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Volumn 78, Issue 12, 2010, Pages 2691-2698

Similarity of cytochrome c oxidases in different organisms

Author keywords

Cytochrome c oxidase; Electron transfer; Heme copper oxygen reductases; PK a calculations; Proton transfer; Redox potentials

Indexed keywords

CYTOCHROME C OXIDASE; PROTON;

EID: 77955833374     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22783     Document Type: Article
Times cited : (51)

References (41)
  • 1
    • 2542464946 scopus 로고    scopus 로고
    • Coupled proton and electron transfer reactions in cytochrome oxidase
    • Gennis RB. Coupled proton and electron transfer reactions in cytochrome oxidase. Front Biosci 2004;9:581-591.
    • (2004) Front Biosci , vol.9 , pp. 581-591
    • Gennis, R.B.1
  • 2
    • 0032143387 scopus 로고    scopus 로고
    • Proton translocation by bacteriorhodopsin and hemecopper oxidases
    • Wikstrom M. Proton translocation by bacteriorhodopsin and hemecopper oxidases. Curr Opin Struct Biol 1998;8:480-488.
    • (1998) Curr. Opin. Struct Biol. , vol.8 , pp. 480-488
    • Wikstrom, M.1
  • 3
    • 36148938761 scopus 로고    scopus 로고
    • Molecular mechanism of proton translocation by cytochrome c oxidase
    • Belevich I, Verkhovsky MI. Molecular mechanism of proton translocation by cytochrome c oxidase. Antioxidants Redox Signal 2008;10:1-29.
    • (2008) Antioxidants Redox Signal , vol.10 , pp. 1-29
    • Belevich, I.1    Verkhovsky, M.I.2
  • 4
    • 57049180108 scopus 로고    scopus 로고
    • Cytochrome c oxidase: Exciting progress and remaining mysteries
    • Brzezinski P, Gennis RB. Cytochrome c oxidase: exciting progress and remaining mysteries. J Bioenerg Biomembr 2008;40:521-531.
    • (2008) J. Bioenerg Biomembr , vol.40 , pp. 521-531
    • Brzezinski, P.1    Gennis, R.B.2
  • 6
    • 70349493006 scopus 로고    scopus 로고
    • The cytochrome ba (3) oxygen reductase from Thermus thermophilus uses a single input channel for proton delivery to the active site and for proton pumping
    • Chang HY, Hemp J, Chen Y, Fee JA, Gennis RB. The cytochrome ba (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 2009;106:16169-16173.
    • (2009) Proc. Natl. Acad. Sci. U S a , vol.106 , pp. 16169-16173
    • Chang, H.Y.1    Hemp, J.2    Chen, Y.3    Fee, J.A.4    Gennis, R.B.5
  • 7
    • 1242314254 scopus 로고    scopus 로고
    • Electrostatic study of the proton pumping mechanism in bovine heart cytochrome c oxidase
    • Popovic DM, Stuchebrukhov AA. Electrostatic study of the proton pumping mechanism in bovine heart cytochrome c oxidase. J Am Chem Soc 2004;126:1858-1871.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 1858-1871
    • Popovic, D.M.1    Stuchebrukhov, A.A.2
  • 8
    • 2442616154 scopus 로고    scopus 로고
    • Proton pumping mechanism and catalytic cycle of cytochrome c oxidase: Coulomb pump model with kinetic gating
    • Popovic DM, Stuchebrukhov AA. Proton pumping mechanism and catalytic cycle of cytochrome c oxidase: coulomb pump model with kinetic gating. FEBS Lett 2004;566:126-130.
    • (2004) FEBS Lett. , vol.566 , pp. 126-130
    • Popovic, D.M.1    Stuchebrukhov, A.A.2
  • 9
    • 77955787539 scopus 로고    scopus 로고
    • Combined DFT/Continuum electrostatics studies of proton pumping mechanism of cytochrome c oxidase
    • Solomon EI, King RB, Scott RA, editors, John Wiley & Sons: Hoboken
    • Quenneville J, Popovic DM, Stuchebrukhov AA. Combined DFT/Continuum electrostatics studies of proton pumping mechanism of cytochrome c oxidase. In: Solomon EI, King RB, Scott RA, editors. Computational inorganic and bioinorganic chemistry. John Wiley & Sons: Hoboken; 2009.
    • (2009) Computational Inorganic and Bioinorganic Chemistry
    • Quenneville, J.1    Popovic, D.M.2    Stuchebrukhov, A.A.3
  • 11
    • 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
    • Sugitani R, Medvedev ES, Stuchebrukhov AA. Theoretical and computational analysis of the membrane potential generated by cytochrome c oxidase upon single electron injection into the enzyme. Biochim Biophys Acta Bioenerg 2008;1777:1129-1139.
    • (2008) Biochim Biophys. Acta Bioenerg , vol.1777 , pp. 1129-1139
    • Sugitani, R.1    Medvedev, E.S.2    Stuchebrukhov, A.A.3
  • 15
    • 65449120359 scopus 로고    scopus 로고
    • Mechanisms of proton transfer in proteins: Localized charge transfer versus delocalized soliton transfer
    • Stuchebrukhov AA. Mechanisms of proton transfer in proteins: localized charge transfer versus delocalized soliton transfer. Phys Rev E 2009;79:031927.
    • (2009) Phys. Rev. e , vol.79 , pp. 031927
    • Stuchebrukhov, A.A.1
  • 16
    • 57049130390 scopus 로고    scopus 로고
    • A chemically explicit model for the mechanism of proton pumping in heme-copper oxidases
    • Sharpe MA, Ferguson-Miller S. A chemically explicit model for the mechanism of proton pumping in heme-copper oxidases. J Bioenerg Biomembr 2008;40:541-549.
    • (2008) J. Bioenerg Biomembr , vol.40 , pp. 541-549
    • Sharpe, M.A.1    Ferguson-Miller, S.2
  • 17
    • 45549107077 scopus 로고    scopus 로고
    • Electrostatic basis for the uniderectionality of hte primary proton transfer in cytochrome c oxidase
    • Pisliakov AV, Sharma PK, Chu ZT, Haranczyk M, Warshel A. Electrostatic basis for the uniderectionality of hte primary proton transfer in cytochrome c oxidase. Proc Natl Acad Sci USA 2008;105:7726-7731.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7726-7731
    • Pisliakov, A.V.1    Sharma, P.K.2    Chu, Z.T.3    Haranczyk, M.4    Warshel, A.5
  • 18
    • 33745605230 scopus 로고    scopus 로고
    • Calculated proton uptake on anaerobic reduction of cytochrome c oxidase: Is the reaction electroneutral?
    • Song YF, Michonova-Alexova E, Gunner MR. Calculated proton uptake on anaerobic reduction of cytochrome c oxidase: is the reaction electroneutral? Biochemistry 2006;45:7959-7975.
    • (2006) Biochemistry , vol.45 , pp. 7959-7975
    • Song, Y.F.1    Michonova-Alexova, E.2    Gunner, M.R.3
  • 19
    • 29144445121 scopus 로고    scopus 로고
    • Acidity of a Cu-bound histidine in the binuclear center of cytochrome C oxidase
    • Fadda E, Chakrabarti N, Pomes R. Acidity of a Cu-bound histidine in the binuclear center of cytochrome C oxidase. J Phys Chem B 2005;109:22629-22640.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 22629-22640
    • Fadda, E.1    Chakrabarti, N.2    Pomes, R.3
  • 20
    • 33748771721 scopus 로고    scopus 로고
    • Comment on "acidity of a Cubound histidine in the binuclear center of cytochrome c oxidase."
    • Stuchebrukhov AA, Popovic DM. Comment on "acidity of a Cubound histidine in the binuclear center of cytochrome c oxidase." J Phys Chem B 2006;110:17286-17287.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 17286-17287
    • Stuchebrukhov, A.A.1    Popovic, D.M.2
  • 21
    • 14844358231 scopus 로고    scopus 로고
    • DFT/electrostatic calculations of pKa values in cytochrome c oxidase
    • Popovic DM, Quenneville J, Stuchebrukhov AA. DFT/electrostatic calculations of pKa values in cytochrome c oxidase. J Phys Chem B 2005;109:3616-3626.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 3616-3626
    • Popovic, D.M.1    Quenneville, J.2    Stuchebrukhov, A.A.3
  • 22
    • 13444305368 scopus 로고    scopus 로고
    • Proton exit channels in bovine cytochrome c oxidase
    • Popovic DM, Stuchebrukhov AA. Proton exit channels in bovine cytochrome c oxidase. J Phys Chem B 2005;109:1999-2006.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 1999-2006
    • Popovic, D.M.1    Stuchebrukhov, A.A.2
  • 23
    • 0032318376 scopus 로고    scopus 로고
    • Multiple proton-conducting pathways in cytochrome oxidase and a proposed role for the active-site tyrosine
    • Gennis RB. Multiple proton-conducting pathways in cytochrome oxidase and a proposed role for the active-site tyrosine. Biophys Biochim Acta 1998;1365:241-248.
    • (1998) Biophys. Biochim Acta , vol.1365 , pp. 241-248
    • Gennis, R.B.1
  • 24
    • 33750807024 scopus 로고    scopus 로고
    • Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase
    • Qin L, Hiser C, Mulichak A, Garavito RM, Ferguson-Miller S. Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase. Proc Natl Acad Sci USA 2006;103:16117-16122.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 16117-16122
    • Qin, L.1    Hiser, C.2    Mulichak, A.3    Garavito, R.M.4    Ferguson-Miller, S.5
  • 25
    • 0036382724 scopus 로고    scopus 로고
    • The X-ray crystal structures of wild-type and EQ (I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides
    • Svensson-Ek M, Abramson J, Larsson G, Tornroth S, Brzezinski P, Iwata S. The X-ray crystal structures of wild-type and EQ (I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides. J Mol Biol 2002;321:329-339.
    • (2002) J. Mol. Biol. , vol.321 , pp. 329-339
    • Svensson-Ek, M.1    Abramson, J.2    Larsson, G.3    Tornroth, S.4    Brzezinski, P.5    Iwata, S.6
  • 26
    • 0030886203 scopus 로고    scopus 로고
    • Structure at 2.7 angstrom resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody F-V fragment
    • Ostermeier C, Harrenga A, Ermler U, Michel H. Structure at 2.7 angstrom resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody F-V fragment. Proc Natl Acad Sci USA 1997;94:10547-10553.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10547-10553
    • Ostermeier, C.1    Harrenga, A.2    Ermler, U.3    Michel, H.4
  • 28
    • 61449125101 scopus 로고    scopus 로고
    • Dielectric relaxation of cytochrome c oxidase: Comparison of the microscopic and continuum models
    • Leontyev IV, Stuchebrukhov AA. Dielectric relaxation of cytochrome c oxidase: comparison of the microscopic and continuum models. J Chem Phys 2009;130:085103.
    • (2009) J. Chem. Phys. , vol.130 , pp. 085103
    • Leontyev, I.V.1    Stuchebrukhov, A.A.2
  • 30
    • 0026612756 scopus 로고
    • Electrostatic calculations of the pKa values of ionizable groups in bacteriorhodopsin
    • Bashford D, Gerwert K. Electrostatic calculations of the pKa values of ionizable groups in bacteriorhodopsin. J Mol Biol 1992;224:473-486.
    • (1992) J. Mol. Biol. , vol.224 , pp. 473-486
    • Bashford, D.1    Gerwert, K.2
  • 31
    • 84957665033 scopus 로고    scopus 로고
    • An object-oriented programming suite for electrostatic effects in biological molecules
    • Ishikawa Y, Oldehoeft RR, Reynders JVW, Tholburn M, editors, volume 1343 of Lecture Notes in Computer Science. Berlin: Springer;, ISCOPE97
    • Bashford D. An object-oriented programming suite for electrostatic effects in biological molecules. In: Ishikawa Y, Oldehoeft RR, Reynders JVW, Tholburn M, editors. Scientific computing in object-oriented parallel environments, Vol. 1343, (volume 1343 of Lecture Notes in Computer Science). Berlin: Springer; 1997. pp 233-240 (ISCOPE97).
    • (1997) Scientific Computing in Object-oriented Parallel Environments , vol.1343 , pp. 233-240
    • Bashford, D.1
  • 32
    • 0034832979 scopus 로고    scopus 로고
    • Artificial cytochrome b: Computer modeling and evaluation of redox potentials
    • Popovic DM, Zaric SD, Rabenstein B, Knapp EW. Artificial cytochrome b: computer modeling and evaluation of redox potentials. J Am Chem Soc 2001;123:6040-6053.
    • (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
  • 34
    • 84860133569 scopus 로고    scopus 로고
    • Monte Carlo methods for simulation of protein folding and titration
    • Available at
    • Rabenstein B. Monte Carlo methods for simulation of protein folding and titration. Karlsberg online manual, Available at: http://www.liechemiefu-berlin/ karlsberg/1999.
    • Karlsberg Online Manual
    • Rabenstein, B.1
  • 38
    • 0030745897 scopus 로고    scopus 로고
    • The roles 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
    • Konstantinov AA, Siletsky S, Mitchell D, Kaulen A, Gennis RB. The roles 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 USA 1997;94:9085-9090.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9085-9090
    • Konstantinov, A.A.1    Siletsky, S.2    Mitchell, D.3    Kaulen, A.4    Gennis, R.B.5
  • 40
    • 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
    • Durr KL, Koepkee J, Hellwig P, Muller H, Angerere H, Peng G, Olkhova E, Richter OMH, Ludwig B, Michele H. 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 2008;384:865-877.
    • (2008) J. Mol. Biol. , vol.384 , pp. 865-877
    • Durr, K.L.1    Koepkee, J.2    Hellwig, P.3    Muller, H.4    Angerere, H.5    Peng, G.6    Olkhova, E.7    Richter, O.M.H.8    Ludwig, B.9    Michele, H.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.