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Volumn 86, Issue 4, 2004, Pages 1873-1889

Dynamic Water Networks in Cytochrome c Oxidase from Paracoccus denitrificans Investigated by Molecular Dynamics Simulations

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C OXIDASE; WATER;

EID: 1942423697     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(04)74254-X     Document Type: Article
Times cited : (88)

References (71)
  • 1
    • 0034719162 scopus 로고    scopus 로고
    • Redesign of the proton-pumping machinery of cytochrome c oxidase: Proton pumping does not require Glu(I-286)
    • Aagaard, A., G. Gilderson, D. A. Mills, S. Ferguson-Miller, and P. Brzezinski. 2000. Redesign of the proton-pumping machinery of cytochrome c oxidase: proton pumping does not require Glu(I-286). Biochemistry. 39:15847-15850.
    • (2000) Biochemistry , vol.39 , pp. 15847-15850
    • Aagaard, A.1    Gilderson, G.2    Mills, D.A.3    Ferguson-Miller, S.4    Brzezinski, P.5
  • 2
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energy in cell respiration
    • Babcock, G. T., and M. Wikström. 1992. Oxygen activation and the conservation of energy in cell respiration. Nature. 356:301-309.
    • (1992) Nature , vol.356 , pp. 301-309
    • Babcock, G.T.1    Wikström, M.2
  • 3
    • 0034636796 scopus 로고    scopus 로고
    • Proton translocation by cytochrome c oxidase can take place without the conserved glutamic acid in subunit I
    • Backgren, C., G. Hummer, M. Wikström, and A. Puustinen. 2000. Proton translocation by cytochrome c oxidase can take place without the conserved glutamic acid in subunit I. Biochemistry. 39:7863-7867.
    • (2000) Biochemistry , vol.39 , pp. 7863-7867
    • Backgren, C.1    Hummer, G.2    Wikström, M.3    Puustinen, A.4
  • 4
    • 0011613265 scopus 로고    scopus 로고
    • Molecular dynamics simulation of melittin in a dimyristoylphosphatidylcholine bilayer membrane
    • Berneche, S., M. Nina, and B. Roux. 1998. Molecular dynamics simulation of melittin in a dimyristoylphosphatidylcholine bilayer membrane. Biophys. J. 75:1603-1618.
    • (1998) Biophys. J. , vol.75 , pp. 1603-1618
    • Berneche, S.1    Nina, M.2    Roux, B.3
  • 5
    • 0042213113 scopus 로고    scopus 로고
    • + channel in a bilayer membrane
    • + channel in a bilayer membrane. Biophys. J. 78:2900-2917.
    • (2000) Biophys. J. , vol.78 , pp. 2900-2917
    • Berneche, S.1    Roux, B.2
  • 8
    • 0024250301 scopus 로고
    • Polar hydrogen positions in proteins: Empirical energy placement and neutron diffraction comparison
    • Brünger, A., and M. Karplus. 1988. Polar hydrogen positions in proteins: empirical energy placement and neutron diffraction comparison. Proteins. 4:148-156.
    • (1988) Proteins , vol.4 , pp. 148-156
    • Brünger, A.1    Karplus, M.2
  • 9
    • 0032130867 scopus 로고    scopus 로고
    • Proton-controlled electron transfer in cytochrome c oxidase: Functional role of the pathways through Glu 286 and Lys 362
    • Brzezinski, P., and P. Adelroth. 1998. Proton-controlled electron transfer in cytochrome c oxidase: functional role of the pathways through Glu 286 and Lys 362. Acta Physiol. Scand. Suppl. 643:7-16.
    • (1998) Acta Physiol. Scand. Suppl. , vol.643 , pp. 7-16
    • Brzezinski, P.1    Adelroth, P.2
  • 10
    • 0041765700 scopus 로고    scopus 로고
    • Redox-driven proton pumping by heme-copper oxidases
    • Brzezinski, P., and G. Larsson. 2003. Redox-driven proton pumping by heme-copper oxidases. Biochim. Biophys. Acta. 1605:1-13.
    • (2003) Biochim. Biophys. Acta , vol.1605 , pp. 1-13
    • Brzezinski, P.1    Larsson, G.2
  • 11
    • 0028814905 scopus 로고
    • Molecular dynamics simulations of the glucocorticoid receptor DNA-binding domain in complex with DNA and free in solution
    • Eriksson, M., T. Härd, and L. Nilsson. 1995. Molecular dynamics simulations of the glucocorticoid receptor DNA-binding domain in complex with DNA and free in solution. Biophys. J. 68:402-426.
    • (1995) Biophys. J. , vol.68 , pp. 402-426
    • Eriksson, M.1    Härd, T.2    Nilsson, L.3
  • 12
    • 0028850103 scopus 로고
    • Structure, thermodynamics and cooperativity of glucocorticoid receptor DNA-DNA-binding domain in complex with different response elements: Molecular dynamics and free energy perturbation study
    • Eriksson, M., and L. Nilsson. 1995. Structure, thermodynamics and cooperativity of glucocorticoid receptor DNA-DNA-binding domain in complex with different response elements: molecular dynamics and free energy perturbation study. J. Mol. Biol. 253:453-472.
    • (1995) J. Mol. Biol. , vol.253 , pp. 453-472
    • Eriksson, M.1    Nilsson, L.2
  • 14
    • 0000021902 scopus 로고    scopus 로고
    • Heme-copper terminal oxidases
    • Ferguson-Miller, S., and G. T. Babcock. 1996. Heme-copper terminal oxidases. Chem. Rev. 96:2889-2908.
    • (1996) Chem. Rev. , vol.96 , pp. 2889-2908
    • Ferguson-Miller, S.1    Babcock, G.T.2
  • 16
    • 0028913025 scopus 로고
    • 3 ubiquinol oxidase of Escherichia coli: Second-site mutations in subunit I that restore proton pumping in the mutant Asp-135→Asn
    • 3 ubiquinol oxidase of Escherichia coli: second-site mutations in subunit I that restore proton pumping in the mutant Asp-135→Asn. Biochemistry. 34:4428-4433.
    • (1995) Biochemistry , vol.34 , pp. 4428-4433
    • Garcia-Horsman, J.A.1    Puustinen, A.2    Gennis, R.B.3    Wikström, M.4
  • 17
    • 0030338497 scopus 로고    scopus 로고
    • Theoretical description of biomolecular hydration. Application to a-DNA
    • Garcia, A. E., G. Hummer, and D. M. Soumpasis. 1996. Theoretical description of biomolecular hydration. Application to a-DNA. Basic Life Sci. 64:299-308.
    • (1996) Basic Life Sci. , vol.64 , pp. 299-308
    • Garcia, A.E.1    Hummer, G.2    Soumpasis, D.M.3
  • 18
    • 0034651984 scopus 로고    scopus 로고
    • Water penetration and escape in proteins
    • Garcia, A. E., and G. Hummer. 2000. Water penetration and escape in proteins. Proteins. 38:261-272.
    • (2000) Proteins , vol.38 , pp. 261-272
    • Garcia, A.E.1    Hummer, G.2
  • 20
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
    • Goodford, P. J. 1985. A computational procedure for determining energetically favorable binding sites on biologically important macromolecules. J. Med. Chem. 28:849-857.
    • (1985) J. Med. Chem. , vol.28 , pp. 849-857
    • Goodford, P.J.1
  • 21
    • 0036708439 scopus 로고    scopus 로고
    • Structural changes during the formation of early intermediates in the bacteriorhodopsin photocycle
    • Hayashi, S., E. Tajkhorshid, and K. Schulten. 2002. Structural changes during the formation of early intermediates in the bacteriorhodopsin photocycle. Biophys. J. 83:1281-1297.
    • (2002) Biophys. J. , vol.83 , pp. 1281-1297
    • Hayashi, S.1    Tajkhorshid, E.2    Schulten, K.3
  • 22
    • 0029160249 scopus 로고
    • cam: A molecular dynamics study
    • cam: a molecular dynamics study. Biophys. J. 69:810-824.
    • (1995) Biophys. J. , vol.69 , pp. 810-824
    • Helms, V.1    Wade, R.C.2
  • 24
    • 0036707992 scopus 로고    scopus 로고
    • Structural and dynamic properties of water around acetylcholinesterase
    • Henchman, R. H., and J. A. McCammon. 2002. Structural and dynamic properties of water around acetylcholinesterase. Protein Sci. 11:2080-2090.
    • (2002) Protein Sci. , vol.11 , pp. 2080-2090
    • Henchman, R.H.1    McCammon, J.A.2
  • 25
    • 0031973948 scopus 로고    scopus 로고
    • Oxygen and proton pathways in cytochrome c oxidase
    • Hofacker, I., and K. Schulten. 1998. Oxygen and proton pathways in cytochrome c oxidase. Proteins. 30:100-107.
    • (1998) Proteins , vol.30 , pp. 100-107
    • Hofacker, I.1    Schulten, K.2
  • 26
    • 0035829539 scopus 로고    scopus 로고
    • Water conduction through the hydrophobic channel of a carbon nanotube
    • Hummer, G., J. C. Rasaiah, and J. P. Noworyta. 2001. Water conduction through the hydrophobic channel of a carbon nanotube. Nature. 414:188-190.
    • (2001) Nature , vol.414 , pp. 188-190
    • Hummer, G.1    Rasaiah, J.C.2    Noworyta, J.P.3
  • 28
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata, S., C. Ostermeier, B. Ludwig, and H. Michel. 1995. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature. 376:660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 30
    • 0031880698 scopus 로고    scopus 로고
    • The coupling of electron transfer and proton translocation: Electrostatic calculations on Paracoccus denitrificans cytochrome c oxidase
    • Kannt, A., C. R. D. Lancaster, and H. Michel. 1998. The coupling of electron transfer and proton translocation: electrostatic calculations on Paracoccus denitrificans cytochrome c oxidase. Biophys. J. 74:708-721.
    • (1998) Biophys. J. , vol.74 , pp. 708-721
    • Kannt, A.1    Lancaster, C.R.D.2    Michel, H.3
  • 31
    • 0030745897 scopus 로고    scopus 로고
    • The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter spheroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer
    • Konstantinov, A. A., S. Siletsky, D. Mitchell, A. Kaulen, and R. B. Gennis. 1997. The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter spheroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer. Proc. Natl. Acad. Sci. USA. 94:9085-9090.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9085-9090
    • Konstantinov, A.A.1    Siletsky, S.2    Mitchell, D.3    Kaulen, A.4    Gennis, R.B.5
  • 33
    • 0029053721 scopus 로고
    • Experimental evidence for hydrogen-bonded network proton transfer in bacteriorhodopsin shown by Fourier-transform infrared spectroscopy using azide as catalyst
    • Le Coutre, J., J. Tittor, D. Oesterhelt, and K. Gerwert. 1995. Experimental evidence for hydrogen-bonded network proton transfer in bacteriorhodopsin shown by Fourier-transform infrared spectroscopy using azide as catalyst. Proc. Natl. Acad. Sci. USA. 92:4962-4966.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4962-4966
    • Le Coutre, J.1    Tittor, J.2    Oesterhelt, D.3    Gerwert, K.4
  • 34
    • 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
  • 35
    • 6344260593 scopus 로고
    • An all-atom empirical energy function for the simulation of nucleic acids
    • MacKerell, A., Jr., J. Wiorkiewicz-Kuczera, and M. Karplus. 1995. An all-atom empirical energy function for the simulation of nucleic acids. J. Am. Chem. Soc. 117:11946-11975.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 11946-11975
    • MacKerell Jr., A.1    Wiorkiewicz-Kuczera, J.2    Karplus, M.3
  • 37
    • 0032573072 scopus 로고    scopus 로고
    • The mechanism of proton pumping by cytochrome c oxidase
    • Michel, H. 1998. The mechanism of proton pumping by cytochrome c oxidase. Proc. Natl. Acad. Sci. USA. 95:12819-12824.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12819-12824
    • Michel, H.1
  • 38
    • 0032318852 scopus 로고    scopus 로고
    • Proton uptake and release in cytochrome c oxidase: Separate pathways in time and space?
    • Mills, D. A., and S. Ferguson-Miller. 1998. Proton uptake and release in cytochrome c oxidase: separate pathways in time and space? Biochim. Biophys. Acta. 1365:46-52.
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 46-52
    • Mills, D.A.1    Ferguson-Miller, S.2
  • 39
    • 0037716158 scopus 로고    scopus 로고
    • Understanding the mechanism of proton movement linked to oxygen reduction in cytochrome c oxidase: Lessons from other proteins
    • Mills, D. A., and S. Ferguson-Miller. 2003. Understanding the mechanism of proton movement linked to oxygen reduction in cytochrome c oxidase: lessons from other proteins. FEBS Lett. 545:47-51.
    • (2003) FEBS Lett. , vol.545 , pp. 47-51
    • Mills, D.A.1    Ferguson-Miller, S.2
  • 40
    • 0042936805 scopus 로고
    • Self-diffusion in normal and heavy water in the range 1-45°
    • Mills, R. 1973. Self-diffusion in normal and heavy water in the range 1-45°. J. Phys. Chem. 77:685-688.
    • (1973) J. Phys. Chem. , vol.77 , pp. 685-688
    • Mills, R.1
  • 41
    • 0345613372 scopus 로고
    • Molecular mechanism for proton transport in membranes
    • Nagle, J. F., and H. J. Morowitz. 1978. Molecular mechanism for proton transport in membranes. 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
  • 42
    • 0027251833 scopus 로고
    • Area/lipid of bilayers from NMR
    • Nagle, J. F. 1993. Area/lipid of bilayers from NMR. Biophys. J. 64:1476-1481.
    • (1993) Biophys. J. , vol.64 , pp. 1476-1481
    • Nagle, J.F.1
  • 43
    • 0027936615 scopus 로고
    • Stacking-unstacking of the dinucleoside monophosphate guanylyl-3′,5′-uridine studied with molecular dynamics
    • Norberg, J., and L. Nilsson. 1994. Stacking-unstacking of the dinucleoside monophosphate guanylyl-3′,5′-uridine studied with molecular dynamics. Biophys. J. 67:812-824.
    • (1994) Biophys. J. , vol.67 , pp. 812-824
    • Norberg, J.1    Nilsson, L.2
  • 46
    • 0034703270 scopus 로고    scopus 로고
    • Modulation of glycophorin A transmembrane helix interactions by lipid bilayers: Molecular dynamics calculations
    • Petrache, H. I., A. Grossfield, K. R. MacKenzie, D. M. Engelman, and T. B. Woolf. 2000. Modulation of glycophorin A transmembrane helix interactions by lipid bilayers: molecular dynamics calculations. J, Mol. Biol. 302:727-746.
    • (2000) J, Mol. Biol. , vol.302 , pp. 727-746
    • Petrache, H.I.1    Grossfield, A.2    MacKenzie, K.R.3    Engelman, D.M.4    Woolf, T.B.5
  • 47
    • 0034643820 scopus 로고    scopus 로고
    • Tracing the D-pathway in reconstituted site-directed mutants of cytochrome c oxidase from Paracoccus denitrificans
    • Pfitzner, U., K. Hoffmeier, A. Harrenga, A. Kannt, H. Michel, E. Bamberg, O. M. Richter, and B. Ludwig. 2000. Tracing the D-pathway in reconstituted site-directed mutants of cytochrome c oxidase from Paracoccus denitrificans. Biochemistry. 39:6756-6762.
    • (2000) Biochemistry , vol.39 , pp. 6756-6762
    • Pfitzner, U.1    Hoffmeier, K.2    Harrenga, A.3    Kannt, A.4    Michel, H.5    Bamberg, E.6    Richter, O.M.7    Ludwig, B.8
  • 48
    • 0030011088 scopus 로고    scopus 로고
    • + translocation along the single-file water chain in the gramicidin A channel
    • + translocation along the single-file water chain in the gramicidin A channel. Biophys. J. 71:19-39.
    • (1996) Biophys. J. , vol.71 , pp. 19-39
    • Pomès, R.1    Roux, B.2
  • 49
    • 0032311173 scopus 로고    scopus 로고
    • Structure and dynamics of a proton shuttle in cytochrome c oxidase
    • Pomès, R., G. Hummer, and M. Wikström. 1998. Structure and dynamics of a proton shuttle in cytochrome c oxidase. Biochim. Biophys. Acta. 1365:255-260.
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 255-260
    • Pomès, R.1    Hummer, G.2    Wikström, M.3
  • 50
    • 0033524476 scopus 로고    scopus 로고
    • Proton exit from the heme-copper oxidase of Escherichia coli
    • Puustinen, A., and M. Wikström. 1999. Proton exit from the heme-copper oxidase of Escherichia coli. Proc. Natl. Acad. Sci. USA. 96:35-37.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 35-37
    • Puustinen, A.1    Wikström, M.2
  • 51
    • 0031719963 scopus 로고    scopus 로고
    • Calculation of protonation patterns in proteins with structural relaxation and molecular ensembles-application to the photosynthetic reaction center
    • Rabenstein, B., G. M. Ullmann, and E.-W. Knapp. 1998. Calculation of protonation patterns in proteins with structural relaxation and molecular ensembles-application to the photosynthetic reaction center. Eur. Biophys. J. 27:626-637.
    • (1998) Eur. Biophys. J. , vol.27 , pp. 626-637
    • Rabenstein, B.1    Ullmann, G.M.2    Knapp, E.-W.3
  • 53
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equation of motions of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J. P., G. Ciccotti, and H. J. C. Berendsen. 1977. Numerical integration of the Cartesian equation of motions of a system with constraints: molecular dynamics of n-alkanes. J. Comp. Chem. 23:327-341.
    • (1977) J. Comp. Chem. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 54
    • 0022816975 scopus 로고
    • Water structure in vitamin B12 coenzyme crystals. I. Analysis of the neutron and x-ray solvent densities
    • Savage, H. 1986. Water structure in vitamin B12 coenzyme crystals. I. Analysis of the neutron and x-ray solvent densities. Biophys. J. 50:947-956.
    • (1986) Biophys. J. , vol.50 , pp. 947-956
    • Savage, H.1
  • 55
    • 0030966534 scopus 로고    scopus 로고
    • Transmembrane helix structure, dynamics, and interactions: Multi-nanosecond molecular dynamics simulations
    • Shen, L., D. Bassolino, and T. Stouch. 1997. Transmembrane helix structure, dynamics, and interactions: multi-nanosecond molecular dynamics simulations. Biophys. J. 73:3-20.
    • (1997) Biophys. J. , vol.73 , pp. 3-20
    • Shen, L.1    Bassolino, D.2    Stouch, T.3
  • 57
    • 0036382724 scopus 로고    scopus 로고
    • The x-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides
    • Svensson-Ek, M., J. Abramson, G. Larsson, S. Tomroth, P. Brzezinski, and S. Iwata. 2002. The x-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides. J. Mol. Biol. 321:329-339.
    • (2002) J. Mol. Biol. , vol.321 , pp. 329-339
    • Svensson-Ek, M.1    Abramson, J.2    Larsson, G.3    Tomroth, S.4    Brzezinski, P.5    Iwata, S.6
  • 58
    • 0032838372 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the complex between human U1A protein and hairpin II of U1 small nuclear RNA and of free RNA in solution
    • Tang, Y., and L. Nilsson. 1999. Molecular dynamics simulations of the complex between human U1A protein and hairpin II of U1 small nuclear RNA and of free RNA in solution. Biophys. J. 77:1284-1305.
    • (1999) Biophys. J. , vol.77 , pp. 1284-1305
    • Tang, Y.1    Nilsson, L.2
  • 59
    • 0027491552 scopus 로고
    • Substitution of asparagine for aspartate-135 in subunit I of the cytochrome bo ubiquinol oxidase of Escherichia coli eliminates proton-pumping activity
    • Thomas, J. W., A. Puustinen, J. O. Alben, R. B. Gennis, and M. Wikström. 1993. Substitution of asparagine for aspartate-135 in subunit I of the cytochrome bo ubiquinol oxidase of Escherichia coli eliminates proton-pumping activity. Biochemistry. 32:10923-10928.
    • (1993) Biochemistry , vol.32 , pp. 10923-10928
    • Thomas, J.W.1    Puustinen, A.2    Alben, J.O.3    Gennis, R.B.4    Wikström, M.5
  • 60
    • 0031860932 scopus 로고    scopus 로고
    • A molecular dynamics study of the pores formed by Escherichia coli OmpF porin in a fully hydrated palmitoyloleoylphosphatidylcholine bilayer
    • Tieleman, D. P., and H. J. C. Berendsen. 1998. A molecular dynamics study of the pores formed by Escherichia coli OmpF porin in a fully hydrated palmitoyloleoylphosphatidylcholine bilayer. Biophys. J. 74:2786-2801.
    • (1998) Biophys. J. , vol.74 , pp. 2786-2801
    • Tieleman, D.P.1    Berendsen, H.J.C.2
  • 62
    • 0027515072 scopus 로고
    • Molecular dynamics simulations of a lipid bilayer and of hexadecane: An investigation of membrane fluidity
    • Venable, R. M., Y. Zhang, B. J. Hardy, and R. W. Pastor. 1993. Molecular dynamics simulations of a lipid bilayer and of hexadecane: an investigation of membrane fluidity. Science. 262:223-226.
    • (1993) Science , vol.262 , pp. 223-226
    • Venable, R.M.1    Zhang, Y.2    Hardy, B.J.3    Pastor, R.W.4
  • 63
    • 0025442659 scopus 로고
    • Solvation of the active site of cytochrome P450 cam
    • Wade, R. C. 1990. Solvation of the active site of cytochrome P450 cam. J, Comput. Aided Mol. Des. 4:199-204.
    • (1990) J, Comput. Aided Mol. Des. , vol.4 , pp. 199-204
    • Wade, R.C.1
  • 64
    • 0027510004 scopus 로고
    • Further development of hydrogen bond functions for use in determining energetically favorable binding sites on molecules of known structure. 2. Ligand probe groups with the ability to form more than two hydrogen bonds
    • Wade, R. C., and P. J. Goodford. 1993. Further development of hydrogen bond functions for use in determining energetically favorable binding sites on molecules of known structure. 2. Ligand probe groups with the ability to form more than two hydrogen bonds. J. Med. Chem. 36: 148-156.
    • (1993) J. Med. Chem. , vol.36 , pp. 148-156
    • Wade, R.C.1    Goodford, P.J.2
  • 65
    • 0017358508 scopus 로고
    • Proton pump coupled to cytochrome c oxidase in mitochondria
    • Wikström, M. K. F. 1977. Proton pump coupled to cytochrome c oxidase in mitochondria. Nature. 266:271-273.
    • (1977) Nature , vol.266 , pp. 271-273
    • Wikström, M.K.F.1
  • 66
    • 0037726809 scopus 로고    scopus 로고
    • Water-gated mechanism of proton translocation by cytochrome c oxidase
    • Wikström, M., M. I. Verkhovsky, and G. Hummer. 2003. Water-gated mechanism of proton translocation by cytochrome c oxidase. Biochim. Biophys. Acta. 1604:61-65.
    • (2003) Biochim. Biophys. Acta , vol.1604 , pp. 61-65
    • Wikström, M.1    Verkhovsky, M.I.2    Hummer, G.3
  • 67
    • 0028020035 scopus 로고
    • Molecular dynamics simulation of the gramicidin channel in a phospholipid bilayer
    • Woolf, T. B., and B. Roux. 1994. Molecular dynamics simulation of the gramicidin channel in a phospholipid bilayer. Proc. Natl. Acad. Sci. USA. 91:11631-11635.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11631-11635
    • Woolf, T.B.1    Roux, B.2
  • 68
    • 0030038849 scopus 로고    scopus 로고
    • Structure, energetics, and dynamics of lipid-protein interactions: A molecular dynamics study of the gramicidin A channel in a DMPC bilayer
    • Woolf, T. B., and B. Roux. 1996. Structure, energetics, and dynamics of lipid-protein interactions: a molecular dynamics study of the gramicidin A channel in a DMPC bilayer. Proteins. 24:92-114.
    • (1996) Proteins , vol.24 , pp. 92-114
    • Woolf, T.B.1    Roux, B.2
  • 69
    • 0034640504 scopus 로고    scopus 로고
    • Proton pumping by cytochrome oxidase: Progress, problems and postulates
    • Zaslavsky, D., and R. B. Gennis. 2000. Proton pumping by cytochrome oxidase: progress, problems and postulates. Biochim. Biophys. Acta. 1458:164-179.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 164-179
    • Zaslavsky, D.1    Gennis, R.B.2
  • 71
    • 0029937870 scopus 로고    scopus 로고
    • Hydrophilicity of cavities in proteins
    • Zhang, L., and J. Hermans. 1996. Hydrophilicity of cavities in proteins. Proteins. 24:433-438.
    • (1996) Proteins , vol.24 , pp. 433-438
    • Zhang, L.1    Hermans, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.