메뉴 건너뛰기




Volumn 1797, Issue 8, 2010, Pages 1512-1520

Redox-coupled proton transfer in the active site of cytochrome cbb3

Author keywords

Density functional theory (DFT); Electron paramagnetic resonance (EPR); Electron transfer; Heme copper oxidases; Proton transfer; Proton coupled electron transfer (PCET)

Indexed keywords

CYTOCHROME C OXIDASE; CYTOCHROME CBB3; HEME; MUTANT PROTEIN; UNCLASSIFIED DRUG;

EID: 77953737411     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2010.03.004     Document Type: Article
Times cited : (14)

References (70)
  • 1
    • 0031776726 scopus 로고    scopus 로고
    • From NO to OO: Nitric Oxide and Dioxygen in Bacterial Respiration
    • Hendriks J., Gohlke U., Saraste M. From NO to OO: Nitric Oxide and Dioxygen in Bacterial Respiration. J. Bioenerg. Biomembr. 1998, 30:15-24.
    • (1998) J. Bioenerg. Biomembr. , vol.30 , pp. 15-24
    • Hendriks, J.1    Gohlke, U.2    Saraste, M.3
  • 2
    • 0035371783 scopus 로고    scopus 로고
    • A novel scenario for the evolution of haem-copper oxygen reductases
    • Pereira M.M., Santana M., Teixeira M. A novel scenario for the evolution of haem-copper oxygen reductases. Biochim. Biophys. Acta 2001, 1505:185-208.
    • (2001) Biochim. Biophys. Acta , vol.1505 , pp. 185-208
    • Pereira, M.M.1    Santana, M.2    Teixeira, M.3
  • 4
    • 44449146602 scopus 로고    scopus 로고
    • Diversity of the Heme-Copper Superfamily in Archaea: Insights from Genomics and Structural Modeling
    • Hemp J., Gennis R.B. Diversity of the Heme-Copper Superfamily in Archaea: Insights from Genomics and Structural Modeling. Results Probl. Cell Differ. 2008, 45:1-31.
    • (2008) Results Probl. Cell Differ. , vol.45 , pp. 1-31
    • Hemp, J.1    Gennis, R.B.2
  • 6
    • 0017358508 scopus 로고
    • Proton pump coupled to cytochrome c oxidase in mitochondria
    • Wikström M.K.F. Proton pump coupled to cytochrome c oxidase in mitochondria. Nature 1977, 266:271-273.
    • (1977) Nature , vol.266 , pp. 271-273
    • Wikström, M.K.F.1
  • 7
    • 34848850437 scopus 로고    scopus 로고
    • Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases
    • Wikström M., Verkhovsky M.I. Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases. Biochim. Biophys. Acta 2007, 1767:1200-1214.
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1200-1214
    • Wikström, M.1    Verkhovsky, M.I.2
  • 8
    • 0035461311 scopus 로고    scopus 로고
    • ATP synthase - a marvellous rotary engine of the cell
    • Yoshida M., Muneyuki E., Hisabori T. ATP synthase - a marvellous rotary engine of the cell. Nature 2001, 2:669-677.
    • (2001) Nature , vol.2 , pp. 669-677
    • Yoshida, M.1    Muneyuki, E.2    Hisabori, T.3
  • 9
    • 0004053611 scopus 로고
    • John Wiley and Sons
    • Voet D., Voet J.G. Biochemistry 1995, 533, 566. John Wiley and Sons. Second Edition.
    • (1995) Biochemistry , pp. 533-566
    • Voet, D.1    Voet, J.G.2
  • 10
    • 0034544593 scopus 로고    scopus 로고
    • 3 oxidase in clinically relevant proteobacteria?
    • 3 oxidase in clinically relevant proteobacteria?. Trends Microbiol. 2000, 8:542-543.
    • (2000) Trends Microbiol. , vol.8 , pp. 542-543
    • Myllykallio, H.1    Liebl, U.2
  • 19
    • 33845989511 scopus 로고    scopus 로고
    • Evolutionary migration of a post-translationally modified active-site residue in the proton-pumping heme-copper oxygen reductase
    • Hemp J., Robinson D.E., Ganesan K.B., Martinez T.J., Kelleher N.L., Gennis R.B. Evolutionary migration of a post-translationally modified active-site residue in the proton-pumping heme-copper oxygen reductase. Biochemistry 2006, 45:15405-15410.
    • (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
  • 20
    • 0032924497 scopus 로고    scopus 로고
    • Evidence for a copper-coordinated histidine-tyrosine cross-link in the active site of cytochrome oxidase
    • Buse G., Soulimane T., Dewor M., Meyer H.E., Blüggel M. Evidence for a copper-coordinated histidine-tyrosine cross-link in the active site of cytochrome oxidase. Protein Sci. 1999, 8:985-990.
    • (1999) Protein Sci. , vol.8 , pp. 985-990
    • Buse, G.1    Soulimane, T.2    Dewor, M.3    Meyer, H.E.4    Blüggel, M.5
  • 22
    • 0036382724 scopus 로고    scopus 로고
    • The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides
    • (202)
    • M. Svensson-Ek, J. Abramson, G. Larsson, S. Törnroth, P. Brzezinski, 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 (202) 329-339.
    • J. Mol. Biol. , vol.321 , pp. 329-339
    • Svensson-Ek, M.1    Abramson, J.2    Larsson, G.3    Törnroth, S.4    Brzezinski, P.5    Iwata, S.6
  • 24
    • 0034654622 scopus 로고    scopus 로고
    • Insights into the Functional Role of the Tyrosine-Histidine Linkage in Cytochrome c Oxidase
    • McCauley K.M., Vrtis J.M., Dupont J., van der Donk W.A. Insights into the Functional Role of the Tyrosine-Histidine Linkage in Cytochrome c Oxidase. J. Am. Chem. Soc. 2000, 122:2403-2404.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2403-2404
    • McCauley, K.M.1    Vrtis, J.M.2    Dupont, J.3    van der Donk, W.A.4
  • 25
    • 28944454616 scopus 로고    scopus 로고
    • Structural Character and Energetics of Tyrosyl Radical Formation by Electron/Proton Transfers of a Covalently Linked Histidine-Tyrosine: A Model for Cytochrome c Oxidase
    • Bu Y., Cukier R.I. Structural Character and Energetics of Tyrosyl Radical Formation by Electron/Proton Transfers of a Covalently Linked Histidine-Tyrosine: A Model for Cytochrome c Oxidase. J. Phys. Chem. B 2005, 109:22013-22026.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 22013-22026
    • Bu, Y.1    Cukier, R.I.2
  • 29
    • 0021723457 scopus 로고
    • Crystal structure of yeast cytochrome c peroxidase refined at 1.7-Å resolution
    • Finzel B.C., Poulos T.L., Kraut J. Crystal structure of yeast cytochrome c peroxidase refined at 1.7-Å resolution. J. Biol. Chem. 1984, 259:13027-13036.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13027-13036
    • Finzel, B.C.1    Poulos, T.L.2    Kraut, J.3
  • 31
    • 0028769662 scopus 로고
    • How a protein binds B12: A 3.0Å X-ray structure of B12-binding domains of methionine synthase
    • Drennan C.L., Huang S., Drummond J.T., Matthews R.G., Ludwig M.L. How a protein binds B12: A 3.0Å X-ray structure of B12-binding domains of methionine synthase. Science 1994, 266:1669-1674.
    • (1994) Science , vol.266 , pp. 1669-1674
    • Drennan, C.L.1    Huang, S.2    Drummond, J.T.3    Matthews, R.G.4    Ludwig, M.L.5
  • 32
    • 0027231963 scopus 로고
    • The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme
    • Goodin D.B., McRee D.E. The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme. Biochemistry 1993, 32:3313-3324.
    • (1993) Biochemistry , vol.32 , pp. 3313-3324
    • Goodin, D.B.1    McRee, D.E.2
  • 33
    • 0030800149 scopus 로고    scopus 로고
    • How enzymes control the reactivity of adenosylcobalamine: Effect on coenzyme binding and catalysis of mutations in conserved histidine-aspartate pair of glutamate mutase
    • Chen H.P., Marsh E.N.G. How enzymes control the reactivity of adenosylcobalamine: Effect on coenzyme binding and catalysis of mutations in conserved histidine-aspartate pair of glutamate mutase. Biochemistry 1997, 36:7884-7889.
    • (1997) Biochemistry , vol.36 , pp. 7884-7889
    • Chen, H.P.1    Marsh, E.N.G.2
  • 34
    • 0033585083 scopus 로고    scopus 로고
    • The cytochrome c oxidase from Paracoccus denitrificans does not change the metal center ligation upon reduction
    • Harrenga A., Michel H. The cytochrome c oxidase from Paracoccus denitrificans does not change the metal center ligation upon reduction. J. Biol. Chem. 1999, 274:33296-33299.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33296-33299
    • Harrenga, A.1    Michel, H.2
  • 35
    • 0041784950 scopus 로고    scopus 로고
    • MacKerell, D. Bashford, M. Bellott, R. L. Jr. Dunbrack, J. D. Evanseck, M. J. Field, S. Fischer, J. Gao, H. Guo, S. Ha, et al., All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • Jr A.D. MacKerell, D. Bashford, M. Bellott, R. L. Jr. Dunbrack, J. D. Evanseck, M. J. Field, S. Fischer, J. Gao, H. Guo, S. Ha, et al., All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B 1998, 102:3586-3616.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 3586-3616
    • Jr, A.D.1
  • 36
    • 40549119124 scopus 로고    scopus 로고
    • Charge parameterization of the metal centers in cytochrome c oxidase
    • Johansson M.P., Kaila V.R.I., Laakkonen L. Charge parameterization of the metal centers in cytochrome c oxidase. J. Comp. Chem. 2007, 29:753-767.
    • (2007) J. Comp. Chem. , vol.29 , pp. 753-767
    • Johansson, M.P.1    Kaila, V.R.I.2    Laakkonen, L.3
  • 38
    • 4243553426 scopus 로고
    • Density-functional exchange-energy approximation with correct asymptotic behaviour
    • Becke A.D. Density-functional exchange-energy approximation with correct asymptotic behaviour. Phys. Rev. A 1988, 38:3098-3100.
    • (1988) Phys. Rev. A , vol.38 , pp. 3098-3100
    • Becke, A.D.1
  • 39
    • 5944261746 scopus 로고
    • Density-functional approximation for the correlation-energy of the inhomogenous electron gas
    • Perdew J.P. Density-functional approximation for the correlation-energy of the inhomogenous electron gas. Phys. Rev. B 1986, 33:8822-8824.
    • (1986) Phys. Rev. B , vol.33 , pp. 8822-8824
    • Perdew, J.P.1
  • 40
    • 0038617492 scopus 로고    scopus 로고
    • Fast evaluation of the coulomb potential for electron densities using multipole accelerated resolution of identity approximation
    • Sierka M., Hogekamp A., Ahlrichs R. Fast evaluation of the coulomb potential for electron densities using multipole accelerated resolution of identity approximation. J. Chem. Phys. 2003, 118:9136-9148.
    • (2003) J. Chem. Phys. , vol.118 , pp. 9136-9148
    • Sierka, M.1    Hogekamp, A.2    Ahlrichs, R.3
  • 41
    • 26344435738 scopus 로고
    • Fully optimized contracted Gaussian basis sets for atoms Li to Kr
    • Schäfer A., Horn H., Ahlrichs R. Fully optimized contracted Gaussian basis sets for atoms Li to Kr. J. Chem. Phys. 1992, 97:2571-2577.
    • (1992) J. Chem. Phys. , vol.97 , pp. 2571-2577
    • Schäfer, A.1    Horn, H.2    Ahlrichs, R.3
  • 42
    • 0039209924 scopus 로고
    • Fully optimized contracted Gaussian basis sets of triple zeta valence quality for atoms Li to Kr
    • Schäfer A., Huber C., Ahlrichs R. Fully optimized contracted Gaussian basis sets of triple zeta valence quality for atoms Li to Kr. J. Chem. Phys. 1994, 100:5829-5835.
    • (1994) J. Chem. Phys. , vol.100 , pp. 5829-5835
    • Schäfer, A.1    Huber, C.2    Ahlrichs, R.3
  • 43
    • 33846103838 scopus 로고    scopus 로고
    • Performance of density functional for first row transition metal systems
    • Jensen K.P., Roos B.O., Ryde U. Performance of density functional for first row transition metal systems. J. Chem. Phys. 2007, 126:1410301-1410314.
    • (2007) J. Chem. Phys. , vol.126 , pp. 1410301-1410314
    • Jensen, K.P.1    Roos, B.O.2    Ryde, U.3
  • 44
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. III The role of exact exchange
    • Becke A.D. Density-functional thermochemistry. III The role of exact exchange. J. Chem. Phys. 1993, 98:5648-5652.
    • (1993) J. Chem. Phys. , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 45
    • 0345491105 scopus 로고
    • Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density
    • Lee C., Yang W., Parr R.G. Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density. Phys. Rev. B Condens. Matter 1988, 37:785-789.
    • (1988) Phys. Rev. B Condens. Matter , vol.37 , pp. 785-789
    • Lee, C.1    Yang, W.2    Parr, R.G.3
  • 46
    • 0001213712 scopus 로고    scopus 로고
    • Assessment of Gaussian-3 and density functional theories for a larger experimental test set
    • Curtiss L.A., Raghavachari K., Redfern P.C., Pople J.A. Assessment of Gaussian-3 and density functional theories for a larger experimental test set. J. Chem. Phys. 2000, 112:7374-7383.
    • (2000) J. Chem. Phys. , vol.112 , pp. 7374-7383
    • Curtiss, L.A.1    Raghavachari, K.2    Redfern, P.C.3    Pople, J.A.4
  • 47
    • 84961980743 scopus 로고
    • COSMO: a new approach to dielectric screening in solvents with explicit expressions for the screening energy and its gradient
    • Klamt A., Schuurmann G. COSMO: a new approach to dielectric screening in solvents with explicit expressions for the screening energy and its gradient. J. Chem. Soc. Perkin Trans. 1993, 2:799-805.
    • (1993) J. Chem. Soc. Perkin Trans. , vol.2 , pp. 799-805
    • Klamt, A.1    Schuurmann, G.2
  • 48
    • 3643084753 scopus 로고
    • The absolute potential of the standard hydrogen elecrode: a new estimate
    • Reiss H., Heller A. The absolute potential of the standard hydrogen elecrode: a new estimate. J. Phys. Chem. 1985, 89:4207-4213.
    • (1985) J. Phys. Chem. , vol.89 , pp. 4207-4213
    • Reiss, H.1    Heller, A.2
  • 49
    • 0035936304 scopus 로고    scopus 로고
    • Prediction of electron paramagnetic resonance g values using coupled perturbed Hartree-Fock and Kohn-Sham theory
    • Neese F. Prediction of electron paramagnetic resonance g values using coupled perturbed Hartree-Fock and Kohn-Sham theory. J. Chem. Phys. 2001, 115:11080-11096.
    • (2001) J. Chem. Phys. , vol.115 , pp. 11080-11096
    • Neese, F.1
  • 50
    • 0037305748 scopus 로고    scopus 로고
    • Quantum chemical calculations of spectroscopic properties of metalloproteins and model compounds: EPR and Mossbauer properties
    • Neese F. Quantum chemical calculations of spectroscopic properties of metalloproteins and model compounds: EPR and Mossbauer properties. Curr. Opin. Chem. Biol. 2003, 7:125-135.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 125-135
    • Neese, F.1
  • 51
    • 34547538177 scopus 로고    scopus 로고
    • Density Functional Study of EPR Parameters and Spin-Density Distribution of Azurin and Other Blue-Copper Proteins
    • Remenyi C., Reviakine R., Kaupp M. Density Functional Study of EPR Parameters and Spin-Density Distribution of Azurin and Other Blue-Copper Proteins. J. Phys. Chem. B 2007, 111:8290-8304.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 8290-8304
    • Remenyi, C.1    Reviakine, R.2    Kaupp, M.3
  • 52
    • 4243539377 scopus 로고
    • Electronic structure calculations on workstation computers: The program system turbomole
    • Ahlrichs R., Bär M., Häser M., Horn H., Kölmel C. Electronic structure calculations on workstation computers: The program system turbomole. Chem. Phys. Lett. 1989, 162:165-169.
    • (1989) Chem. Phys. Lett. , vol.162 , pp. 165-169
    • Ahlrichs, R.1    Bär, M.2    Häser, M.3    Horn, H.4    Kölmel, C.5
  • 53
    • 0031276121 scopus 로고    scopus 로고
    • Equilibrium Geometries and Electronic Structure of Iron-Porphyrin Complexes: A Density Functional Study
    • Rovira C., Kunc K., Hutter J., Ballone P., Parrinello M. Equilibrium Geometries and Electronic Structure of Iron-Porphyrin Complexes: A Density Functional Study. J. Phys. Chem. A 1997, 101:8914-8925.
    • (1997) J. Phys. Chem. A , vol.101 , pp. 8914-8925
    • Rovira, C.1    Kunc, K.2    Hutter, J.3    Ballone, P.4    Parrinello, M.5
  • 54
    • 1542347678 scopus 로고    scopus 로고
    • Importance of proximal hydrogen bonds in haem proteins
    • Jensen K.P., Ryde U. Importance of proximal hydrogen bonds in haem proteins. Mol. Phys. 2003, 101:2003-2018.
    • (2003) Mol. Phys. , vol.101 , pp. 2003-2018
    • Jensen, K.P.1    Ryde, U.2
  • 55
    • 40549129032 scopus 로고    scopus 로고
    • Protonation of the proximal histidine ligand in haem peroxidases
    • Heimdal J., Rydberg P., Ryde U. Protonation of the proximal histidine ligand in haem peroxidases. J. Phys. Chem. B 2008, 112:2501-2510.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 2501-2510
    • Heimdal, J.1    Rydberg, P.2    Ryde, U.3
  • 56
    • 0000444479 scopus 로고
    • NMR evidence for a horseradish peroxidase state with a deprotonated histidine
    • De Ropp J.S., Thanabal V., La Mar G.N. NMR evidence for a horseradish peroxidase state with a deprotonated histidine. J. Am. Chem. Soc. 1985, 107:8268-8270.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 8268-8270
    • De Ropp, J.S.1    Thanabal, V.2    La Mar, G.N.3
  • 57
    • 36849137094 scopus 로고
    • A molecular orbital theory of reactivity in aromatic hydrocarbons
    • Fukui K., Yonezawa T., Shingu H. A molecular orbital theory of reactivity in aromatic hydrocarbons. J. Chem. Phys. 1952, 20:722-725.
    • (1952) J. Chem. Phys. , vol.20 , pp. 722-725
    • Fukui, K.1    Yonezawa, T.2    Shingu, H.3
  • 58
    • 27544442115 scopus 로고    scopus 로고
    • Proton-Mediated Electron Configuration Change in High-Spin Iron(II) Porphyrinates
    • Hu C., Noll B.C., Schulz C.E., Scheidt W.R. Proton-Mediated Electron Configuration Change in High-Spin Iron(II) Porphyrinates. J. Am. Chem. Soc. 2005, 127:15018-15019.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 15018-15019
    • Hu, C.1    Noll, B.C.2    Schulz, C.E.3    Scheidt, W.R.4
  • 59
    • 17644392758 scopus 로고    scopus 로고
    • Electronic Configuration Assignment and the Importance of Low-Lying Excited States in High-Spin Imidazole-Ligated Iron(II) Porphyrinates
    • Hu C., Roth A., Ellison M.K., Jin A., Ellis C.M., Schulz C.M., Scheidt W.R. Electronic Configuration Assignment and the Importance of Low-Lying Excited States in High-Spin Imidazole-Ligated Iron(II) Porphyrinates. J. Am. Chem. Soc. 2005, 127:5675-5688.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 5675-5688
    • Hu, C.1    Roth, A.2    Ellison, M.K.3    Jin, A.4    Ellis, C.M.5    Schulz, C.M.6    Scheidt, W.R.7
  • 60
    • 67649476220 scopus 로고    scopus 로고
    • Recent developments of the quantum chemical cluster approach for modeling enzyme reactions
    • Siegbahn P.E.M., Himo F. Recent developments of the quantum chemical cluster approach for modeling enzyme reactions. J. Biol. Inorg. Chem. 2009, 14:643-651.
    • (2009) J. Biol. Inorg. Chem. , vol.14 , pp. 643-651
    • Siegbahn, P.E.M.1    Himo, F.2
  • 61
    • 33744479736 scopus 로고    scopus 로고
    • Quantum-Chemical Predictions of Redox Potentials of Organic Anions in Dimethyl Sulfoxide and Reevaluation of Bond Dissociation Enthalpies Measured by the Electrochemical Methods
    • Fu Y., Liu L., Wang Y.M., Li J.N., Yu T.Q., Guo Q.X. Quantum-Chemical Predictions of Redox Potentials of Organic Anions in Dimethyl Sulfoxide and Reevaluation of Bond Dissociation Enthalpies Measured by the Electrochemical Methods. J. Phys. Chem. A 2006, 110:5874-5886.
    • (2006) J. Phys. Chem. A , vol.110 , pp. 5874-5886
    • Fu, Y.1    Liu, L.2    Wang, Y.M.3    Li, J.N.4    Yu, T.Q.5    Guo, Q.X.6
  • 62
    • 18744394619 scopus 로고    scopus 로고
    • Quantum-Chemical Predictions of Absolute Standard Redox Potentials of Diverse Organic Molecules and Free Radicals in Acetonitrile
    • Fu Y., Liu L., Yu H.Z., Wang Y.M., Guo Q.X. Quantum-Chemical Predictions of Absolute Standard Redox Potentials of Diverse Organic Molecules and Free Radicals in Acetonitrile. J. Am. Chem. Soc. 2005, 127:7227-7234.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 7227-7234
    • Fu, Y.1    Liu, L.2    Yu, H.Z.3    Wang, Y.M.4    Guo, Q.X.5
  • 64
    • 0028210150 scopus 로고
    • Oxygen binding and activation: Early steps in the reaction of oxygen with Cytochrome c Oxidase
    • Verkhovsky M.I., Morgan J.E., Wikström M. Oxygen binding and activation: Early steps in the reaction of oxygen with Cytochrome c Oxidase. Biochemistry 1994, 33:3079-3086.
    • (1994) Biochemistry , vol.33 , pp. 3079-3086
    • Verkhovsky, M.I.1    Morgan, J.E.2    Wikström, M.3
  • 65
    • 0016709349 scopus 로고
    • Functional intermediates in the reaction of membrane-bound cytochrome oxidase with oxygen
    • Chance B., Saronio C., Leigh J.S. Functional intermediates in the reaction of membrane-bound cytochrome oxidase with oxygen. J. Biol. Chem. 1975, 250:9226-9237.
    • (1975) J. Biol. Chem. , vol.250 , pp. 9226-9237
    • Chance, B.1    Saronio, C.2    Leigh, J.S.3
  • 66
    • 0041508308 scopus 로고    scopus 로고
    • Metal-bridging mechanism for O-O bond cleavage in cytochrome c oxidase
    • Blomberg M.R., Siegbahn P.E., Wikström M. Metal-bridging mechanism for O-O bond cleavage in cytochrome c oxidase. Inorg. Chem. 2003, 42:5231-5243.
    • (2003) Inorg. Chem. , vol.42 , pp. 5231-5243
    • Blomberg, M.R.1    Siegbahn, P.E.2    Wikström, M.3
  • 70
    • 0026590397 scopus 로고
    • A graphics program for the analysis and display of molecular dynamics trajectories
    • Laaksonen L. A graphics program for the analysis and display of molecular dynamics trajectories. J. Mol. Graph. 1992, 10:33-34.
    • (1992) J. Mol. Graph. , vol.10 , pp. 33-34
    • Laaksonen, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.