메뉴 건너뛰기




Volumn 1817, Issue 4, 2012, Pages 506-517

Coupled electron and proton transfer reactions during the O → e transition in bovine cytochrome c oxidase

Author keywords

Cytochrome c oxidase; Donor acceptor system; Gating mechanism; pK a and E m calculation; Proton pumping; Proton loading site

Indexed keywords

CYTOCHROME C OXIDASE; HEME; HISTIDINE; PROTON PUMP;

EID: 84857916864     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2011.10.013     Document Type: Review
Times cited : (27)

References (110)
  • 1
    • 0017358508 scopus 로고
    • Proton pump coupled to cytochrome c oxidase in mitochondria
    • M. Wikström Proton pump coupled to cytochrome c oxidase in mitochondria Nature 266 1977 271 273
    • (1977) Nature , vol.266 , pp. 271-273
    • Wikström, M.1
  • 2
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energy in cell respiration
    • G.T. Babcock, and M. Wikström Oxygen activation and the conservation of energy in cell respiration Nature 356 1992 301 309
    • (1992) Nature , vol.356 , pp. 301-309
    • Babcock, G.T.1    Wikström, M.2
  • 5
    • 0034640504 scopus 로고    scopus 로고
    • Proton pumping by cytochrome oxidase: Progress, problems and postulates
    • D. Zaslavsky, and R.B. Gennis Proton pumping by cytochrome oxidase: progress, problems and postulates Biochim. Biophys. Acta 1458 2000 164 179
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 164-179
    • Zaslavsky, D.1    Gennis, R.B.2
  • 6
    • 0030886203 scopus 로고    scopus 로고
    • Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody Fv fragment
    • C. Ostermeier, A. Harrenga, U. Ermler, and H. Michel Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody Fv fragment Proc. Natl. Acad. Sci. U. S. A. 94 1997 10547 10553
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 10547-10553
    • Ostermeier, C.1    Harrenga, A.2    Ermler, U.3    Michel, H.4
  • 8
    • 0036382724 scopus 로고    scopus 로고
    • The x-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter Sphaeroides
    • M. Svensson-Ek, J. Abramson, G. Larsson, S. Tornroth, P. Brzezinski, and S. Iwata The x-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter Sphaeroides J. Mol. Biol. 321 2002 329 335
    • (2002) J. Mol. Biol. , vol.321 , pp. 329-335
    • Svensson-Ek, M.1    Abramson, J.2    Larsson, G.3    Tornroth, S.4    Brzezinski, P.5    Iwata, S.6
  • 10
    • 56249146306 scopus 로고    scopus 로고
    • A D-pathway mutation decouples the Paracoccus denitrificans cytochrome c oxidase by altering the side-chain orientation of a distant conserved glutamate
    • K.L. Dürr, J. Koepke, P. Hellwig, H. Müller, H. Angerer, G. Peng, E. Olkhova, O.-M.H. Richter, B. Ludwig, and H. Michel A D-pathway mutation decouples the Paracoccus denitrificans cytochrome c oxidase by altering the side-chain orientation of a distant conserved glutamate J. Mol. Biol. 384 2008 865 877
    • (2008) J. Mol. Biol. , vol.384 , pp. 865-877
    • Dürr, K.L.1    Koepke, J.2    Hellwig, P.3    Müller, H.4    Angerer, H.5    Peng, G.6    Olkhova, E.7    Richter, O.-M.H.8    Ludwig, B.9    Michel, H.10
  • 11
    • 67049086176 scopus 로고    scopus 로고
    • Redox-dependent conformational changes in cytochrome c oxidase suggest a gating mechanism for proton uptake
    • L. Qin, J. Liu, D.A. Mills, D.A. Proshlyakov, C. Hiser, and S. Ferguson-Miller Redox-dependent conformational changes in cytochrome c oxidase suggest a gating mechanism for proton uptake Biochemistry 48 2009 5121 5130
    • (2009) Biochemistry , vol.48 , pp. 5121-5130
    • Qin, L.1    Liu, J.2    Mills, D.A.3    Proshlyakov, D.A.4    Hiser, C.5    Ferguson-Miller, S.6
  • 12
    • 0030745897 scopus 로고    scopus 로고
    • The role of the 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 role of the 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
  • 13
    • 0034663494 scopus 로고    scopus 로고
    • The role of the D- and K-pathways of proton transfer in the function of the heam-copper oxidases
    • M. Wikström, A. Jasaitis, C. Backgren, A. Puustinen, and M.I. Verkhovsky The role of the D- and K-pathways of proton transfer in the function of the heam-copper oxidases Biochim. Biophys. Acta 1459 2000 514 520
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 514-520
    • Wikström, M.1    Jasaitis, A.2    Backgren, C.3    Puustinen, A.4    Verkhovsky, M.I.5
  • 16
    • 0034695481 scopus 로고    scopus 로고
    • Time dependence of the catalytic intermediates in cytochrome c oxidase
    • S. Han, S. Takahashi, and D.L. Rousseau Time dependence of the catalytic intermediates in cytochrome c oxidase J. Biol. Chem. 275 2000 1910 1919
    • (2000) J. Biol. Chem. , vol.275 , pp. 1910-1919
    • Han, S.1    Takahashi, S.2    Rousseau, D.L.3
  • 17
    • 1942472486 scopus 로고    scopus 로고
    • Cytochrome c oxidase: 25 years of the elusive proton pump
    • M. Wikström Cytochrome c oxidase: 25 years of the elusive proton pump Biochim. Biophys. Acta 1655 2004 241 247
    • (2004) Biochim. Biophys. Acta , vol.1655 , pp. 241-247
    • Wikström, M.1
  • 18
    • 2542464946 scopus 로고    scopus 로고
    • Coupled proton and electron transfer reactions in cytochrome oxidase
    • R.B. Gennis Coupled proton and electron transfer reactions in cytochrome oxidase Front. Biosci. 9 2004 581 591
    • (2004) Front. Biosci. , vol.9 , pp. 581-591
    • Gennis, R.B.1
  • 19
    • 3242763877 scopus 로고    scopus 로고
    • Redox-driven membrane-bound proton pumps
    • P. Brzezinski Redox-driven membrane-bound proton pumps Trends Biochem. Sci. 29 2004 380 387
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 380-387
    • Brzezinski, P.1
  • 20
    • 33645732495 scopus 로고    scopus 로고
    • Proton-coupled electron transfer drives the proton pump of cytochrome c oxidase
    • I. Belevich, M.I. Verkhovsky, and M. Wikström Proton-coupled electron transfer drives the proton pump of cytochrome c oxidase Nature 440 2006 829 832
    • (2006) Nature , vol.440 , pp. 829-832
    • Belevich, I.1    Verkhovsky, M.I.2    Wikström, M.3
  • 21
    • 33746349218 scopus 로고    scopus 로고
    • Energy transduction: Proton transfer through the respiratory complexes
    • J.P. Hosler, S. Ferguson-Miller, and D.A. Mills Energy transduction: proton transfer through the respiratory complexes Annu. Rev. Biochem. 75 2006 165 187
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 165-187
    • Hosler, J.P.1    Ferguson-Miller, S.2    Mills, D.A.3
  • 22
    • 57049180108 scopus 로고    scopus 로고
    • Cytochrome c oxidase: Exciting progress and remaining mysteries
    • P. Brzezinski, and R.B. Gennis Cytochrome c oxidase: exciting progress and remaining mysteries J. Bioenerg. Biomembr. 40 2008 521 531
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 521-531
    • Brzezinski, P.1    Gennis, R.B.2
  • 23
    • 57049130390 scopus 로고    scopus 로고
    • A chemically explicit model for the mechanism of proton pumping in heme-copper oxidases
    • M.A. Sharpe, and S. Ferguson-Miller A chemically explicit model for the mechanism of proton pumping in heme-copper oxidases J. Bioenerg. Biomembr. 40 2008 541 549
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 541-549
    • Sharpe, M.A.1    Ferguson-Miller, S.2
  • 24
    • 1242314254 scopus 로고    scopus 로고
    • Electrostatic study of proton pumping mechanism of bovine heart cytochrome c oxidase
    • D.M. Popovic, and A.A. Stuchebrukhov Electrostatic study of proton pumping mechanism of bovine heart cytochrome c oxidase J. Am. Chem. Soc. 126 2004 1858 1871
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 1858-1871
    • Popovic, D.M.1    Stuchebrukhov, A.A.2
  • 25
    • 2442616154 scopus 로고    scopus 로고
    • Proton pumping mechanism and catalytic cycle of cytochrome c oxidase: Coulomb pump model with kinetic gating
    • D.M. Popovic, and A.A. Stuchebrukhov Proton pumping mechanism and catalytic cycle of cytochrome c oxidase: Coulomb pump model with kinetic gating FEBS Lett. 566 2004 126 130
    • (2004) FEBS Lett. , vol.566 , pp. 126-130
    • Popovic, D.M.1    Stuchebrukhov, A.A.2
  • 26
    • 14844358231 scopus 로고    scopus 로고
    • DFT/electrostatic calculations of pKa values in cytochrome c oxidase
    • D.M. Popovic, J. Quenneville, and A.A. Stuchebrukhov DFT/electrostatic calculations of pKa values in cytochrome c oxidase J. Phys. Chem. B 109 2005 3616 3626
    • (2005) J. Phys. Chem. B , vol.109 , pp. 3616-3626
    • Popovic, D.M.1    Quenneville, J.2    Stuchebrukhov, A.A.3
  • 27
    • 33748895869 scopus 로고    scopus 로고
    • Combined DFT and electrostatics study of the proton pumping mechanism in cytochrome c oxidase
    • J. Quenneville, D.M. Popovic, and A.A. Stuchebrukhov Combined DFT and electrostatics study of the proton pumping mechanism in cytochrome c oxidase Biochim. Biophys. Acta 1757 2006 1035 1046
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1035-1046
    • Quenneville, J.1    Popovic, D.M.2    Stuchebrukhov, A.A.3
  • 29
    • 68049115408 scopus 로고    scopus 로고
    • Properties of Arg481 mutants of the aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides suggest that neither R481 nor the Nearby D-propionate of heme a(3) is likely to be the proton loading site of the proton pump
    • H.J. Lee, L. Ojemyr, A. Vakkasoglu, P. Brzezinski, and R.B. Gennis Properties of Arg481 mutants of the aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides suggest that neither R481 nor the Nearby D-propionate of heme a(3) is likely to be the proton loading site of the proton pump Biochemistry 48 2009 7123 7131
    • (2009) Biochemistry , vol.48 , pp. 7123-7131
    • Lee, H.J.1    Ojemyr, L.2    Vakkasoglu, A.3    Brzezinski, P.4    Gennis, R.B.5
  • 31
    • 0032546595 scopus 로고    scopus 로고
    • Involvement of glutamic acid 278 in the redox reaction of the cytochrome c oxidase from Paracoccus denitrificans investigated by FT-IR spectroscopy
    • P. Hellwig, J. Behr, C. Ostermeier, O.-M.H. Richter, U. Pfitzner, A. Odenwald, B. Ludwig, H. Michel, and W. Mantele Involvement of glutamic acid 278 in the redox reaction of the cytochrome c oxidase from Paracoccus denitrificans investigated by FT-IR spectroscopy Biochemistry 37 1998 7390 7399
    • (1998) Biochemistry , vol.37 , pp. 7390-7399
    • Hellwig, P.1    Behr, J.2    Ostermeier, C.3    Richter, O.-M.H.4    Pfitzner, U.5    Odenwald, A.6    Ludwig, B.7    Michel, H.8    Mantele, W.9
  • 32
    • 0037069405 scopus 로고    scopus 로고
    • A mutation in subunit i of cytochrome oxidase from Rhodobacter sphaeroides results in an increase in steady-state activity but completely eliminates proton pumping
    • A.S. Pawate, J. Morgan, A. Namslauer, D. Mills, P. Brzezinski, S. Ferguson-Miller, and R.B. Gennis A mutation in subunit I of cytochrome oxidase from Rhodobacter sphaeroides results in an increase in steady-state activity but completely eliminates proton pumping Biochemistry 41 2002 13417 13423
    • (2002) Biochemistry , vol.41 , pp. 13417-13423
    • Pawate, A.S.1    Morgan, J.2    Namslauer, A.3    Mills, D.4    Brzezinski, P.5    Ferguson-Miller, S.6    Gennis, R.B.7
  • 33
    • 0037790647 scopus 로고    scopus 로고
    • A role for subunit III in proton uptake into the D pathway and a possible proton exit pathway in Rhodobacter sphaeroides cytochrome c oxidase
    • D.A. Mills, Z. Tan, S. Ferguson-Miller, and J. Hosler A role for subunit III in proton uptake into the D pathway and a possible proton exit pathway in Rhodobacter sphaeroides cytochrome c oxidase Biochemistry 42 2003 7410 7417
    • (2003) Biochemistry , vol.42 , pp. 7410-7417
    • Mills, D.A.1    Tan, Z.2    Ferguson-Miller, S.3    Hosler, J.4
  • 34
    • 33745097480 scopus 로고    scopus 로고
    • Two conformational states of Glu242 and pKas in bovine cytochrome c oxidase
    • D.M. Popovic, and A.A. Stuchebrukhov Two conformational states of Glu242 and pKas in bovine cytochrome c oxidase Photochem. Photobiol. Sci. 5 2006 611 620
    • (2006) Photochem. Photobiol. Sci. , vol.5 , pp. 611-620
    • Popovic, D.M.1    Stuchebrukhov, A.A.2
  • 36
    • 34548170174 scopus 로고    scopus 로고
    • Energy diagrams and mechanism for proton pumping in cytochrome c oxidase
    • P.E.M. Siegbahn, and M.R. 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.2
  • 37
    • 64849103999 scopus 로고    scopus 로고
    • Microscopic pK(a) analysis of Glu286 in cytochrome c oxidase (Rhodobacter sphaeroides): Toward a calibrated molecular model
    • N. Ghosh, X. Prat-Resina, M.R. Gunner, and Q. Cui Microscopic pK(a) analysis of Glu286 in cytochrome c oxidase (Rhodobacter sphaeroides): toward a calibrated molecular model Biochemistry 48 2009 2468 2485
    • (2009) Biochemistry , vol.48 , pp. 2468-2485
    • Ghosh, N.1    Prat-Resina, X.2    Gunner, M.R.3    Cui, Q.4
  • 38
    • 38749152834 scopus 로고    scopus 로고
    • Redox-coupled proton pumping in cytochrome c oxidase: Further insights from computer simulation
    • J. Xu, and G. Voth Redox-coupled proton pumping in cytochrome c oxidase: further insights from computer simulation Biochim. Biophys. Acta 1777 2008 196 201
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 196-201
    • Xu, J.1    Voth, G.2
  • 39
    • 33646268674 scopus 로고    scopus 로고
    • Monte Carlo simulations of proton pumps: On the working principles of the biological valve that controls proton pumping in cytochrome c oxidase
    • M.H.M. Olsson, and A. Warshel Monte Carlo simulations of proton pumps: on the working principles of the biological valve that controls proton pumping in cytochrome c oxidase Proc. Natl. Acad. Sci. U. S. A. 103 2006 6500 6505
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 6500-6505
    • Olsson, M.H.M.1    Warshel, A.2
  • 40
    • 0038101048 scopus 로고    scopus 로고
    • Ab initio study of coupled electron transfer/proton transfer in cytochrome c oxidase
    • D.B. Moore, and T.J. Martinez Ab initio study of coupled electron transfer/proton transfer in cytochrome c oxidase J. Phys. Chem. A 104 2000 2367 2374
    • (2000) J. Phys. Chem. A , vol.104 , pp. 2367-2374
    • Moore, D.B.1    Martinez, T.J.2
  • 41
    • 1542298196 scopus 로고    scopus 로고
    • Investigation of protonatable residues in Rhodothermus marinus caa3 haem-copper oxygen reductase: Comparison with Paracoccus denitrificans aa3 haem-copper oxygen reductase
    • C.M. Soares, A.M. Baptista, M.M. Pereira, and M. Teixeira Investigation of protonatable residues in Rhodothermus marinus caa3 haem-copper oxygen reductase: Comparison with Paracoccus denitrificans aa3 haem-copper oxygen reductase J. Biol. Inorg. Chem. 9 2004 124 134
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 124-134
    • Soares, C.M.1    Baptista, A.M.2    Pereira, M.M.3    Teixeira, M.4
  • 42
    • 0142091718 scopus 로고    scopus 로고
    • Theoretical study of the energetics of proton pumping and oxygen reduction in cytochrome oxidase
    • P.E.M. Siegbahn, M.R.A. Blomberg, and M.L. Blomberg Theoretical study of the energetics of proton pumping and oxygen reduction in cytochrome oxidase J. Phys. Chem. B 107 2003 10946 10955
    • (2003) J. Phys. Chem. B , vol.107 , pp. 10946-10955
    • Siegbahn, P.E.M.1    Blomberg, M.R.A.2    Blomberg, M.L.3
  • 43
    • 33745774349 scopus 로고    scopus 로고
    • Improved density functional theory/electrostatic calculation of the His291 protonation state in cytochrome c oxidase: Self-consistent charges for solvation energy calculation
    • D.V. Makhov, D.M. Popovic, and A.A. Stuchebrukhov Improved density functional theory/electrostatic calculation of the His291 protonation state in cytochrome c oxidase: self-consistent charges for solvation energy calculation J. Phys. Chem. B 110 2006 12162 12166
    • (2006) J. Phys. Chem. B , vol.110 , pp. 12162-12166
    • Makhov, D.V.1    Popovic, D.M.2    Stuchebrukhov, A.A.3
  • 44
    • 57349108758 scopus 로고    scopus 로고
    • Toward a chemical mechanism of proton pumping by the B-type cytochrome c oxidases: Application of density functional theory to cytochrome ba(3) of Thermus thermophilus
    • J.A. Fee, D.A. Case, and L. Noodleman Toward a chemical mechanism of proton pumping by the B-type cytochrome c oxidases: application of density functional theory to cytochrome ba(3) of Thermus thermophilus J. Am. Chem. Soc. 130 2008 15002 15021
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 15002-15021
    • Fee, J.A.1    Case, D.A.2    Noodleman, L.3
  • 45
    • 78449267413 scopus 로고    scopus 로고
    • A quantum chemical study of the mechanism for proton-coupled electron transfer leading to proton pumping in cytochrome c oxidase
    • M.R. Blomberg, and P.E.M. Siegbahn A quantum chemical study of the mechanism for proton-coupled electron transfer leading to proton pumping in cytochrome c oxidase Mol. Phys. 108 2010 2733 2743
    • (2010) Mol. Phys. , vol.108 , pp. 2733-2743
    • Blomberg, M.R.1    Siegbahn, P.E.M.2
  • 46
    • 79956042304 scopus 로고    scopus 로고
    • Computational calculations of pKa values of imidazole in Cu(II) complexes of biological relevance
    • J. Ali-Torres, L. Rodriguez-Santiago, and M. Sodupe Computational calculations of pKa values of imidazole in Cu(II) complexes of biological relevance Phys. Chem. Chem. Phys. 13 2011 7852 7861
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 7852-7861
    • Ali-Torres, J.1    Rodriguez-Santiago, L.2    Sodupe, M.3
  • 47
    • 0031880698 scopus 로고    scopus 로고
    • The coupling of electron transfer and proton translocation: Electrostatic calculations on Parracocus denitrificants cytochrome c oxidase
    • A. Kannt, R.D. Lancaster, and H. Michel The coupling of electron transfer and proton translocation: electrostatic calculations on Parracocus denitrificants cytochrome c oxidase Biophys. J. 74 1998 708 721
    • (1998) Biophys. J. , vol.74 , pp. 708-721
    • Kannt, A.1    Lancaster, R.D.2    Michel, H.3
  • 48
    • 13444305368 scopus 로고    scopus 로고
    • Proton exit channels in bovine cytochrome c oxidase
    • D.M. Popovic, and A.A. Stuchebrukhov Proton exit channels in bovine cytochrome c oxidase J. Phys. Chem. B 109 2005 1999 2006
    • (2005) J. Phys. Chem. B , vol.109 , pp. 1999-2006
    • Popovic, D.M.1    Stuchebrukhov, A.A.2
  • 49
    • 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
  • 51
    • 45549107077 scopus 로고    scopus 로고
    • Electrostatic basis for the unidirectionality of the primary proton transfer in cytochrome c oxidase
    • A.V. Pisliakov, P.K. Sharma, Z.T. Chu, M. Haranczyk, and A. Warshel Electrostatic basis for the unidirectionality of the primary proton transfer in cytochrome c oxidase Proc. Natl. Acad. Sci. U. S. A. 105 2008 7726 7731
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 7726-7731
    • Pisliakov, A.V.1    Sharma, P.K.2    Chu, Z.T.3    Haranczyk, M.4    Warshel, A.5
  • 52
    • 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
  • 55
    • 0033514982 scopus 로고    scopus 로고
    • Assignment and charge translocation stoichiometries of the electrogenic phases in the reaction of cytochrome c with dioxygen
    • A. Jasaitis, M.I. Verkhovsky, J.E. Morgan, M.L. Verkhovskaya, and M. Wikström Assignment and charge translocation stoichiometries of the electrogenic phases in the reaction of cytochrome c with dioxygen Biochemistry 38 1999 2697 2706
    • (1999) Biochemistry , vol.38 , pp. 2697-2706
    • Jasaitis, A.1    Verkhovsky, M.I.2    Morgan, J.E.3    Verkhovskaya, M.L.4    Wikström, M.5
  • 56
    • 0034712938 scopus 로고    scopus 로고
    • Single-electron reduction of the oxidized state is coupled to proton uptake via the K-pathway in Paracoccus denitrificans cytochrome c oxidase
    • M. Ruitenberg, A. Kannt, E. Bamberg, B. Ludwig, H. Michel, and K. Fendler Single-electron reduction of the oxidized state is coupled to proton uptake via the K-pathway in Paracoccus denitrificans cytochrome c oxidase Proc. Natl. Acad. Sci. U. S. A. 97 2000 4632 4636
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 4632-4636
    • Ruitenberg, M.1    Kannt, A.2    Bamberg, E.3    Ludwig, B.4    Michel, H.5    Fendler, K.6
  • 57
    • 0037007627 scopus 로고    scopus 로고
    • Reduction of cytochrome c oxidase by a second electron leads to proton translocation
    • M. Ruitenberg, A. Kannt, E. Bamberg, K. Fendler, and H. Michel Reduction of cytochrome c oxidase by a second electron leads to proton translocation Nature 417 2002 99 102
    • (2002) Nature , vol.417 , pp. 99-102
    • Ruitenberg, M.1    Kannt, A.2    Bamberg, E.3    Fendler, K.4    Michel, H.5
  • 58
    • 10644252589 scopus 로고    scopus 로고
    • Transmembrane charge separation during the ferryl-oxo → oxidized transition in a nonpumping mutant of cytochrome c oxidase
    • S.A. Siletsky, A.S. Pawate, K. Weiss, R.B. Gennis, and A.A. Konstantinov Transmembrane charge separation during the ferryl-oxo → oxidized transition in a nonpumping mutant of cytochrome c oxidase J. Biol. Chem. 279 2004 52558 52565
    • (2004) J. Biol. Chem. , vol.279 , pp. 52558-52565
    • Siletsky, S.A.1    Pawate, A.S.2    Weiss, K.3    Gennis, R.B.4    Konstantinov, A.A.5
  • 60
    • 0028813330 scopus 로고
    • Towards an understanding of the chemistry of oxygen reduction and proton translocation in the iron-copper respiratory oxidases
    • P.R. Rich Towards an understanding of the chemistry of oxygen reduction and proton translocation in the iron-copper respiratory oxidases Aust. J. Plant Physiol. 22 1995 479 486
    • (1995) Aust. J. Plant Physiol. , vol.22 , pp. 479-486
    • Rich, P.R.1
  • 62
    • 84857913011 scopus 로고    scopus 로고
    • Jaguar 5.5, Schrödinger, L. L. C., Portland, OR, 1991-2003
    • Jaguar 5.5, Schrödinger, L. L. C., Portland, OR, 1991-2003.
  • 63
    • 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
    • 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 vol. 1343 1997 Springer Berlin 233 240
    • (1997) Scientific Computing in Object-Oriented Parallel Environments , vol.1343 , pp. 233-240
    • Bashford, D.1
  • 64
    • 0035112206 scopus 로고    scopus 로고
    • Calculated pH-dependent population of CO-myoglobin coformers
    • B. Rabenstein, and E.W. Knapp Calculated pH-dependent population of CO-myoglobin coformers Biophys. J. 80 2001 1141 1150
    • (2001) Biophys. J. , vol.80 , pp. 1141-1150
    • Rabenstein, B.1    Knapp, E.W.2
  • 65
    • 0042113153 scopus 로고
    • Self-consistent equations including exchange and correlation effects
    • K. Kohn, and L.J. Sham Self-consistent equations including exchange and correlation effects Phys. Rev. 140 1965 A1133 A1136
    • (1965) Phys. Rev. , vol.140
    • Kohn, K.1    Sham, L.J.2
  • 66
    • 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
  • 67
    • 27344448074 scopus 로고
    • Ab initio effective core potentials for molecular calculations. Potentials for K to Au including the outermost core orbitals
    • P.J. Hay, and W.R. Wadt Ab initio effective core potentials for molecular calculations. Potentials for K to Au including the outermost core orbitals J. Chem. Phys. 82 1985 299 310
    • (1985) J. Chem. Phys. , vol.82 , pp. 299-310
    • Hay, P.J.1    Wadt, W.R.2
  • 68
    • 0000304948 scopus 로고
    • Accurate first principles calculation of molecular charge distributions and solvation energies from ab initio quantum mechanics and continuum dielectric theory
    • D.J. Tannor, B. Marten, R. Marphy, R.A. Friesner, D. Sitkoff, A. Nicholls, M. Ringnalda, W.A. Goddard, and B. Honig Accurate first principles calculation of molecular charge distributions and solvation energies from ab initio quantum mechanics and continuum dielectric theory J. Am. Chem. Soc. 116 1994 11875 11880
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 11875-11880
    • Tannor, D.J.1    Marten, B.2    Marphy, R.3    Friesner, R.A.4    Sitkoff, D.5    Nicholls, A.6    Ringnalda, M.7    Goddard, W.A.8    Honig, B.9
  • 69
    • 10044290841 scopus 로고    scopus 로고
    • Redox-dependent pKa of CuB histidine ligand in cytochrome c oxidase
    • J. Quenneville, D.M. Popovic, and A.A. Stuchebrukhov Redox-dependent pKa of CuB histidine ligand in cytochrome c oxidase J. Phys. Chem. B 108 2004 18383 18389
    • (2004) J. Phys. Chem. B , vol.108 , pp. 18383-18389
    • Quenneville, J.1    Popovic, D.M.2    Stuchebrukhov, A.A.3
  • 70
    • 33751159055 scopus 로고
    • Incorporating solvation effects into density functional electronic structure calculations
    • J.L. Chen, L. Noodleman, D.A. Case, and D. Bashford Incorporating solvation effects into density functional electronic structure calculations J. Phys. Chem. 98 1994 11059 11068
    • (1994) J. Phys. Chem. , vol.98 , pp. 11059-11068
    • Chen, J.L.1    Noodleman, L.2    Case, D.A.3    Bashford, D.4
  • 71
    • 0000318315 scopus 로고
    • Density functional/Poisson-Boltzmann calculations of redox potentials for iron-sulfur clusters
    • J.M. Mouesca, J.L. Chen, L. Noodleman, D. Bashford, and D.A. Case Density functional/Poisson-Boltzmann calculations of redox potentials for iron-sulfur clusters J. Am. Chem. Soc. 116 1994 11898 11914
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 11898-11914
    • Mouesca, J.M.1    Chen, J.L.2    Noodleman, L.3    Bashford, D.4    Case, D.A.5
  • 72
    • 84962367570 scopus 로고    scopus 로고
    • Incorporating protein environments in density functional theory: A self-consistent reaction field calculation of redox potentials of [2Fe2S] clusters in ferredoxin and phthalate dioxygenase reductase
    • J. Li, M.R. Nelson, C.Y. Peng, D. Bashford, and L. Noodleman Incorporating protein environments in density functional theory: a self-consistent reaction field calculation of redox potentials of [2Fe2S] clusters in ferredoxin and phthalate dioxygenase reductase J. Phys. Chem. A 102 1998 6311 6324
    • (1998) J. Phys. Chem. A , vol.102 , pp. 6311-6324
    • Li, J.1    Nelson, M.R.2    Peng, C.Y.3    Bashford, D.4    Noodleman, L.5
  • 73
    • 0000192330 scopus 로고    scopus 로고
    • Density functional and electrostatic calculations of manganese superoxide dismutase active site complexes in protein environments
    • J. Li, C.L. Fisher, R. Konecny, D. Bashford, and L. Noodleman Density functional and electrostatic calculations of manganese superoxide dismutase active site complexes in protein environments Inorg. Chem. 38 1999 929 939
    • (1999) Inorg. Chem. , vol.38 , pp. 929-939
    • Li, J.1    Fisher, C.L.2    Konecny, R.3    Bashford, D.4    Noodleman, L.5
  • 74
    • 0026612756 scopus 로고
    • Electrostatic calculations of the pKa values of ionizable groups in bacteriorhodopsin
    • D. Bashford, and K. Gerwert Electrostatic calculations of the pKa 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
  • 76
    • 0034832979 scopus 로고    scopus 로고
    • Artificial cytochrome b: Computer modeling and evaluation of redox potentials
    • D.M. Popovic, S.D. Zaric, B. Rabenstein, and E.W. Knapp Artificial cytochrome b: computer modeling and evaluation of redox potentials J. Am. Chem. Soc. 123 2001 6040 6053
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 6040-6053
    • Popovic, D.M.1    Zaric, S.D.2    Rabenstein, B.3    Knapp, E.W.4
  • 77
    • 0034640465 scopus 로고    scopus 로고
    • A pragmatic approach to structure based calculation of coupled proton and electron transfer in proteins
    • M.R. Gunner, and E. Alexov A pragmatic approach to structure based calculation of coupled proton and electron transfer in proteins Biochim. Biophys. Acta 1458 2000 63 87
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 63-87
    • Gunner, M.R.1    Alexov, E.2
  • 78
    • 33745622986 scopus 로고    scopus 로고
    • Electrostatic environment of hemes in proteins: PKas of hydroxyl ligands
    • Y. Song, J. Mao, and M.R. Gunner Electrostatic environment of hemes in proteins: pKas of hydroxyl ligands Biochemistry 45 2006 7949 7958
    • (2006) Biochemistry , vol.45 , pp. 7949-7958
    • Song, Y.1    Mao, J.2    Gunner, M.R.3
  • 79
    • 0034641675 scopus 로고    scopus 로고
    • Self-assembly of heme a and heme b in a designed four-helix bundle: Implications for a cytochrome c oxidase maquette
    • B.R. Gibney, Y. Isogai, F. Rabanal, K.S. Reddy, A.M. Grosset, C.C. Moser, and P.L. Dutton Self-assembly of heme a and heme b in a designed four-helix bundle: implications for a cytochrome c oxidase maquette Biochemistry 39 2000 11041 11049
    • (2000) Biochemistry , vol.39 , pp. 11041-11049
    • Gibney, B.R.1    Isogai, Y.2    Rabanal, F.3    Reddy, K.S.4    Grosset, A.M.5    Moser, C.C.6    Dutton, P.L.7
  • 80
    • 1542274547 scopus 로고    scopus 로고
    • Heme protein assemblies
    • C.J. Reedy, and B.R. Gibney Heme protein assemblies Chem. Rev. 104 2004 617 649
    • (2004) Chem. Rev. , vol.104 , pp. 617-649
    • Reedy, C.J.1    Gibney, B.R.2
  • 82
    • 0025283002 scopus 로고
    • Electrostatic interactions in macromolecules: Theory and applications
    • K. Sharp, and B. Honig Electrostatic interactions in macromolecules: theory and applications Annu. Rev. Biophys. Biophys. Chem. 19 1990 301 332
    • (1990) Annu. Rev. Biophys. Biophys. Chem. , vol.19 , pp. 301-332
    • Sharp, K.1    Honig, B.2
  • 83
    • 0029833446 scopus 로고    scopus 로고
    • Charge separation and the dielectric constant of proteins: Insights from molecular dynamics
    • T. Simonson, and C.L. Brooks Charge separation and the dielectric constant of proteins: Insights from molecular dynamics J. Am. Chem. Soc. 118 1996 8452 8458
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8452-8458
    • Simonson, T.1    Brooks, C.L.2
  • 84
    • 84962477148 scopus 로고    scopus 로고
    • Structure/function correlations of proteins using MM, QM/MM, and related approaches: Methods, concepts, pitfalls, and current progress
    • A. Shurki, and A. Warshel Structure/function correlations of proteins using MM, QM/MM, and related approaches: methods, concepts, pitfalls, and current progress Adv. Protein Chem. 66 2003 249 259
    • (2003) Adv. Protein Chem. , vol.66 , pp. 249-259
    • Shurki, A.1    Warshel, A.2
  • 86
  • 87
    • 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
  • 88
    • 78650530548 scopus 로고    scopus 로고
    • Theory of coupled electron and proton transfer reactions
    • S. Hammes-Schiffer, and A.A. Stuchebrukhov Theory of coupled electron and proton transfer reactions Chem. Rev. 110 2010 6939 6960
    • (2010) Chem. Rev. , vol.110 , pp. 6939-6960
    • Hammes-Schiffer, S.1    Stuchebrukhov, A.A.2
  • 89
    • 70149103333 scopus 로고    scopus 로고
    • The steady-state mechanism of cytochrome c oxidase: Redox interactions between metal centres
    • M.G. Mason, P. Nicholls, and C.E. Cooper The steady-state mechanism of cytochrome c oxidase: redox interactions between metal centres Biochem. J. 422 2009 237 246
    • (2009) Biochem. J. , vol.422 , pp. 237-246
    • Mason, M.G.1    Nicholls, P.2    Cooper, C.E.3
  • 90
    • 0022967236 scopus 로고
    • Spectroelectrochemical study of cytochrome c oxidase: PH and temperature dependences of the cytochrome potentials. Characterization of site-site interactions
    • D.F. Blair, W.R. Ellis Jr., H. Wang, H.B. Gray, and S.I. Chan Spectroelectrochemical study of cytochrome c oxidase: pH and temperature dependences of the cytochrome potentials. Characterization of site-site interactions J. Biol. Chem. 261 1986 11524 11537
    • (1986) J. Biol. Chem. , vol.261 , pp. 11524-11537
    • Blair, D.F.1    Ellis, Jr.W.R.2    Wang, H.3    Gray, H.B.4    Chan, S.I.5
  • 91
    • 0034732938 scopus 로고    scopus 로고
    • Coupling of electron transfer with proton transfer at heme a and CuA (redox Bohr effects) in cytochrome c oxidase. Studies with the carbon monoxide inhibited enzyme
    • N. Capitanio, G. Capitanio, M. Minuto, E.D. Nitto, L.L. Palese, P. Nicholls, and S. Papa Coupling of electron transfer with proton transfer at heme a and CuA (redox Bohr effects) in cytochrome c oxidase. Studies with the carbon monoxide inhibited enzyme Biochemistry 39 2000 6373 6379
    • (2000) Biochemistry , vol.39 , pp. 6373-6379
    • Capitanio, N.1    Capitanio, G.2    Minuto, M.3    Nitto, E.D.4    Palese, L.L.5    Nicholls, P.6    Papa, S.7
  • 93
    • 0023821272 scopus 로고
    • The location of CuA in mammalian cytochrome c oxidase
    • P.R. Rich, I.C. West, and P. Mitchell The location of CuA in mammalian cytochrome c oxidase FEBS Lett. 233 1988 25 30
    • (1988) FEBS Lett. , vol.233 , pp. 25-30
    • Rich, P.R.1    West, I.C.2    Mitchell, P.3
  • 94
    • 0014216748 scopus 로고
    • Multiple molecular forms of bovine heart cytochrome c: A comparative study of their physicochemical properties and their reactions in biological systems
    • T. Flatmark Multiple molecular forms of bovine heart cytochrome c: a comparative study of their physicochemical properties and their reactions in biological systems J. Biol. Chem. 242 1967 2454 2459
    • (1967) J. Biol. Chem. , vol.242 , pp. 2454-2459
    • Flatmark, T.1
  • 95
    • 0016371404 scopus 로고
    • Thermodynamic relationships in mitochondrial oxidative phosphorylation
    • D.F. Wilson, M. Erecinska, and P.L. Dutton Thermodynamic relationships in mitochondrial oxidative phosphorylation Annu. Rev. Biophys. Bioeng. 3 1974 203 230
    • (1974) Annu. Rev. Biophys. Bioeng. , vol.3 , pp. 203-230
    • Wilson, D.F.1    Erecinska, M.2    Dutton, P.L.3
  • 96
    • 0037093975 scopus 로고    scopus 로고
    • Control of cytochrome c redox potential: Axial ligation and protein environment effects
    • G. Battistuzzi, M. Borsari, J.A. Cowan, A. Ranieri, and M. Sola Control of cytochrome c redox potential: axial ligation and protein environment effects J. Am. Chem. Soc. 124 2002 5315 5324
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5315-5324
    • Battistuzzi, G.1    Borsari, M.2    Cowan, J.A.3    Ranieri, A.4    Sola, M.5
  • 97
    • 0025125898 scopus 로고
    • The effect of pH on redox titrations of haem a in cyanide-liganded cytochrome-c oxidase: Experimental and modelling studies
    • A.J. Moody, and P.R. Rich The effect of pH on redox titrations of haem a in cyanide-liganded cytochrome-c oxidase: experimental and modelling studies Biochim. Biophys. Acta 1015 1990 205 215
    • (1990) Biochim. Biophys. Acta , vol.1015 , pp. 205-215
    • Moody, A.J.1    Rich, P.R.2
  • 98
    • 33646355978 scopus 로고    scopus 로고
    • Redox titration of all electron carriers of cytochrome c oxidase by Fourier transform infrared spectroscopy
    • E.A. Gorbikova, K. Vuorilehto, M. Wikström, and M.I. Verkhovsky Redox titration of all electron carriers of cytochrome c oxidase by Fourier transform infrared spectroscopy Biochemistry 45 2006 5641 5649
    • (2006) Biochemistry , vol.45 , pp. 5641-5649
    • Gorbikova, E.A.1    Vuorilehto, K.2    Wikström, M.3    Verkhovsky, M.I.4
  • 99
    • 0029036305 scopus 로고
    • Control of electron delivery to the oxygen reduction site of cytochrome c oxidase: A role for protons
    • M.I. Verkhovsky, J.E. Morgan, and M. Wikström Control of electron delivery to the oxygen reduction site of cytochrome c oxidase: a role for protons Biochemistry 34 1995 7483 7491
    • (1995) Biochemistry , vol.34 , pp. 7483-7491
    • Verkhovsky, M.I.1    Morgan, J.E.2    Wikström, M.3
  • 100
    • 16344363592 scopus 로고    scopus 로고
    • Simulating redox coupled proton transfer in cytochrome c oxidase: Looking for the proton bottleneck
    • M.H.M. Olsson, P.K. Sharma, and A. Warshel Simulating redox coupled proton transfer in cytochrome c oxidase: looking for the proton bottleneck FEBS Lett. 579 2005 2026 2034
    • (2005) FEBS Lett. , vol.579 , pp. 2026-2034
    • Olsson, M.H.M.1    Sharma, P.K.2    Warshel, A.3
  • 101
  • 102
    • 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
  • 103
    • 39949085428 scopus 로고    scopus 로고
    • Electrostatic control of proton pumping in cytochrome c oxidase
    • E. Fadda, C.-H. Yu, and R. Pomès Electrostatic control of proton pumping in cytochrome c oxidase Biochim. Biophys. Acta 1777 2008 277 284
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 277-284
    • Fadda, E.1    Yu, C.-H.2    Pomès, R.3
  • 104
    • 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
  • 105
    • 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
  • 106
    • 13244260957 scopus 로고    scopus 로고
    • Thermodynamic properties of internal water molecules in the hydrophobic cavity around the catalytic center of cytochrome c oxidase
    • M. Tashiro, and A.A. Stuchebrukhov Thermodynamic properties of internal water molecules in the hydrophobic cavity around the catalytic center of cytochrome c oxidase J. Phys. Chem. B 109 2005 1015 1022
    • (2005) J. Phys. Chem. B , vol.109 , pp. 1015-1022
    • Tashiro, M.1    Stuchebrukhov, A.A.2
  • 107
    • 67649511725 scopus 로고    scopus 로고
    • Molecular dynamics simulation of water in cytochrome c oxidase reveals two water exit pathways and the mechanism of its transport
    • R. Sugitani, and A.A. Stuchebrukhov Molecular dynamics simulation of water in cytochrome c oxidase reveals two water exit pathways and the mechanism of its transport Biochim. Biophys. Acta 1787 2009 1140 1150
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1140-1150
    • Sugitani, R.1    Stuchebrukhov, A.A.2
  • 108
    • 33746928351 scopus 로고    scopus 로고
    • Mutations which decouple the proton pump of the cytochrome c oxidase from Rhodobacter sphaeroides perturb the environment of glutamate 286
    • A.S. Vakkasoglu, J.E. Morgan, D. Han, A.S. Pawate, and R.B. Gennis Mutations which decouple the proton pump of the cytochrome c oxidase from Rhodobacter sphaeroides perturb the environment of glutamate 286 FEBS Lett. 580 2006 4613 4617
    • (2006) FEBS Lett. , vol.580 , pp. 4613-4617
    • Vakkasoglu, A.S.1    Morgan, J.E.2    Han, D.3    Pawate, A.S.4    Gennis, R.B.5
  • 110
    • 80052475923 scopus 로고    scopus 로고
    • Glu-286 rotation and water wire reorientation are unlikely the gating elements for proton pumping in cytochrome c oxidase
    • S. Yang, and Q. Cui Glu-286 rotation and water wire reorientation are unlikely the gating elements for proton pumping in cytochrome c oxidase Biophys. J. 101 2011 61 69
    • (2011) Biophys. J. , vol.101 , pp. 61-69
    • Yang, S.1    Cui, Q.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.