and J. Åqvist. 2002. The catalytic power of ketosteroid isomerase investigated by computer simulation. Biochemistry. 41:15728-15735.
    • (2002) Biochemistry , vol.41 , pp. 15728-15735
    • Feierberg, I.1    Åqvist, J.2
  • 18
    • 0037118374 scopus 로고    scopus 로고
    • Comment on molecular mechanics for chemical reactions
    • Florian, J. 2002. Comment on molecular mechanics for chemical reactions. J. Phys. Chem. A. 106:5046-5047.
    • (2002) J. Phys. Chem. A , vol.106 , pp. 5046-5047
    • Florian, J.1
  • 20
    • 0032560607 scopus 로고    scopus 로고
    • Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase
    • Girvin, M. E., V. K. Rastogi, F. Abildgaard, J. L. Markley, and R. H. Fillingame. 1998. Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase. Biochemistry. 37:8817-8824.
    • (1998) Biochemistry , vol.37 , pp. 8817-8824
    • Girvin, M.E.1    Rastogi, V.K.2    Abildgaard, F.3    Markley, J.L.4    Fillingame, R.H.5
  • 22
    • 0029951263 scopus 로고    scopus 로고
    • How important are quantum mechanical nuclear motions in enzyme catalysis?
    • Hwang, J.-K., and A. Warshel. 1996. How important are quantum mechanical nuclear motions in enzyme catalysis? J. Am. Chem. Soc. 118:11745-11751.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11745-11751
    • Hwang, J.-K.1    Warshel, A.2
  • 23
    • 1842583051 scopus 로고    scopus 로고
    • The mechanism of proton exclusion in aquaporin channels
    • In press
    • Ilan, B., E. Tajkhorshid, K. Schulten, and G. A. Voth. 2004. The mechanism of proton exclusion in aquaporin channels. Proteins. In press.
    • (2004) Proteins
    • Ilan, B.1    Tajkhorshid, E.2    Schulten, K.3    Voth, G.A.4
  • 24
    • 0035850352 scopus 로고    scopus 로고
    • Proton conduction by a chain of water molecules in carbonic anhydrase
    • Isaev, A., and S. Scheiner. 2001. Proton conduction by a chain of water molecules in carbonic anhydrase. J. Phys. Chem. B. 105:6420-6426.
    • (2001) J. Phys. Chem. B. , vol.105 , pp. 6420-6426
    • Isaev, A.1    Scheiner, S.2
  • 25
    • 0242269040 scopus 로고    scopus 로고
    • Electrostatic tuning of permeation and selectivity in aquaporin water channels
    • Jensen, M. O., E. Tajkhorshid, and K. Schulten. 2003. Electrostatic tuning of permeation and selectivity in aquaporin water channels. Biophys. J. 85:2884-2899.
    • (2003) Biophys. J. , vol.85 , pp. 2884-2899
    • Jensen, M.O.1    Tajkhorshid, E.2    Schulten, K.3
  • 26
    • 0031880698 scopus 로고    scopus 로고
    • The coupling of electron transfer and proton translocation: Electrostatic calculations on Paracoccus dentrificans cytochrome c oxidase
    • Kannt, A., R. D. Lancaster, and H. Michel. 1998. The coupling of electron transfer and proton translocation: electrostatic calculations on Paracoccus dentrificans cytochrome c oxidase. Biophys. J. 74:708-721.
    • (1998) Biophys. J. , vol.74 , pp. 708-721
    • Kannt, A.1    Lancaster, R.D.2    Michel, H.3
  • 27
    • 0001477037 scopus 로고    scopus 로고
    • Multiconfiguration molecular mechanics algorithm for potential energy surfaces of chemical reactions
    • Kim, Y., J. C. Corchado, J. Villà, J. Xing, and D. G. Truhlar. 2000. Multiconfiguration molecular mechanics algorithm for potential energy surfaces of chemical reactions. J. Chem. Phys. 112:2718-2735.
    • (2000) J. Chem. Phys. , vol.112 , pp. 2718-2735
    • Kim, Y.1    Corchado, J.C.2    Villà, J.3    Xing, J.4    Truhlar, D.G.5
  • 28
    • 0035807795 scopus 로고    scopus 로고
    • Dynamic mechanisms of the membrane water channel aquaporin-1 (AQP1)
    • Kong, Y., and G. Ma. 2001. Dynamic mechanisms of the membrane water channel aquaporin-1 (AQP1). Proc. Natl. Acad. Sci. USA. 98:14345-14349.
    • (2001) Proc. Natl. Acad. Sci. USA. , vol.98 , pp. 14345-14349
    • Kong, Y.1    Ma, G.2
  • 30
    • 0001494018 scopus 로고
    • Application of the method of generating function to radiative and non-radiative transitions of a trapped electron in a crystal
    • Kubo, R., and Y. Toyozawa. 1955. Application of the method of generating function to radiative and non-radiative transitions of a trapped electron in a crystal. Prog. Theor. Phys. 13:160-182.
    • (1955) Prog. Theor. Phys. , vol.13 , pp. 160-182
    • Kubo, R.1    Toyozawa, Y.2
  • 31
    • 0030030176 scopus 로고    scopus 로고
    • Calculated coupling of electron and proton transfer in the photosynthetic reaction center of Rhodopsedomonas viridis
    • Lancaster, C. R. D., H. Michel, and B. Honig. 1996. Calculated coupling of electron and proton transfer in the photosynthetic reaction center of Rhodopsedomonas viridis. Biophys. J. 70:2469-2492.
    • (1996) Biophys. J. , vol.70 , pp. 2469-2492
    • Lancaster, C.R.D.1    Michel, H.2    Honig, B.3
  • 32
    • 0037007052 scopus 로고    scopus 로고
    • Water transporters: How so fast yet so selective?
    • Law, R. J., and M. S. P. Sansom. 2002. Water transporters: how so fast yet so selective? Curr. Biol. 12:R250-R252.
    • (2002) Curr. Biol. , vol.12
    • Law, R.J.1    Sansom, M.S.P.2
  • 33
    • 0000728542 scopus 로고
    • Microscopic and semimicroscopic calculations of electrostatic energies in proteins by the POLARIS and ENZYMIX programs
    • Lee, F. S., Z. T. Chu, and A. Warshel. 1993. Microscopic and semimicroscopic calculations of electrostatic energies in proteins by the POLARIS and ENZYMIX programs. J. Comp. Chem. 14:161-185.
    • (1993) J. Comp. Chem. , vol.14 , pp. 161-185
    • Lee, F.S.1    Chu, Z.T.2    Warshel, A.3
  • 34
    • 0035124287 scopus 로고    scopus 로고
    • Compact parameter set for fast estimation of proton transfer rates
    • Lill, M. A., and V. Helms. 2001. Compact parameter set for fast estimation of proton transfer rates. J. Chem. Phys. 114:1125-1132.
    • (2001) J. Chem. Phys. , vol.114 , pp. 1125-1132
    • Lill, M.A.1    Helms, V.2
  • 35
    • 0032577041 scopus 로고    scopus 로고
    • Proton transfer in the enzyme carbonic anhydrase: An ab initio study
    • Lu, D., and G. A. Voth. 1998. Proton transfer in the enzyme carbonic anhydrase: an ab initio study. J. Am. Chem. Soc. 120:4006-4014.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 4006-4014
    • Lu, D.1    Voth, G.A.2
  • 36
    • 0034734246 scopus 로고    scopus 로고
    • Atomic resolution structures of bacteriorhodopsin photocycle intermediates: The role of discrete water molecules in the function of this light-driven ion pump
    • Luecke, H. 2000. Atomic resolution structures of bacteriorhodopsin photocycle intermediates: the role of discrete water molecules in the function of this light-driven ion pump. Biochim. Biophys. Acta. 1460:133-156.
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 133-156
    • Luecke, H.1
  • 39
    • 0001672288 scopus 로고
    • Chemical and electrochemical electron transfer theory
    • Marcus, R. A. 1964. Chemical and electrochemical electron transfer theory. Annu. Rev. Phys. Chem. 15:155-196.
    • (1964) Annu. Rev. Phys. Chem. , vol.15 , pp. 155-196
    • Marcus, R.A.1
  • 40
    • 0029782010 scopus 로고    scopus 로고
    • Proton transport across transient single-file water pores in a lipid membrane studied by molecular dynamics simulations
    • Marrink, S. J., F. Jahnig, and H. J. Berendsen. 1996. Proton transport across transient single-file water pores in a lipid membrane studied by molecular dynamics simulations. Biophys. J. 71:632-647.
    • (1996) Biophys. J. , vol.71 , pp. 632-647
    • Marrink, S.J.1    Jahnig, F.2    Berendsen, H.J.3
  • 42
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
    • Mitchel, P. 1961. Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism. Nature. 191:144-148.
    • (1961) Nature , vol.191 , pp. 144-148
    • Mitchel, P.1
  • 44
    • 0001728579 scopus 로고
    • Molecular models of proton pumps
    • Nagle, J. F., and M. Mille. 1981. Molecular models of proton pumps. J. Chem. Phys. 74:1367-1372.
    • (1981) J. Chem. Phys. , vol.74 , pp. 1367-1372
    • Nagle, J.F.1    Mille, M.2
  • 45
    • 35349003733 scopus 로고
    • Theory of hydrogen bonded chains in bioenergetics
    • Nagle, J. F., M. Mille, and H. J. Morowitz. 1980. Theory of hydrogen bonded chains in bioenergetics. J. Chem. Phys. 72:3959-3971.
    • (1980) J. Chem. Phys. , vol.72 , pp. 3959-3971
    • Nagle, J.F.1    Mille, M.2    Morowitz, H.J.3
  • 46
    • 0345613372 scopus 로고
    • Theory of hydrogen bonded chains in bioenergetics
    • Nagle, J. F., and H. J. Morowitz. 1978. Theory of hydrogen bonded chains in bioenergetics. Proc. Natl. Acad. Sci. USA. 75:298-302.
    • (1978) Proc. Natl. Acad. Sci. USA. , vol.75 , pp. 298-302
    • Nagle, J.F.1    Morowitz, H.J.2
  • 47
    • 0026718120 scopus 로고
    • Proton transfer in reaction centers from photosynthetic bacteria
    • Okamura, M. Y., and G. Feher. 1992. Proton transfer in reaction centers from photosynthetic bacteria. Annu. Rev. Biochem. 61:861-896.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 861-896
    • Okamura, M.Y.1    Feher, G.2
  • 48
    • 0030886203 scopus 로고    scopus 로고
    • Structure at 2.7 a resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment
    • Ostermeier, C., A. Harrenga, U. Ermler, and H. Michel. 1997. Structure at 2.7 A resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment. Proc. Natl. Acad. Sci. USA. 94:10547-10553.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10547-10553
    • Ostermeier, C.1    Harrenga, A.2    Ermler, U.3    Michel, H.4
  • 49
    • 0031862465 scopus 로고    scopus 로고
    • + conduction along hydrogen-bonded chains of water molecules
    • + conduction along hydrogen-bonded chains of water molecules. Biophys. J. 75:33-10.
    • (1998) Biophys. J. , vol.75 , pp. 33-110
    • Pomes, R.1    Roux, B.2
  • 50
    • 0036225143 scopus 로고    scopus 로고
    • + conduction in the single-file chain of the gramicidin channel
    • + conduction in the single-file chain of the gramicidin channel. Biophys. J. 82:2304-2316.
    • (2002) Biophys. J. , vol.82 , pp. 2304-2316
    • Pomes, R.1    Roux, B.2
  • 51
    • 0034632821 scopus 로고    scopus 로고
    • Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin
    • Royant, A., K. Edman, T. Ursby, E. Pebay-Peyroula, E. M. Landau, and R. Neutze. 2000. Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin. Nature. 406:645-648.
    • (2000) Nature , vol.406 , pp. 645-648
    • Royant, A.1    Edman, K.2    Ursby, T.3    Pebay-Peyroula, E.4    Landau, E.M.5    Neutze, R.6
  • 52
    • 0035936571 scopus 로고    scopus 로고
    • Aquaporins: Channels without ions
    • Sansom, M. S. P., and R. J. Law. 2001. Aquaporins: channels without ions. Curr. Biol. 11:R71-R73.
    • (2001) Curr. Biol. , vol.11
    • Sansom, M.S.P.1    Law, R.J.2
  • 53
    • 0342646933 scopus 로고    scopus 로고
    • Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin
    • Sass, H. J., G. Buldt, R. Gessenich, D. Hehn, D. Neff, R. Schlesinger, J. Berendzen, and P. Ormos. 2000. Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin. Nature. 406:649-653.
    • (2000) Nature , vol.406 , pp. 649-653
    • Sass, H.J.1    Buldt, G.2    Gessenich, R.3    Hehn, D.4    Neff, D.5    Schlesinger, R.6    Berendzen, J.7    Ormos, P.8
  • 54
    • 11644271492 scopus 로고    scopus 로고
    • Multistate empirical valence bond model for proton transport in water
    • Schmitt, U. W., and G. A. Voth. 1998. Multistate empirical valence bond model for proton transport in water. J. Phys. Chem. B. 102:5547-5551.
    • (1998) J. Phys. Chem. B. , vol.102 , pp. 5547-5551
    • Schmitt, U.W.1    Voth, G.A.2
  • 55
    • 0001213767 scopus 로고    scopus 로고
    • The computer simulation of proton transport in water
    • Schmitt, U. W., and G. A. Voth. 1999. The computer simulation of proton transport in water. J. Chem. Phys. 111:9361-9381.
    • (1999) J. Chem. Phys. , vol.111 , pp. 9361-9381
    • Schmitt, U.W.1    Voth, G.A.2
  • 56
    • 0003756939 scopus 로고
    • Theory and applications of stochastic differential equations
    • John Wiley & Sons, New York, NY
    • Schuss, Z. 1980. Theory and applications of stochastic differential equations. In Wiley Series in Probability and Mathematical Statistics. John Wiley & Sons, New York, NY. 321.
    • (1980) Wiley Series in Probability and Mathematical Statistics , pp. 321
    • Schuss, Z.1
  • 57
    • 0035451052 scopus 로고    scopus 로고
    • What are the dielectric "constants" of proteins and how to validate electrostatic models
    • Schutz, C. N., and A. Warshel. 2001. What are the dielectric "constants" of proteins and how to validate electrostatic models. Proteins Struct. Funct. Genet. 44:400-417.
    • (2001) Proteins Struct. Funct. Genet. , vol.44 , pp. 400-417
    • Schutz, C.N.1    Warshel, A.2
  • 58
    • 1342281185 scopus 로고    scopus 로고
    • Analyzing free energy relationships for proton translations in enzymes: Carbonic anhydrase revisted
    • Schutz, C. N., and A. Warshel. 2004. Analyzing free energy relationships for proton translations in enzymes: carbonic anhydrase revisted. J. Phys. Chem. B. 108:2066-2075.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 2066-2075
    • Schutz, C.N.1    Warshel, A.2
  • 59
    • 0344418714 scopus 로고    scopus 로고
    • Simulating proton translocations in proteins: Probing proton transfer pathways in the Rhodobacter sphaeroides reaction center
    • Sham, Y., I. Muegge, and A. Warshel. 1999. Simulating proton translocations in proteins: probing proton transfer pathways in the Rhodobacter sphaeroides reaction center. Proteins. 36:484-500.
    • (1999) Proteins , vol.36 , pp. 484-500
    • Sham, Y.1    Muegge, I.2    Warshel, A.3
  • 60
    • 84962477148 scopus 로고    scopus 로고
    • Structure/function correlations of proteins using MM, QM/MM and related approaches: Methods, concepts, pitfalls and current progress
    • Shurki, A., and A. Warshel. 2003. Structure/function correlations of proteins using MM, QM/MM and related approaches: methods, concepts, pitfalls and current progress. Adv. Protein Chem. 66:249-312.
    • (2003) Adv. Protein Chem. , vol.66 , pp. 249-312
    • Shurki, A.1    Warshel, A.2
  • 61
    • 0034640335 scopus 로고    scopus 로고
    • Marcus rate theory applied to enzymatic proton transfer
    • Silverman, D. N. 2000. Marcus rate theory applied to enzymatic proton transfer. Biochem. Biophys. Acta. 1458:88-103.
    • (2000) Biochem. Biophys. Acta , vol.1458 , pp. 88-103
    • Silverman, D.N.1
  • 62
    • 33845278732 scopus 로고
    • Catalytic mechanism of carbonic anhydrase
    • Silverman, D. N., and S. Lindskog. 1988. Catalytic mechanism of carbonic anhydrase. Acc. Chem. Res. 21:30-36.
    • (1988) Acc. Chem. Res. , vol.21 , pp. 30-36
    • Silverman, D.N.1    Lindskog, S.2
  • 63
    • 0027438252 scopus 로고
    • Rate-equilibria relationships in intramolecular proton transfer in human carbonic anhydrase III
    • Silverman, D. N., C. Tu, X. Chen, S. M. Tanhauser, A. J. Kresge, and P. J. Laipis. 1993. Rate-equilibria relationships in intramolecular proton transfer in human carbonic anhydrase III. Biochemistry. 34:10757-10762.
    • (1993) Biochemistry , vol.34 , pp. 10757-10762
    • Silverman, D.N.1    Tu, C.2    Chen, X.3    Tanhauser, S.M.4    Kresge, A.J.5    Laipis, P.J.6
  • 64
    • 0037180863 scopus 로고    scopus 로고
    • Ab-initio QM/MM simulation with proper sampling: "first principle" calculations of the free energy of the auto-dissociation of water in aqueous solution
    • Strajbl, M., G. Hong, and A. Warshel. 2002. Ab-initio QM/MM simulation with proper sampling: "first principle" calculations of the free energy of the auto-dissociation of water in aqueous solution. J. Phys. Chem. B. 106:13333-13343.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 13333-13343
    • Strajbl, M.1    Hong, G.2    Warshel, A.3
  • 65
    • 0000997465 scopus 로고    scopus 로고
    • Calculations of activation entropies of chemical reactions in solution
    • Strajbl, M., Y. Y. Sham, J. Villà, Z. T. Chu, and A. Warshel. 2000. Calculations of activation entropies of chemical reactions in solution. J. Phys. Chem. B. 104:4578-4584.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 4578-4584
    • Strajbl, M.1    Sham, Y.Y.2    Villà, J.3    Chu, Z.T.4    Warshel, A.5
  • 66
    • 0037134267 scopus 로고    scopus 로고
    • Control of the selectivity of the aquaporin water channel by global orientational tuning
    • Tajkhorshid, E., P. Nollert, M. Jensen, L. Miercke, R. M. Stroud, and K. Schulten. 2002. Control of the selectivity of the aquaporin water channel by global orientational tuning. Science. 296:525-530.
    • (2002) Science , vol.296 , pp. 525-530
    • Tajkhorshid, E.1    Nollert, P.2    Jensen, M.3    Miercke, L.4    Stroud, R.M.5    Schulten, K.6
  • 67
    • 9644301524 scopus 로고
    • Stochastic dynamics for molecules with constraints. Brownian dynamics of n-alkanes
    • van Gunsteren, W. F., H. J. C. Berendsen, and J. A. C. Rullmann. 1981. Stochastic dynamics for molecules with constraints. Brownian dynamics of n-alkanes. Molecular Physics. 44:69-95.
    • (1981) Molecular Physics , vol.44 , pp. 69-95
    • Van Gunsteren, W.F.1    Berendsen, H.J.C.2    Rullmann, J.A.C.3
  • 68
    • 0035940264 scopus 로고    scopus 로고
    • Energetics and dynamics of enzymatic reactions
    • Villa, J., and A. Warshel. 2001. Energetics and dynamics of enzymatic reactions. J. Phys. Chem. B. 105:7887-7907.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 7887-7907
    • Villa, J.1    Warshel, A.2
  • 69
    • 7644225147 scopus 로고    scopus 로고
    • Molecular dynamics of an excess proton in water using a non-additive valence bond force field
    • Vuilleumier, R., and D. Borgis. 1997. Molecular dynamics of an excess proton in water using a non-additive valence bond force field. J. Mol. Struct. 436-437:555-565.
    • (1997) J. Mol. Struct. , vol.436-437 , pp. 555-565
    • Vuilleumier, R.1    Borgis, D.2
  • 71
    • 0347356002 scopus 로고    scopus 로고
    • Quantum dynamics of an excess proton in water using an extended empirical valence-bond Hamiltonian
    • Vuilleumier, R., and D. Borgis. 1998b. Quantum dynamics of an excess proton in water using an extended empirical valence-bond Hamiltonian. J. Phys. Chem. B. 102:4261-4264.
    • (1998) J. Phys. Chem. B. , vol.102 , pp. 4261-4264
    • Vuilleumier, R.1    Borgis, D.2
  • 72
    • 0347924514 scopus 로고    scopus 로고
    • Transport and spectroscopy of the hydrated proton: A molecular dynamics study
    • Vuilleumier, R., and D. Borgis. 1999. Transport and spectroscopy of the hydrated proton: a molecular dynamics study. J. Chem. Phys. 111:4251-4266.
    • (1999) J. Chem. Phys. , vol.111 , pp. 4251-4266
    • Vuilleumier, R.1    Borgis, D.2
  • 73
    • 0018504783 scopus 로고
    • Conversion of light energy to electrostatic energy in the proton pump of Halobacterium halobium
    • Warshel, A. 1979. Conversion of light energy to electrostatic energy in the proton pump of Halobacterium halobium. Photochem. Photobiol. 30:285-290.
    • (1979) Photochem. Photobiol. , vol.30 , pp. 285-290
    • Warshel, A.1
  • 74
    • 0019889036 scopus 로고
    • a, proton transfer reactions, and general acid catalysis reactions in enzymes
    • a, proton transfer reactions, and general acid catalysis reactions in enzymes. Biochemistry. 20:3167-3177.
    • (1981) Biochemistry , vol.20 , pp. 3167-3177
    • Warshel, A.1
  • 75
    • 0007836334 scopus 로고
    • Dynamics of reactions in polar solvents. semiclassical trajectory studies of electron-transfer and proton-transfer reactions
    • Warshel, A. 1982. Dynamics of reactions in polar solvents. semiclassical trajectory studies of electron-transfer and proton-transfer reactions. J. Phys. Chem. 86:2218-2224.
    • (1982) J. Phys. Chem. , vol.86 , pp. 2218-2224
    • Warshel, A.1
  • 76
    • 0000969221 scopus 로고
    • Dynamics of enzymatic reactions
    • Warshel, A. 1984. Dynamics of enzymatic reactions. Proc. Natl. Acad. Sci. USA. 81:444-448.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 444-448
    • Warshel, A.1
  • 77
    • 0001253991 scopus 로고
    • Correlation between structure and efficiency of light-induced proton pumps
    • L. Packer, editor. Academic Press, London
    • Warshel, A. 1986. Correlation between structure and efficiency of light-induced proton pumps. In Methods in Enzymology. L. Packer, editor. Academic Press, London. 578-587.
    • (1986) Methods in Enzymology , pp. 578-587
    • Warshel, A.1
  • 79
    • 0041876227 scopus 로고    scopus 로고
    • Computer simulations of enzyme catalysis: Methods, progress, and insights
    • Warshel, A. 2003. Computer simulations of enzyme catalysis: methods, progress, and insights. Annu. Rev. Biophys. Biomol. Struct. 32:425-443.
    • (2003) Annu. Rev. Biophys. Biomol. Struct. , vol.32 , pp. 425-443
    • Warshel, A.1
  • 80
    • 33544471258 scopus 로고    scopus 로고
    • The empirical valence bond (EVB) method
    • P.R. Schreiner, editor. John Wiley & Sons, Chichester, UK
    • Warshel, A. and J. Florian. 2004. The empirical valence bond (EVB) method. In The Encyclopedia of Computational Chemistry. P.R. Schreiner, editor. John Wiley & Sons, Chichester, UK.
    • (2004) The Encyclopedia of Computational Chemistry
    • Warshel, A.1    Florian, J.2
  • 81
    • 0035707451 scopus 로고    scopus 로고
    • Dynamics of biochemical and biophysical reactions: Insight from computer simulations
    • Warshel, A., and W. W. Parson. 2001. Dynamics of biochemical and biophysical reactions: insight from computer simulations. Q. Rev. Biophys. 34:563-679.
    • (2001) Q. Rev. Biophys. , vol.34 , pp. 563-679
    • Warshel, A.1    Parson, W.W.2
  • 82
    • 0001650759 scopus 로고
    • Theoretical correlation of structure and energetics in the catalytic reaction of trypsin
    • Warshel, A., and S. Russell. 1986. Theoretical correlation of structure and energetics in the catalytic reaction of trypsin. J. Am. Chem. Soc. 108:6569-6579.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 6569-6579
    • Warshel, A.1    Russell, S.2
  • 83
    • 0024278562 scopus 로고
    • Evaluation of catalytic free energies in genetically modified proteins
    • Warshel, A., F. Sussman, and J.-K. Hwang. 1988. Evaluation of catalytic free energies in genetically modified proteins. J. Mol. Biol. 201:139-159.
    • (1988) J. Mol. Biol. , vol.201 , pp. 139-159
    • Warshel, A.1    Sussman, F.2    Hwang, J.-K.3
  • 84
    • 0043141259 scopus 로고
    • An empirical valence bond approach for comparing reactions in solutions and in enzymes
    • Warshel, A., and R. M. Weiss. 1980. An empirical valence bond approach for comparing reactions in solutions and in enzymes. J. Am. Chem. Soc. 102:6218-6226.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 6218-6226
    • Warshel, A.1    Weiss, R.M.2
  • 85
    • 0032143387 scopus 로고    scopus 로고
    • Proton translocation by bacteriorhodopsin and heme-copper oxidases
    • Wikstrom, M. 1998. Proton translocation by bacteriorhodopsin and heme-copper oxidases. Curr. Op. Struct. Biol. 8:480-488.
    • (1998) Curr. Op. Struct. Biol. , vol.8 , pp. 480-488
    • Wikstrom, M.1
  • 86
    • 0036428795 scopus 로고    scopus 로고
    • The problem of proton transfer in membranes
    • Williams, R. P. J. 2002. The problem of proton transfer in membranes. J. Theor. Biol. 219:389-396.
    • (2002) J. Theor. Biol. , vol.219 , pp. 389-396
    • Williams, R.P.J.1
  • 87
    • 0742303493 scopus 로고    scopus 로고
    • Blockade in the cell's waterway
    • Yarnell, A. 2004. Blockade in the cell's waterway. Chem. Eng. News. 82:42-44.
    • (2004) Chem. Eng. News. , vol.82 , pp. 42-44
    • Yarnell, A.1
  • 89
    • 0035253050 scopus 로고    scopus 로고
    • How water molecules pass through aquaporins
    • Zeuthen, T. 2001. How water molecules pass through aquaporins. Trends Biochem. Sci. 26:77-78.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 77-78
    • Zeuthen, T.1


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