메뉴 건너뛰기




Volumn 103, Issue 6, 2012, Pages 1305-1314

Hydrogen-bonded networks along and bifurcation of the E-pathway in quinol: Fumarate reductase

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMIC ACID; LIGAND; OXIDOREDUCTASE; PROPIONIC ACID; PROPIONIC ACID DERIVATIVE; PROTON; QUINOL FUMARATE REDUCTASE; WATER;

EID: 84866480328     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.07.037     Document Type: Article
Times cited : (8)

References (81)
  • 1
    • 0018183608 scopus 로고
    • Fumarate as terminal acceptor of phosphorylative electron transport
    • A. Kröger Fumarate as terminal acceptor of phosphorylative electron transport Biochim. Biophys. Acta 505 1978 129 145 (Pubitemid 9029614)
    • (1978) Biochimica et Biophysica Acta , vol.505 , Issue.2 , pp. 129-145
    • Kroger, A.1
  • 2
    • 84866492956 scopus 로고    scopus 로고
    • The superfamily of succinate:quinone oxidoreductases and its implications for the cyanobacterial enzymes
    • G.A. Peschek, C. Obinger, G. Renger, Springer Dordrecht, The Netherlands
    • C.R.D. Lancaster The superfamily of succinate:quinone oxidoreductases and its implications for the cyanobacterial enzymes G.A. Peschek, C. Obinger, G. Renger, Bioenergetic Processes of Cyanobacteria 2011 Springer Dordrecht, The Netherlands 469 511
    • (2011) Bioenergetic Processes of Cyanobacteria , pp. 469-511
    • Lancaster, C.R.D.1
  • 3
    • 0037122940 scopus 로고    scopus 로고
    • Succinate: Quinone oxidoreductases from ε-proteobacteria
    • C.R.D. Lancaster, and J. Simon Succinate: quinone oxidoreductases from ε-proteobacteria Biochim. Biophys. Acta 1553 2002 84 101
    • (2002) Biochim. Biophys. Acta , vol.1553 , pp. 84-101
    • Lancaster, C.R.D.1    Simon, J.2
  • 4
    • 33645568742 scopus 로고    scopus 로고
    • Heterologous production in Wolinella succinogenes and characterization of the quinol:fumarate reductase enzymes from Helicobacter pylori and Campylobacter jejuni
    • M. Mileni, and F. MacMillan C.R. Lancaster Heterologous production in Wolinella succinogenes and characterization of the quinol:fumarate reductase enzymes from Helicobacter pylori and Campylobacter jejuni Biochem. J. 395 2006 191 201
    • (2006) Biochem. J. , vol.395 , pp. 191-201
    • Mileni, M.1    MacMillan, F.2    Lancaster, C.R.3
  • 5
    • 0010049951 scopus 로고    scopus 로고
    • Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution
    • C.R.D. Lancaster, and A. Kröger H. Michel Structure of fumarate reductase from Wolinella succinogenes at 2.2 Å resolution Nature 402 1999 377 385 (Pubitemid 129544818)
    • (1999) Nature , vol.402 , Issue.6760 , pp. 377-385
    • Lancaster, C.R.D.1    Kroger, A.2    Auer, M.3    Michel, H.4
  • 6
    • 33750218146 scopus 로고    scopus 로고
    • Evidence for transmembrane proton transfer in a dihaem-containing membrane protein complex
    • DOI 10.1038/sj.emboj.7601361, PII 7601361
    • M.G. Madej, and H.R. Nasiri C.R. Lancaster Evidence for transmembrane proton transfer in a dihaem-containing membrane protein complex EMBO J. 25 2006 4963 4970 (Pubitemid 44607040)
    • (2006) EMBO Journal , vol.25 , Issue.20 , pp. 4963-4970
    • Madej, M.G.1    Nasiri, H.R.2    Hilgendorff, N.S.3    Schwalbe, H.4    Lancaster, C.R.D.5
  • 7
    • 0034831591 scopus 로고    scopus 로고
    • A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction
    • DOI 10.1046/j.1432-1327.2001.02053.x
    • C.R.D. Lancaster, R. Gross, and J. Simon A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction Eur. J. Biochem. 268 2001 1820 1827 (Pubitemid 32862717)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.6 , pp. 1820-1827
    • Lancaster, C.R.D.1    Gross, R.2    Simon, J.3
  • 8
    • 0034700104 scopus 로고    scopus 로고
    • Essential role of Glu-C66 for menaquinol oxidation indicates transmembrane electrochemical potential generation by Wolinella succinogenes fumarate reductase
    • C.R.D. Lancaster, and R. Gross A. Kröger Essential role of Glu-C66 for menaquinol oxidation indicates transmembrane electrochemical potential generation by Wolinella succinogenes fumarate reductase Proc. Natl. Acad. Sci. USA 97 2000 13051 13056
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13051-13056
    • Lancaster, C.R.D.1    Gross, R.2    Kröger, A.3
  • 9
    • 0037064218 scopus 로고    scopus 로고
    • Wolinella succinogenes quinol: Fumarate reductase: 2.2-Å resolution crystal structure and the E-pathway hypothesis of coupled transmembrane proton and electron transfer
    • C.R.D. Lancaster Wolinella succinogenes quinol: fumarate reductase: 2.2-Å resolution crystal structure and the E-pathway hypothesis of coupled transmembrane proton and electron transfer Biochim. Biophys. Acta 1565 2002 215 231
    • (2002) Biochim. Biophys. Acta , vol.1565 , pp. 215-231
    • Lancaster, C.R.D.1
  • 11
    • 10044230751 scopus 로고    scopus 로고
    • Calculated coupling of transmembrane electron and proton transfer in dihemic quinol:fumarate reductase
    • DOI 10.1529/biophysj.104.042945
    • A.H. Haas, and C.R.D. Lancaster Calculated coupling of transmembrane electron and proton transfer in dihemic quinol:fumarate reductase Biophys. J. 87 2004 4298 4315 (Pubitemid 39602931)
    • (2004) Biophysical Journal , vol.87 , Issue.6 , pp. 4298-4315
    • Haas, A.H.1    Lancaster, C.R.D.2
  • 12
    • 27144473873 scopus 로고    scopus 로고
    • FTIR difference spectra of Wolinella succinogenes quinol:fumarate reductase support a key role of Glu C180 within the "E-pathway hypothesis" of coupled transmembrane electron and proton transfer
    • DOI 10.1021/bi051011d
    • A.H. Haas, and U.S. Sauer C.R. Lancaster FTIR difference spectra of Wolinella succinogenes quinol:fumarate reductase support a key role of Glu-C180 within the "E-pathway hypothesis" of coupled transmembrane electron and proton transfer Biochemistry 44 2005 13949 13961 (Pubitemid 41507475)
    • (2005) Biochemistry , vol.44 , Issue.42 , pp. 13949-13961
    • Haas, A.H.1    Sauer, U.S.2    Gross, R.3    Simon, J.4    Mantele, W.5    Lancaster, C.R.D.6
  • 14
    • 66349088622 scopus 로고    scopus 로고
    • Limited reversibility of transmembrane proton transfer assisting transmembrane electron transfer in a dihaem-containing succinate:quinone oxidoreductase
    • M.G. Madej, and F.G. Müller C.R.D. Lancaster Limited reversibility of transmembrane proton transfer assisting transmembrane electron transfer in a dihaem-containing succinate:quinone oxidoreductase Biochim. Biophys. Acta 1787 2009 593 600
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 593-600
    • Madej, M.G.1    Müller, F.G.2    Lancaster, C.R.D.3
  • 15
    • 53849112973 scopus 로고    scopus 로고
    • Electroneutral and electrogenic catalysis by dihaem-containing succinate:quinone oxidoreductases
    • C.R.D. Lancaster, and E. Herzog P.G. Schleidt Electroneutral and electrogenic catalysis by dihaem-containing succinate:quinone oxidoreductases Biochem. Soc. Trans. 36 2008 996 1000
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 996-1000
    • Lancaster, C.R.D.1    Herzog, E.2    Schleidt, P.G.3
  • 16
    • 36849126204 scopus 로고
    • Studies in molecular dynamics. I. General method
    • B.J. Alder, and T.E. Wainwright Studies in molecular dynamics. I. General method J. Chem. Phys. 31 1959 459 466
    • (1959) J. Chem. Phys. , vol.31 , pp. 459-466
    • Alder, B.J.1    Wainwright, T.E.2
  • 18
    • 0036725277 scopus 로고    scopus 로고
    • Molecular dynamics simulations of biomolecules
    • DOI 10.1038/nsb0902-646
    • M. Karplus, and J.A. McCammon Molecular dynamics simulations of biomolecules Nat. Struct. Biol. 9 2002 646 652 (Pubitemid 34977295)
    • (2002) Nature Structural Biology , vol.9 , Issue.9 , pp. 646-652
    • Karplus, M.1    McCammon, J.A.2
  • 19
    • 28244492966 scopus 로고    scopus 로고
    • Application of classical molecular dynamics for evaluation of proton transfer mechanism on a protein
    • DOI 10.1016/j.bbabio.2005.09.005, PII S0005272805002288
    • R. Friedman, E. Nachliel, and M. Gutman Application of classical molecular dynamics for evaluation of proton transfer mechanism on a protein Biochim. Biophys. Acta 1710 2005 67 77 (Pubitemid 41714002)
    • (2005) Biochimica et Biophysica Acta - Bioenergetics , vol.1710 , Issue.2-3 , pp. 67-77
    • Friedman, R.1    Nachliel, E.2    Gutman, M.3
  • 20
    • 33644989063 scopus 로고    scopus 로고
    • Computer simulation of proton solvation and transport in aqueous and biomolecular systems
    • G.A. Voth Computer simulation of proton solvation and transport in aqueous and biomolecular systems Acc. Chem. Res. 39 2006 143 150
    • (2006) Acc. Chem. Res. , vol.39 , pp. 143-150
    • Voth, G.A.1
  • 21
    • 1942423697 scopus 로고    scopus 로고
    • Dynamic Water Networks in Cytochrome c Oxidase from Paracoccus denitrificans Investigated by Molecular Dynamics Simulations
    • E. Olkhova, and M.C. Hutter H. Michel Dynamic water networks in cytochrome c oxidase from Paracoccus denitrificans investigated by molecular dynamics simulations Biophys. J. 86 2004 1873 1889 (Pubitemid 38524385)
    • (2004) Biophysical Journal , vol.86 , Issue.4 , pp. 1873-1889
    • Olkhova, E.1    Hutter, M.C.2    Lill, M.A.3    Helms, V.4    Michel, H.5
  • 23
    • 69549101850 scopus 로고    scopus 로고
    • Kinetic gating of the proton pump in cytochrome c oxidase
    • Y.C. Kim, M. Wikström, and G. Hummer Kinetic gating of the proton pump in cytochrome c oxidase Proc. Natl. Acad. Sci. USA 106 2009 13707 13712
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 13707-13712
    • Kim, Y.C.1    Wikström, M.2    Hummer, G.3
  • 24
    • 11144304570 scopus 로고    scopus 로고
    • A molecular dynamics study of water chain formation in the proton-conducting K channel of cytochrome c oxidase
    • DOI 10.1016/j.bbabio.2004.10.004, PII S0005272804002816
    • R.I. Cukier A molecular dynamics study of water chain formation in the proton-conducting K channel of cytochrome c oxidase Biochim. Biophys. Acta 1706 2005 134 146 (Pubitemid 40037769)
    • (2005) Biochimica et Biophysica Acta - Bioenergetics , vol.1706 , Issue.1-2 , pp. 134-146
    • Cukier, R.I.1
  • 25
    • 1142310689 scopus 로고    scopus 로고
    • Dynamics of Water Molecules in the Bacteriorhodopsin Trimer in Explicit Lipid/Water Environment
    • C. Kandt, J. Schlitter, and K. Gerwert Dynamics of water molecules in the bacteriorhodopsin trimer in explicit lipid/water environment Biophys. J. 86 2004 705 717 (Pubitemid 38209519)
    • (2004) Biophysical Journal , vol.86 , Issue.2 , pp. 705-717
    • Kandt, C.1    Schlitter, J.2    Gerwert, K.3
  • 26
    • 77956589405 scopus 로고    scopus 로고
    • Directional proton transfer in membrane proteins achieved through protonated protein-bound water molecules: A proton diode
    • S. Wolf, and E. Freier K. Gerwert Directional proton transfer in membrane proteins achieved through protonated protein-bound water molecules: a proton diode Angew. Chem. Int. Ed. Engl. 49 2010 6889 6893
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , pp. 6889-6893
    • Wolf, S.1    Freier, E.2    Gerwert, K.3
  • 27
    • 0028097538 scopus 로고
    • Ordered water in macromolecular structure
    • DOI 10.1016/S0959-440X(94)90178-3
    • A.P. Karplus, and C. Faerman Ordered water in macromolecular structure Curr. Opin. Struct. Biol. 4 1994 770 776 (Pubitemid 24325299)
    • (1994) Current Opinion in Structural Biology , vol.4 , Issue.5 , pp. 770-776
    • Karplus, P.A.1    Faerman, C.2
  • 28
    • 0033081137 scopus 로고    scopus 로고
    • How many water molecules can be detected by protein crystallography?
    • DOI 10.1107/S0907444998012086
    • O. Carugo, and D. Bordo How many water molecules can be detected by protein crystallography? Acta Crystallogr. D Biol. Crystallogr. 55 1999 479 483 (Pubitemid 29083721)
    • (1999) Acta Crystallographica Section D: Biological Crystallography , vol.55 , Issue.2 , pp. 479-483
    • Carugo, O.1    Bordo, D.2
  • 31
    • 0027082924 scopus 로고
    • Internal water molecules and H-bonding in biological macromolecules: A review of structural features with functional implications
    • E. Meyer Internal water molecules and H-bonding in biological macromolecules: a review of structural features with functional implications Protein Sci. 1 1992 1543 1562 (Pubitemid 23047471)
    • (1992) Protein Science , vol.1 , Issue.12 , pp. 1543-1562
    • Meyer, E.1
  • 32
    • 77956527543 scopus 로고    scopus 로고
    • + site and the sequence of extracellular binding events in the glutamate transporter
    • + site and the sequence of extracellular binding events in the glutamate transporter Biophys. J. 99 2010 1416 1425
    • (2010) Biophys. J. , vol.99 , pp. 1416-1425
    • Huang, Z.1    Tajkhorshid, E.2
  • 33
    • 34447256364 scopus 로고    scopus 로고
    • Conformational Change in an MFS Protein: MD Simulations of LacY
    • DOI 10.1016/j.str.2007.06.004, PII S0969212607002092
    • J. Holyoake, and M.S.P. Sansom Conformational change in an MFS protein: MD simulations of LacY Structure 15 2007 873 884 (Pubitemid 47042433)
    • (2007) Structure , vol.15 , Issue.7 , pp. 873-884
    • Holyoake, J.1    Sansom, M.S.P.2
  • 34
    • 0036606442 scopus 로고    scopus 로고
    • Water in protein cavities: A procedure to identify internal water and exchange pathways and application to fatty acid-binding protein
    • DOI 10.1002/prot.10079
    • D. Bakowies, and W.F. Van Gunsteren Water in protein cavities: a procedure to identify internal water and exchange pathways and application to fatty acid-binding protein Proteins 47 2002 534 545 (Pubitemid 34614733)
    • (2002) Proteins: Structure, Function and Genetics , vol.47 , Issue.4 , pp. 534-545
    • Bakowies, D.1    Van Gunsteren, W.F.2
  • 35
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • B. Lee, and F.M. Richards The interpretation of protein structures: estimation of static accessibility J. Mol. Biol. 55 1971 379 400
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 36
    • 0017429069 scopus 로고
    • Areas, volumes, packing and protein structure
    • F.M. Richards Areas, volumes, packing and protein structure Annu. Rev. Biophys. Bioeng. 6 1977 151 176
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 37
    • 0000538815 scopus 로고
    • Analytical molecular surface calculation
    • M.L. Connolly Analytical molecular surface calculation J. Appl. Cryst. 16 1983 548 558
    • (1983) J. Appl. Cryst. , vol.16 , pp. 548-558
    • Connolly, M.L.1
  • 38
    • 33846417622 scopus 로고    scopus 로고
    • Protein dynamics tightly connected to the dynamics of surrounding and internal water molecules
    • V. Helms Protein dynamics tightly connected to the dynamics of surrounding and internal water molecules ChemPhysChem 8 2007 23 33
    • (2007) ChemPhysChem , vol.8 , pp. 23-33
    • Helms, V.1
  • 39
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
    • DOI 10.1021/jm00145a002
    • P.J. Goodford A computational procedure for determining energetically favorable binding sites on biologically important macromolecules J. Med. Chem. 28 1985 849 857 (Pubitemid 15012490)
    • (1985) Journal of Medicinal Chemistry , vol.28 , Issue.7 , pp. 849-857
    • Goodford, P.J.1
  • 41
    • 0033527325 scopus 로고    scopus 로고
    • Molecular dynamics of mouse acetylcholinesterase complexed with huperzine A
    • DOI 10.1002/(SICI)1097-0282(19991005)50:4<347::AID-BIP1>3.0.CO;2-R
    • S. Tara, and V. Helms J.A. McCammon Molecular dynamics of mouse acetylcholinesterase complexed with huperzine A Biopolymers 50 1999 347 359 (Pubitemid 29390076)
    • (1999) Biopolymers , vol.50 , Issue.4 , pp. 347-359
    • Tara, S.1    Helms, V.2    Straatsma, T.P.3    McCammon, J.A.4
  • 42
    • 0028228418 scopus 로고
    • The entropic cost of bound water in crystals and biomolecules
    • J.D. Dunitz The entropic cost of bound water in crystals and biomolecules Science 264 1994 670 (Pubitemid 24186849)
    • (1994) Science , vol.264 , Issue.5159 , pp. 670
    • Dunitz, J.D.1
  • 43
    • 0029937870 scopus 로고    scopus 로고
    • Hydrophilicity of cavities in proteins
    • DOI 10.1002/(SICI)1097-0134(199604)24:4<433::AID-PROT3>3.0.CO;2-F
    • L. Zhang, and J. Hermans Hydrophilicity of cavities in proteins Proteins 24 1996 433 438 (Pubitemid 26122057)
    • (1996) Proteins: Structure, Function and Genetics , vol.24 , Issue.4 , pp. 433-438
    • Zhang, L.1    Hermans, J.2
  • 45
    • 0029160249 scopus 로고
    • Thermodynamics of water mediating protein-ligand interactions in cytochrome P450cam: A molecular dynamics study
    • V. Helms, and R.C. Wade Thermodynamics of water mediating protein-ligand interactions in cytochrome P450cam: a molecular dynamics study Biophys. J. 69 1995 810 824
    • (1995) Biophys. J. , vol.69 , pp. 810-824
    • Helms, V.1    Wade, R.C.2
  • 46
    • 41049115037 scopus 로고    scopus 로고
    • Computation of binding free energy with molecular dynamics and grand canonical Monte Carlo simulations
    • Y. Deng, and B. Roux Computation of binding free energy with molecular dynamics and grand canonical Monte Carlo simulations J. Chem. Phys. 128 2008 115103
    • (2008) J. Chem. Phys. , vol.128 , pp. 115103
    • Deng, Y.1    Roux, B.2
  • 47
    • 0032529586 scopus 로고    scopus 로고
    • Hydration energy landscape of the active site cavity in cytochrome P450cam
    • DOI 10.1002/(SICI)1097-0134(19980815)32:3<381::AID-PROT12>3.0.CO;2- 5
    • V. Helms, and R.C. Wade Hydration energy landscape of the active site cavity in cytochrome P450cam Proteins 32 1998 381 396 (Pubitemid 28360833)
    • (1998) Proteins: Structure, Function and Genetics , vol.32 , Issue.3 , pp. 381-396
    • Helms, V.1    Wade, R.C.2
  • 48
    • 0032054675 scopus 로고    scopus 로고
    • Computational alchemy to calculate absolute protein-Ligand binding free energy
    • DOI 10.1021/ja9738539
    • V. Helms, and R.C. Wade Computational alchemy to calculate absolute protein-ligand binding free energy J. Am. Chem. Soc. 120 1998 2710 2713 (Pubitemid 28191625)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.12 , pp. 2710-2713
    • Helms, V.1    Wade, R.C.2
  • 49
    • 41549149586 scopus 로고    scopus 로고
    • Biomolecular simulations of membranes: Physical properties from different force fields
    • S.W.I. Siu, and R. Vácha R.A. Böckmann Biomolecular simulations of membranes: physical properties from different force fields J. Chem. Phys. 128 2008 125103
    • (2008) J. Chem. Phys. , vol.128 , pp. 125103
    • Siu, S.W.I.1    Vácha, R.2    Böckmann, R.A.3
  • 52
    • 0001216964 scopus 로고    scopus 로고
    • A second generation force field for the simulation of proteins, nucleic acids, and organic molecules (vol 117, pg 5179, 1995)
    • 2309-2309
    • W.D. Cornell, and P. Cieplak P.A. Kollman A second generation force field for the simulation of proteins, nucleic acids, and organic molecules (vol 117, pg 5179, 1995) J. Am. Chem. Soc. 118 1996 2309-2309
    • (1996) J. Am. Chem. Soc. , vol.118
    • Cornell, W.D.1    Cieplak, P.2    Kollman, P.A.3
  • 55
    • 33750587438 scopus 로고
    • Molecular dynamics with coupling to an external bath
    • H.J.C. Berendsen, and J.P.M. Postma J.R. Haak Molecular dynamics with coupling to an external bath J. Chem. Phys. 81 1984 3684 3690
    • (1984) J. Chem. Phys. , vol.81 , pp. 3684-3690
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Haak, J.R.3
  • 56
    • 67049114092 scopus 로고    scopus 로고
    • Distance-dependent proton transfer along water wires connecting acid-base pairs
    • M.J. Cox, and R.L.A. Timmer N. Agmon Distance-dependent proton transfer along water wires connecting acid-base pairs J. Phys. Chem. A 113 2009 6599 6606
    • (2009) J. Phys. Chem. A , vol.113 , pp. 6599-6606
    • Cox, M.J.1    Timmer, R.L.A.2    Agmon, N.3
  • 57
    • 35948939425 scopus 로고    scopus 로고
    • On the role of water in intermolecular proton-transfer reactions
    • DOI 10.1021/ja069265p
    • B.J. Siwick, and H.J. Bakker On the role of water in intermolecular proton-transfer reactions J. Am. Chem. Soc. 129 2007 13412 13420 (Pubitemid 350071769)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.44 , pp. 13412-13420
    • Siwick, B.J.1    Bakker, H.J.2
  • 58
    • 38749091716 scopus 로고    scopus 로고
    • Long-range proton transfer in aqueous acid - Base reactions
    • DOI 10.1021/jp075663i
    • B.J. Siwick, M.J. Cox, and H.J. Bakker Long-range proton transfer in aqueous acid-base reactions J. Phys. Chem. B 112 2008 378 389 (Pubitemid 351184611)
    • (2008) Journal of Physical Chemistry B , vol.112 , Issue.2 , pp. 378-389
    • Siwick, B.J.1    Cox, M.J.2    Bakker, H.J.3
  • 59
    • 67749114486 scopus 로고    scopus 로고
    • Tightly connected water wires facilitate fast proton uptake at the proton entrance of proton pumping proteins
    • W. Gu, and V. Helms Tightly connected water wires facilitate fast proton uptake at the proton entrance of proton pumping proteins J. Am. Chem. Soc. 131 2009 2080 2081
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 2080-2081
    • Gu, W.1    Helms, V.2
  • 60
    • 69349101503 scopus 로고    scopus 로고
    • Quantifying uncertainty and sampling quality in biomolecular simulations
    • A.W. Ralph, Elsevier New York
    • A. Grossfield, and D.M. Zuckerman Quantifying uncertainty and sampling quality in biomolecular simulations A.W. Ralph, Annual Reports in Computational Chemistry 2009 Elsevier New York 23 48
    • (2009) Annual Reports in Computational Chemistry , pp. 23-48
    • Grossfield, A.1    Zuckerman, D.M.2
  • 61
    • 0019319527 scopus 로고
    • Isolation and functional aspects of the fumarate reductase involved in the phosphorylative electron transport of Vibrio succinogenes
    • G. Unden, H. Hackenberg, and A. Kröger Isolation and functional aspects of the fumarate reductase involved in the phosphorylative electron transport of Vibrio succinogenes Biochim. Biophys. Acta 591 1980 275 288
    • (1980) Biochim. Biophys. Acta , vol.591 , pp. 275-288
    • Unden, G.1    Hackenberg, H.2    Kröger, A.3
  • 62
    • 27144507189 scopus 로고    scopus 로고
    • Crystallization of Wolinella succinogenes quinol:fumarate reductase
    • C. Hunte, H. Schägger, G. von Jagow, 2nd ed. Academic Press San Diego
    • C.R.D. Lancaster Crystallization of Wolinella succinogenes quinol:fumarate reductase C. Hunte, H. Schägger, G. von Jagow, Membrane Protein Purification and Crystallization: A Practical Guide 2nd ed. 2003 Academic Press San Diego 219 228
    • (2003) Membrane Protein Purification and Crystallization: A Practical Guide , pp. 219-228
    • Lancaster, C.R.D.1
  • 63
    • 0032518289 scopus 로고    scopus 로고
    • Deletion and site-directed mutagenesis of the Wolinella succinogenes fumarate reductase operon
    • DOI 10.1046/j.1432-1327.1998.2510418.x
    • J. Simon, and R. Gross A. Kröger Deletion and site-directed mutagenesis of the Wolinella succinogenes fumarate reductase operon Eur. J. Biochem. 251 1998 418 426 (Pubitemid 28080942)
    • (1998) European Journal of Biochemistry , vol.251 , Issue.1-2 , pp. 418-426
    • Simon, J.1    Gross, R.2    Ringel, M.3    Schmidt, E.4    Kroger, A.5
  • 64
    • 60649087951 scopus 로고    scopus 로고
    • Production, characterization and determination of the real catalytic properties of the putative "succinate dehydrogenase" from Wolinella succinogenes
    • H.D. Juhnke, and H. Hiltscher C.R. Lancaster Production, characterization and determination of the real catalytic properties of the putative "succinate dehydrogenase" from Wolinella succinogenes Mol. Microbiol. 71 2009 1088 1101
    • (2009) Mol. Microbiol. , vol.71 , pp. 1088-1101
    • Juhnke, H.D.1    Hiltscher, H.2    Lancaster, C.R.3
  • 65
    • 0020322828 scopus 로고
    • Biosynthetic pathways of Vibrio succinogenes growing with fumarate as terminal electron acceptor and sole carbon source
    • DOI 10.1007/BF00405882
    • M. Bronder, and H. Mell A. Kröger Biosynthetic pathways of Vibrio succinogenes growing with fumarate as terminal electron acceptor and sole carbon source Arch. Microbiol. 131 1982 216 223 (Pubitemid 12066925)
    • (1982) Archives of Microbiology , vol.131 , Issue.3 , pp. 216-223
    • Bronder, M.1    Mell, H.2    Stupperich, E.3    Kroeger, A.4
  • 66
    • 0027411256 scopus 로고
    • Regulation of anaerobic respiratory pathways in Wolinella succinogenes by the presence of electron acceptors
    • J.P. Lorenzen, A. Kröger, and G. Unden Regulation of the anaerobic respiratory pathways in Wolinella succinogenes by the presence of electron acceptors Arch. Microbiol. 159 1993 477 483 (Pubitemid 23113718)
    • (1993) Archives of Microbiology , vol.159 , Issue.5 , pp. 477-483
    • Lorenzen, J.P.1    Kroger, A.2    Unden, G.3
  • 67
    • 84931997607 scopus 로고
    • Elimination of errors caused by turbidity in the determination of protein by the biuret method
    • C. Bode, H. Goebell, and E. Stähler Elimination of errors caused by turbidity in the determination of protein by the biuret method Z. Klin. Chem. Klin. Biochem. 6 1968 418 422
    • (1968) Z. Klin. Chem. Klin. Biochem. , vol.6 , pp. 418-422
    • Bode, C.1    Goebell, H.2    Stähler, E.3
  • 68
    • 0019783989 scopus 로고
    • The function of the subunits of the fumarate reductase complex of Vibrio succinogenes
    • G. Unden, and A. Kröger The function of the subunits of the fumarate reductase complex of Vibrio succinogenes Eur. J. Biochem. 120 1981 577 584 (Pubitemid 12189048)
    • (1981) European Journal of Biochemistry , vol.120 , Issue.3 , pp. 577-584
    • Unden, G.1    Kroger, A.2
  • 69
    • 0038670109 scopus 로고    scopus 로고
    • Infrared and Fourier transform infrared spectroscopy
    • A.J. Hoff, J. Amesz, Kluwer Dordrecht, The Netherlands
    • W. Mäntele Infrared and Fourier transform infrared spectroscopy A.J. Hoff, J. Amesz, Biophysical Techniques in Photosynthesis 1996 Kluwer Dordrecht, The Netherlands 137 160
    • (1996) Biophysical Techniques in Photosynthesis , pp. 137-160
    • Mäntele, W.1
  • 70
    • 0025115245 scopus 로고
    • Redox-linked conformational changes in proteins detected by a combination of infrared spectroscopy and protein electrochemistry. Evaluation of the technique with cytochrome c
    • D. Moss, and E. Nabedryk W. Mäntele Redox-linked conformational changes in proteins detected by a combination of infrared spectroscopy and protein electrochemistry. Evaluation of the technique with cytochrome c Eur. J. Biochem. 187 1990 565 572 (Pubitemid 20074919)
    • (1990) European Journal of Biochemistry , vol.187 , Issue.3 , pp. 565-572
    • Moss, D.1    Nabedryk, E.2    Breton, J.3    Mantele, W.4
  • 71
    • 0027316209 scopus 로고
    • Reaction-induced infrared difference spectroscopy for the study of protein function and reaction mechanisms
    • DOI 10.1016/0968-0004(93)90186-Q
    • W. Mäntele Reaction-induced infrared difference spectroscopy for the study of protein function and reaction mechanisms Trends Biochem. Sci. 18 1993 197 202 (Pubitemid 23167621)
    • (1993) Trends in Biochemical Sciences , vol.18 , Issue.6 , pp. 197-202
    • Mantele, W.1
  • 72
    • 0026410605 scopus 로고
    • An electrochemical assay for the characterization of redox proteins from biological electron transfer chains
    • F. Baymann, D.A. Moss, and W. Mäntele An electrochemical assay for the characterization of redox proteins from biological electron transfer chains Anal. Biochem. 199 1991 269 274
    • (1991) Anal. Biochem. , vol.199 , pp. 269-274
    • Baymann, F.1    Moss, D.A.2    Mäntele, W.3
  • 73
    • 0031572857 scopus 로고    scopus 로고
    • The coupling of light-induced electron transfer and proton uptake as derived from crystal structures of reaction centres from Rhodopseudomonas viridis modified at the binding site of the secondary quinone, Q(B)
    • B Structure 5 1997 1339 1359 (Pubitemid 27484476)
    • (1997) Structure , vol.5 , Issue.10 , pp. 1339-1359
    • Roy, C.1    Lancaster, D.2    Michel, H.3
  • 74
    • 0034625269 scopus 로고    scopus 로고
    • High performance computational chemistry: An overview of NWChem a distributed parallel application
    • R.A. Kendall, and E. Apra A.T. Wong High performance computational chemistry: an overview of NWChem a distributed parallel application Comput. Phys. Commun. 128 2000 260 283
    • (2000) Comput. Phys. Commun. , vol.128 , pp. 260-283
    • Kendall, R.A.1    Apra, E.2    Wong, A.T.3
  • 75
    • 0036618993 scopus 로고    scopus 로고
    • Setting up and optimization of membrane protein simulations
    • J.D. Faraldo-Gómez, G.R. Smith, and M.S.P. Sansom Setting up and optimization of membrane protein simulations Eur. Biophys. J. 31 2002 217 227
    • (2002) Eur. Biophys. J. , vol.31 , pp. 217-227
    • Faraldo-Gómez, J.D.1    Smith, G.R.2    Sansom, M.S.P.3
  • 76
    • 77957110065 scopus 로고    scopus 로고
    • Potentials of mean force and permeabilities for carbon dioxide, ammonia, and water flux across a Rhesus protein channel and lipid membranes
    • J.S. Hub, and F.K. Winkler B.L. de Groot Potentials of mean force and permeabilities for carbon dioxide, ammonia, and water flux across a Rhesus protein channel and lipid membranes J. Am. Chem. Soc. 132 2010 13251 13263
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 13251-13263
    • Hub, J.S.1    Winkler, F.K.2    De Groot, B.L.3
  • 77
    • 34447515681 scopus 로고    scopus 로고
    • Contribution of the putative inner-pore region to the gating of the transient receptor potential vanilloid subtype 1 channel (TRPV1)
    • DOI 10.1523/JNEUROSCI.1956-07.2007
    • K. Susankova, and R. Ettrich V. Vlachova Contribution of the putative inner-pore region to the gating of the transient receptor potential vanilloid subtype 1 channel (TRPV1) J. Neurosci. 27 2007 7578 7585 (Pubitemid 47066567)
    • (2007) Journal of Neuroscience , vol.27 , Issue.28 , pp. 7578-7585
    • Susankova, K.1    Ettrich, R.2    Vyklicky, L.3    Teisinger, J.4    Vlachova, V.5
  • 80
    • 0029011701 scopus 로고
    • A second generation force field for the simulation of proteins, nucleic acids, and organic molecules
    • W.D. Cornell, and P. Cieplak P.A. Kollman A second generation force field for the simulation of proteins, nucleic acids, and organic molecules J. Am. Chem. Soc. 117 1995 5179 5197
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5179-5197
    • Cornell, W.D.1    Cieplak, P.2    Kollman, P.A.3
  • 81
    • 33748903845 scopus 로고    scopus 로고
    • Recent progress on obtaining theoretical and experimental support for the "E-pathway hypothesis" of coupled transmembrane electron and proton transfer in dihaem-containing quinol:fumarate reductase
    • DOI 10.1016/j.bbabio.2006.05.012, PII S0005272806001277
    • C.R.D. Lancaster, and A.H. Haas M. Mileni Recent progress on obtaining theoretical and experimental support for the "E-pathway hypothesis" of coupled transmembrane electron and proton transfer in dihaem-containing quinol: fumarate reductase Biochim. Biophys. Acta 1757 2006 988 995 (Pubitemid 44427756)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.8 , pp. 988-995
    • Lancaster, C.R.D.1    Haas, A.H.2    Madej, M.G.3    Mileni, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.