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Volumn 1817, Issue 5, 2012, Pages 726-734

Dynamic water networks in cytochrome cbb3 oxidase

Author keywords

cbb3 type cytochrome c oxidase; Continuum electrostatics; Density functional theory (DFT); Molecular dynamics (MD) simulation; Proton channel; Proton pumping

Indexed keywords

CYTOCHROME CBB3 OXIDASE; HEME; OXIDOREDUCTASE; PROTON PUMP; UNCLASSIFIED DRUG; WATER;

EID: 84858717058     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2011.09.010     Document Type: Article
Times cited : (16)

References (86)
  • 1
    • 0017358508 scopus 로고
    • Proton pump coupled to cytochrome c oxidase in mitochondria
    • M.K.F. Wikström Proton pump coupled to cytochrome c oxidase in mitochondria Nature 266 1977 271 273
    • (1977) Nature , vol.266 , pp. 271-273
    • Wikström, M.K.F.1
  • 2
  • 3
    • 78650545848 scopus 로고    scopus 로고
    • Proton-coupled electron transfer in cytochrome oxidase
    • V.R.I. Kaila, M.I. Verkhovsky, and M. Wikström Proton-coupled electron transfer in cytochrome oxidase Chem. Rev. 110 2010 7062 7081
    • (2010) Chem. Rev. , vol.110 , pp. 7062-7081
    • Kaila, V.R.I.1    Verkhovsky, M.I.2    Wikström, M.3
  • 6
    • 0035371783 scopus 로고    scopus 로고
    • A novel scenario for the evolution of haem-copper oxygen reductases
    • M.M. Pereira, M. Santana, and M. Teixeira A novel scenario for the evolution of haem-copper oxygen reductases Biochim. Biophys. Acta 1505 2001 185 208
    • (2001) Biochim. Biophys. Acta , vol.1505 , pp. 185-208
    • Pereira, M.M.1    Santana, M.2    Teixeira, M.3
  • 7
    • 44449146602 scopus 로고    scopus 로고
    • Diversity of the heme-copper superfamily in Archaea: Insights from genomics and structural modeling
    • J. Hemp, and R.B. Gennis Diversity of the heme-copper superfamily in Archaea: insights from genomics and structural modeling Results Probl. Cell Differ. 45 2008 1 31
    • (2008) Results Probl. Cell Differ. , vol.45 , pp. 1-31
    • Hemp, J.1    Gennis, R.B.2
  • 8
    • 0034711407 scopus 로고    scopus 로고
    • Oxygen activation and reduction in respiration: Involvement of redox-active tyrosine 244
    • D.A. Proshlyakov, M.A. Pressier, C. DeMaso, J.F. Leykam, D.L. DeWitt, and G.T. Babcock Oxygen activation and reduction in respiration: involvement of redox-active tyrosine 244 Science 290 2000 1588 1591
    • (2000) Science , vol.290 , pp. 1588-1591
    • Proshlyakov, D.A.1    Pressier, M.A.2    Demaso, C.3    Leykam, J.F.4    Dewitt, D.L.5    Babcock, G.T.6
  • 10
    • 34848850437 scopus 로고    scopus 로고
    • Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases
    • M. Wikström, and M.I. Verkhovsky Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases Biochim. Biophys. Acta 1767 2007 1200 1214
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1200-1214
    • Wikström, M.1    Verkhovsky, M.I.2
  • 11
    • 80051590965 scopus 로고    scopus 로고
    • Redox Bohr effects and the role of heme a in the proton pump of bovine heart cytochrome c oxidase
    • G. Capitanio, P.L. Martino, N. Capitanio, and S. Papa Redox Bohr effects and the role of heme a in the proton pump of bovine heart cytochrome c oxidase Biochim. Biophys. Acta 1807 2011 1287 1294
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 1287-1294
    • Capitanio, G.1    Martino, P.L.2    Capitanio, N.3    Papa, S.4
  • 12
    • 0017883558 scopus 로고
    • Involvement of intramitochondrial protons in redox reactions of cytochrome a
    • V.Y. Artzatbanov, A.A. Konstantinov, and V.P. Skulachev Involvement of intramitochondrial protons in redox reactions of cytochrome a FEBS Lett. 87 1978 180 185
    • (1978) FEBS Lett. , vol.87 , pp. 180-185
    • Artzatbanov, V.Y.1    Konstantinov, A.A.2    Skulachev, V.P.3
  • 13
    • 0033576277 scopus 로고    scopus 로고
    • Cytochrome c oxidase: Catalytic cycle and mechanisms of proton pump - A discussion
    • H. Michel Cytochrome c oxidase: catalytic cycle and mechanisms of proton pump - a discussion Biochemistry 38 1999 15129 15140
    • (1999) Biochemistry , vol.38 , pp. 15129-15140
    • Michel, H.1
  • 16
    • 34548170174 scopus 로고    scopus 로고
    • Energy diagrams and mechanism for proton pumping in cytochrome c oxidase
    • P.E.M. Siegbahn, and M.R.A. Blomberg Energy diagrams and mechanism for proton pumping in cytochrome c oxidase Biochim. Biophys. Acta 1767 2007 1143 1156
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1143-1156
    • Siegbahn, P.E.M.1    Blomberg, M.R.A.2
  • 17
    • 49349116297 scopus 로고    scopus 로고
    • Theoretical and computational analysis of the membrane potential generated by cytochrome c oxidase upon single electron injection into the enzyme
    • R. Sugitani, E.S. Medvedev, and A.A. Stuchebrukhov Theoretical and computational analysis of the membrane potential generated by cytochrome c oxidase upon single electron injection into the enzyme Biochim. Biophys. Acta 1777 2008 1129 1139
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1129-1139
    • Sugitani, R.1    Medvedev, E.S.2    Stuchebrukhov, A.A.3
  • 18
    • 78249242740 scopus 로고    scopus 로고
    • The identity of the transient proton loading site of the proton-pumping mechanism of cytochrome c oxidase
    • V.R.I. Kaila, V. Sharma, and M. Wikström The identity of the transient proton loading site of the proton-pumping mechanism of cytochrome c oxidase Biochim. Biophys. Acta 1807 2011 80 84
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 80-84
    • Kaila, V.R.I.1    Sharma, V.2    Wikström, M.3
  • 19
    • 33746601087 scopus 로고    scopus 로고
    • Design principles of proton-pumping haem-copper oxidases
    • P. Brzezinski, and P. Ädelroth Design principles of proton-pumping haem-copper oxidases Curr. Opin. Struct. Biol. 16 2006 465 472
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 465-472
    • Brzezinski, P.1    Ädelroth, P.2
  • 24
    • 33845989511 scopus 로고    scopus 로고
    • Evolutionary migration of a post-translationally modified active-site residue in the proton-pumping heme-copper oxygen reductases
    • J. Hemp, D.E. Robinson, K.B. Ganesan, T.J. Martinez, N.L. Kelleher, and R.B. Gennis Evolutionary migration of a post-translationally modified active-site residue in the proton-pumping heme-copper oxygen reductases Biochemistry 45 2006 15405 15410
    • (2006) Biochemistry , vol.45 , pp. 15405-15410
    • Hemp, J.1    Robinson, D.E.2    Ganesan, K.B.3    Martinez, T.J.4    Kelleher, N.L.5    Gennis, R.B.6
  • 29
    • 0029792229 scopus 로고    scopus 로고
    • The variation of Km for oxygen of cytochrome oxidase with turnover under de-energized and energized conditions
    • S. Massari, A. Bösel, and J.M. Wrigglesworth The variation of Km for oxygen of cytochrome oxidase with turnover under de-energized and energized conditions Biochem. Soc. Trans. 24 1996 464S
    • (1996) Biochem. Soc. Trans. , vol.24
    • Massari, S.1    Bösel, A.2    Wrigglesworth, J.M.3
  • 36
    • 0030745897 scopus 로고    scopus 로고
    • The roles of two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer
    • A.A. Konstantinov, S. Siletsky, D. Mitchell, A. Kaulen, and R.B. Gennis The roles of two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer Proc. Natl. Acad. Sci. U. S. A. 94 1997 9085 9090
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 9085-9090
    • Konstantinov, A.A.1    Siletsky, S.2    Mitchell, D.3    Kaulen, A.4    Gennis, R.B.5
  • 38
    • 70349493006 scopus 로고    scopus 로고
    • 3 oxygen reductase from Thermus thermophilus uses a single input channel for proton delivery to the active site and for proton pumping
    • 3 oxygen reductase from Thermus thermophilus uses a single input channel for proton delivery to the active site and for proton pumping Proc. Natl. Acad. Sci. U. S. A. 106 2009 16169 16173
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 16169-16173
    • Chang, H.1    Hemp, J.2    Chen, Y.3    Fee, J.A.4    Gennis, R.B.5
  • 39
    • 4243553426 scopus 로고
    • Density-functional exchange-energy approximation with correct asymptotic behaviour
    • A.D. Becke Density-functional exchange-energy approximation with correct asymptotic behaviour Phys. Rev. A 38 1988 3098 3100
    • (1988) Phys. Rev. A , vol.38 , pp. 3098-3100
    • Becke, A.D.1
  • 40
    • 5944261746 scopus 로고
    • Density-functional approximation for the correlation energy of the inhomogeneous electron gas
    • J.P. Perdew Density-functional approximation for the correlation energy of the inhomogeneous electron gas Phys. Rev. B 33 1986 8822 8824
    • (1986) Phys. Rev. B , vol.33 , pp. 8822-8824
    • Perdew, J.P.1
  • 41
    • 0038617492 scopus 로고    scopus 로고
    • Fast evaluation of the coulomb potential for electron densities using multipole accelerated resolution of identity approximation
    • M. Sierka, A. Hogekamp, and R. Ahlrichs Fast evaluation of the coulomb potential for electron densities using multipole accelerated resolution of identity approximation J. Chem. Phys. 118 2003 9136 9148
    • (2003) J. Chem. Phys. , vol.118 , pp. 9136-9148
    • Sierka, M.1    Hogekamp, A.2    Ahlrichs, R.3
  • 42
    • 4243539377 scopus 로고
    • Electronic structure calculations on workstation computers: The program system turbomole
    • R. Ahlrichs, M. Bär, M. Häser, H. Horn, and C. Kölmel Electronic structure calculations on workstation computers: the program system turbomole Chem. Phys. Lett. 162 1989 165 169
    • (1989) Chem. Phys. Lett. , vol.162 , pp. 165-169
    • Ahlrichs, R.1    Bär, M.2    Häser, M.3    Horn, H.4    Kölmel, C.5
  • 43
    • 26344435738 scopus 로고
    • Fully optimized contracted Gaussian basis sets for atoms Li to Kr
    • A. Schäfer, H. Horn, and R. Ahlrichs Fully optimized contracted Gaussian basis sets for atoms Li to Kr J. Chem. Phys. 97 1992 2571 2577
    • (1992) J. Chem. Phys. , vol.97 , pp. 2571-2577
    • Schäfer, A.1    Horn, H.2    Ahlrichs, R.3
  • 44
    • 26244461462 scopus 로고    scopus 로고
    • Balanced basis sets of split valence, triple zeta valence and quadruple zeta valence quality for H to Rn: Design and assessment of accuracy
    • F. Weigend, and R. Ahlrichs Balanced basis sets of split valence, triple zeta valence and quadruple zeta valence quality for H to Rn: design and assessment of accuracy Phys. Chem. Chem. Phys. 7 2005 3297 3305
    • (2005) Phys. Chem. Chem. Phys. , vol.7 , pp. 3297-3305
    • Weigend, F.1    Ahlrichs, R.2
  • 45
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. III. The role of exact exchange
    • A.D. Becke Density-functional thermochemistry. III. The role of exact exchange J. Chem. Phys. 98 1993 5648 5652
    • (1993) J. Chem. Phys. , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 46
    • 0345491105 scopus 로고
    • Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density
    • C. Lee, W. Yang, and R.G. Parr Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density Phys. Rev. B 37 1988 785 789
    • (1988) Phys. Rev. B , vol.37 , pp. 785-789
    • Lee, C.1    Yang, W.2    Parr, R.G.3
  • 47
    • 84986468608 scopus 로고
    • An approach to computing electrostatic charges for molecules
    • U.C. Singh, and P.A. Kollman An approach to computing electrostatic charges for molecules J. Comp. Chem. 5 1984 129 145
    • (1984) J. Comp. Chem. , vol.5 , pp. 129-145
    • Singh, U.C.1    Kollman, P.A.2
  • 48
    • 84961980743 scopus 로고
    • COSMO: A new approach to dielectric screening in solvents with explicit expressions for the screening energy and its gradient
    • A. Klamt, and G. Schüürmann COSMO: a new approach to dielectric screening in solvents with explicit expressions for the screening energy and its gradient J. Chem. Soc. Perkin Trans. 2 1993 799 805
    • (1993) J. Chem. Soc. Perkin Trans. , vol.2 , pp. 799-805
    • Klamt, A.1    Schüürmann, G.2
  • 49
    • 40549119124 scopus 로고    scopus 로고
    • Charge parameterization of the metal centers in cytochrome c oxidase
    • M.P. Johansson, V.R.I. Kaila, and L. Laakkonen Charge parameterization of the metal centers in cytochrome c oxidase J. Comp. Chem. 29 2008 753 767
    • (2008) J. Comp. Chem. , vol.29 , pp. 753-767
    • Johansson, M.P.1    Kaila, V.R.I.2    Laakkonen, L.3
  • 50
    • 13844270250 scopus 로고    scopus 로고
    • The protonation status of compound II in myoglobin, studied by a combination of experimental data and quantum chemical calculations: Quantum refinement
    • K. Nilsson, H.P. Hersleth, T.H. Rod, K.K. Andersson, and U. Ryde The protonation status of compound II in myoglobin, studied by a combination of experimental data and quantum chemical calculations: quantum refinement Biophys. J. 87 2004 3437 3447
    • (2004) Biophys. J. , vol.87 , pp. 3437-3447
    • Nilsson, K.1    Hersleth, H.P.2    Rod, T.H.3    Andersson, K.K.4    Ryde, U.5
  • 52
    • 7444271459 scopus 로고    scopus 로고
    • Ab initio investigation of the atomic charges in the KcsA channel selectivity filter
    • M. Compoint, C. Ramseyer, and P. Huetz Ab initio investigation of the atomic charges in the KcsA channel selectivity filter Chem. Phys. Lett. 397 2004 510 515
    • (2004) Chem. Phys. Lett. , vol.397 , pp. 510-515
    • Compoint, M.1    Ramseyer, C.2    Huetz, P.3
  • 55
  • 57
    • 23244450116 scopus 로고    scopus 로고
    • Water chain formation and possible proton pumping routes in Rhodobacter sphaeroides cytochrome c oxidase: A molecular dynamics comparison of the wild type and R481K mutant
    • S.A. Seibold, D.A. Mills, S. Ferguson-Miller, and R.I. Cukier Water chain formation and possible proton pumping routes in Rhodobacter sphaeroides cytochrome c oxidase: a molecular dynamics comparison of the wild type and R481K mutant Biochemistry 44 2005 10475 10485
    • (2005) Biochemistry , vol.44 , pp. 10475-10485
    • Seibold, S.A.1    Mills, D.A.2    Ferguson-Miller, S.3    Cukier, R.I.4
  • 58
    • 11144304570 scopus 로고    scopus 로고
    • A molecular dynamics study of water chain formation in the proton-conducting K channel of cytochrome c oxidase
    • 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
    • (2005) Biochim. Biophys. Acta , vol.1706 , pp. 134-146
    • Cukier, R.I.1
  • 59
    • 1942423697 scopus 로고    scopus 로고
    • Dynamic water networks in cytochrome C oxidase from Paracoccus denitrificans investigated by molecular dynamics simulations
    • E. Olkhova, M.C. Hutter, M.A. Lill, V. Helms, and H. Michel Dynamic water networks in cytochrome C oxidase from Paracoccus denitrificans investigated by molecular dynamics simulations Biophys. J. 86 2004 1873 1889
    • (2004) Biophys. J. , vol.86 , pp. 1873-1889
    • Olkhova, E.1    Hutter, M.C.2    Lill, M.A.3    Helms, V.4    Michel, H.5
  • 60
    • 43049122273 scopus 로고    scopus 로고
    • Water in nonpolar confinement: From nanotubes to proteins and beyond
    • J.C. Rasaiah, S. Garde, and G. Hummer Water in nonpolar confinement: from nanotubes to proteins and beyond Annu. Rev. Phys. Chem. 59 2008 713 740
    • (2008) Annu. Rev. Phys. Chem. , vol.59 , pp. 713-740
    • Rasaiah, J.C.1    Garde, S.2    Hummer, G.3
  • 62
    • 4444240014 scopus 로고    scopus 로고
    • Classical force field parameters for the heme prosthetic group of cytochrome c
    • F. Autenrieth, E. Tajkhorshid, J. Baudry, and Z. Luthey-Schulten Classical force field parameters for the heme prosthetic group of cytochrome c J. Comp. Chem. 25 2004 1613 1622
    • (2004) J. Comp. Chem. , vol.25 , pp. 1613-1622
    • Autenrieth, F.1    Tajkhorshid, E.2    Baudry, J.3    Luthey-Schulten, Z.4
  • 65
    • 0026612756 scopus 로고
    • a values of ionizable groups in bacteriorhodopsin
    • a values of ionizable groups in bacteriorhodopsin J. Mol. Biol. 224 1992 473 486
    • (1992) J. Mol. Biol. , vol.224 , pp. 473-486
    • Bashford, D.1    Gerwert, K.2
  • 66
    • 84957665033 scopus 로고    scopus 로고
    • An object-oriented programming suite for electrostatic effects in biological molecules
    • Y. Ishikawa, R.R. Oldehoeft, J.V.W. Reynders, M. Tholburn, Springer Berlin/Heidelberg
    • D. Bashford An object-oriented programming suite for electrostatic effects in biological molecules Y. Ishikawa, R.R. Oldehoeft, J.V.W. Reynders, M. Tholburn, Scientific Computing in Object-oriented Parallel Environments 1997 Springer Berlin/Heidelberg 233 240
    • (1997) Scientific Computing in Object-oriented Parallel Environments , pp. 233-240
    • Bashford, D.1
  • 67
    • 33745605230 scopus 로고    scopus 로고
    • Calculated proton uptake on anaerobic reduction of cytochrome c oxidase: Is the reaction electroneutral?
    • Y. Song, E. Michonova-Alexova, and M.R. Gunner Calculated proton uptake on anaerobic reduction of cytochrome c oxidase: is the reaction electroneutral? Biochemistry 45 2006 7959 7975
    • (2006) Biochemistry , vol.45 , pp. 7959-7975
    • Song, Y.1    Michonova-Alexova, E.2    Gunner, M.R.3
  • 69
    • 0035112206 scopus 로고    scopus 로고
    • Calculated pH-dependent population and protonation of carbon-monoxy-myoglobin conformers
    • B. Rabenstein, and E.W. Knapp Calculated pH-dependent population and protonation of carbon-monoxy-myoglobin conformers Biophys. J. 80 2001 1141 1150
    • (2001) Biophys. J. , vol.80 , pp. 1141-1150
    • Rabenstein, B.1    Knapp, E.W.2
  • 70
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
    • P.J. Goodford A computational procedure for determining energetically favorable binding sites on biologically important macromolecules J. Med. Chem. 28 1985 849 857
    • (1985) J. Med. Chem. , vol.28 , pp. 849-857
    • Goodford, P.J.1
  • 72
    • 79960352688 scopus 로고    scopus 로고
    • Energetics and dynamics of proton transfer reactions along short water wires
    • V.R.I. Kaila, and G. Hummer Energetics and dynamics of proton transfer reactions along short water wires Phys. Chem. Chem. Phys. 13 2011 13207 13215
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 13207-13215
    • Kaila, V.R.I.1    Hummer, G.2
  • 73
    • 0035829539 scopus 로고    scopus 로고
    • Water conduction through the hydrophobic channel of a carbon nanotube
    • G. Hummer, J.C. Rasaiah, and J.P. Noworyta Water conduction through the hydrophobic channel of a carbon nanotube Nature 414 2001 188 190
    • (2001) Nature , vol.414 , pp. 188-190
    • Hummer, G.1    Rasaiah, J.C.2    Noworyta, J.P.3
  • 74
    • 0037726809 scopus 로고    scopus 로고
    • Water-gated mechanism of proton translocation by cytochrome c oxidase
    • M. Wikström, M.I. Verkhovsky, and G. Hummer Water-gated mechanism of proton translocation by cytochrome c oxidase Biochim. Biophys. Acta 1604 2003 61 65
    • (2003) Biochim. Biophys. Acta , vol.1604 , pp. 61-65
    • Wikström, M.1    Verkhovsky, M.I.2    Hummer, G.3
  • 75
    • 0027231963 scopus 로고
    • The Asp-His-iron triad of cytochrome c peroxidase controls the reduction potential electronic structure, and coupling of the tryptophan free radical to the heme
    • D.B. Goodin, and D.E. McRee The Asp-His-iron triad of cytochrome c peroxidase controls the reduction potential electronic structure, and coupling of the tryptophan free radical to the heme Biochemistry 32 1993 3313 3324
    • (1993) Biochemistry , vol.32 , pp. 3313-3324
    • Goodin, D.B.1    McRee, D.E.2
  • 77
    • 79953290363 scopus 로고    scopus 로고
    • Regulation of electron and proton transfer by the protein matrix of cytochrome c oxidase
    • V. Daskalakis, S.C. Farantos, V. Guallar, and C. Varotsis Regulation of electron and proton transfer by the protein matrix of cytochrome c oxidase J. Phys. Chem. B. 115 2011 3648 3655
    • (2011) J. Phys. Chem. B. , vol.115 , pp. 3648-3655
    • Daskalakis, V.1    Farantos, S.C.2    Guallar, V.3    Varotsis, C.4
  • 78
    • 0031880698 scopus 로고    scopus 로고
    • The coupling of electron transfer and proton translocation: Electrostatic calculations on Paracoccus denitrificans cytochrome c oxidase
    • A. Kannt, C.R.D. Lancaster, and H. Michel The coupling of electron transfer and proton translocation: electrostatic calculations on Paracoccus denitrificans cytochrome c oxidase Biophys. J. 74 1998 708 721
    • (1998) Biophys. J. , vol.74 , pp. 708-721
    • Kannt, A.1    Lancaster, C.R.D.2    Michel, H.3
  • 80
    • 33747848994 scopus 로고    scopus 로고
    • 3 cytochrome c oxidase on its function
    • 3 cytochrome c oxidase on its function J. Microbiol. 44 2006 284 292
    • (2006) J. Microbiol. , vol.44 , pp. 284-292
    • Oh, J.I.1
  • 81
    • 63449091255 scopus 로고    scopus 로고
    • Functional hydration and conformational gating of proton uptake in cytochrome c oxidase
    • R.M. Henry, C.H. Yu, T. Rodinger, and R. Pomès Functional hydration and conformational gating of proton uptake in cytochrome c oxidase J. Mol. Biol. 387 2009 1165 1185
    • (2009) J. Mol. Biol. , vol.387 , pp. 1165-1185
    • Henry, R.M.1    Yu, C.H.2    Rodinger, T.3    Pomès, R.4
  • 83
    • 67649986251 scopus 로고    scopus 로고
    • Mechanism and energetics by which glutamic acid 242 prevents leaks in cytochrome c oxidase
    • V.R.I. Kaila, M.I. Verkhovsky, G. Hummer, and M. Wikström Mechanism and energetics by which glutamic acid 242 prevents leaks in cytochrome c oxidase Biochim. Biophys. Acta 1787 2009 1205 1214
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1205-1214
    • Kaila, V.R.I.1    Verkhovsky, M.I.2    Hummer, G.3    Wikström, M.4


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