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Volumn 1777, Issue 7-8, 2008, Pages 1001-1019

The Q-cycle reviewed: How well does a monomeric mechanism of the bc1 complex account for the function of a dimeric complex?

Author keywords

bc1 complex; Constraints on molecular mechanism; Coulombic interaction; Kinetic model; Q cycle; Thermodynamic model

Indexed keywords

ANION; ASPARAGINE; CYTOCHROME B; CYTOCHROME C1; DIMER; GLUTAMIC ACID; HEMOPROTEIN; HISTIDINE; IRON SULFUR PROTEIN; MONOMER; MUTANT PROTEIN; MYXOTHIAZOL; OXYGEN; PROTON; SEMIQUINONE; SUPEROXIDE; TYROSINE; UBIQUINOL CYTOCHROME C REDUCTASE; UBIQUINONE;

EID: 46449118774     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2008.04.037     Document Type: Review
Times cited : (107)

References (148)
  • 2
    • 1942447877 scopus 로고    scopus 로고
    • 1 complex - function in the context of structure
    • 1 complex - function in the context of structure. Annu. Rev. Physiol. 66 (2004) 689-733
    • (2004) Annu. Rev. Physiol. , vol.66 , pp. 689-733
    • Crofts, A.R.1
  • 3
    • 33748893871 scopus 로고    scopus 로고
    • 1 complex: what is there left to argue about?
    • Wikström M. (Ed), Royal Society of Chemistry Publishing, Cambridge
    • 1 complex: what is there left to argue about?. In: Wikström M. (Ed). Biophysical and Structural Aspects of Bioenergetics (2005), Royal Society of Chemistry Publishing, Cambridge 123-155
    • (2005) Biophysical and Structural Aspects of Bioenergetics , pp. 123-155
    • Crofts, A.R.1
  • 4
    • 1942472600 scopus 로고    scopus 로고
    • 1 complex controls the rate of ubihydroquinone oxidation
    • 1 complex controls the rate of ubihydroquinone oxidation. Biochim. Biophys. Acta 1655 (2004) 77-92
    • (2004) Biochim. Biophys. Acta , vol.1655 , pp. 77-92
    • Crofts, A.R.1
  • 6
    • 20744443796 scopus 로고    scopus 로고
    • 1 complex dimer is reduced through center N
    • 1 complex dimer is reduced through center N. J. Biol. Chem. 280 (2005) 22732-22740
    • (2005) J. Biol. Chem. , vol.280 , pp. 22732-22740
    • Covian, R.1    Trumpower, B.L.2
  • 7
    • 1342325555 scopus 로고    scopus 로고
    • Reversible redox energy coupling in electron transfer chains
    • Osyczka A., Moser C.C., Daldal F., and Dutton P.L. Reversible redox energy coupling in electron transfer chains. Nature 427 (2004) 607-612
    • (2004) Nature , vol.427 , pp. 607-612
    • Osyczka, A.1    Moser, C.C.2    Daldal, F.3    Dutton, P.L.4
  • 9
    • 23244438766 scopus 로고    scopus 로고
    • 1 complex: reaction mechanism and prevention of short-circuiting
    • 1 complex: reaction mechanism and prevention of short-circuiting. Biochim. Biophys. Acta 1709 (2005) 5-34
    • (2005) Biochim. Biophys. Acta , vol.1709 , pp. 5-34
    • Mulkidjanian, A.Y.1
  • 10
    • 33846029501 scopus 로고    scopus 로고
    • Proton translocation by the cytochrome bc1 complexes of phototrophic bacteria: introducing the activated Q-cycle
    • Mulkidjanian A.Y. Proton translocation by the cytochrome bc1 complexes of phototrophic bacteria: introducing the activated Q-cycle. Photochem. Photobiol. Sci. 6 (2007) 19-34
    • (2007) Photochem. Photobiol. Sci. , vol.6 , pp. 19-34
    • Mulkidjanian, A.Y.1
  • 11
    • 3542991515 scopus 로고    scopus 로고
    • The quinone chemistry of bc complexes
    • Rich P.R. The quinone chemistry of bc complexes. Biochim. Biophys. Acta 1658 (2004) 165-171
    • (2004) Biochim. Biophys. Acta , vol.1658 , pp. 165-171
    • Rich, P.R.1
  • 12
    • 0001104663 scopus 로고
    • The role of the quinone pool in the cyclic electron-transfer chain of Rhodopseudomonas sphaeroides: a modified Q-cycle mechanism
    • Crofts A.R., Meinhardt S.W., Jones K.R., and Snozzi M. The role of the quinone pool in the cyclic electron-transfer chain of Rhodopseudomonas sphaeroides: a modified Q-cycle mechanism. Biochim. Biophys. Acta 723 (1983) 202-218
    • (1983) Biochim. Biophys. Acta , vol.723 , pp. 202-218
    • Crofts, A.R.1    Meinhardt, S.W.2    Jones, K.R.3    Snozzi, M.4
  • 13
    • 3042767574 scopus 로고    scopus 로고
    • The Q-cycle, - a personal perspective
    • Crofts A.R. The Q-cycle, - a personal perspective. Photosynth. Res. 80 (2003) 223-243
    • (2003) Photosynth. Res. , vol.80 , pp. 223-243
    • Crofts, A.R.1
  • 14
    • 0029765443 scopus 로고    scopus 로고
    • Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants
    • Skulachev V.P. Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants. Q. Rev. Biophys. 29 (1996) 169-202
    • (1996) Q. Rev. Biophys. , vol.29 , pp. 169-202
    • Skulachev, V.P.1
  • 15
    • 0021288856 scopus 로고
    • Determination of the production of superoxide radicals and hydrogen-peroxide in mitochondria
    • Boveris A. Determination of the production of superoxide radicals and hydrogen-peroxide in mitochondria. Methods Enzymol. 105 (1984) 429-435
    • (1984) Methods Enzymol. , vol.105 , pp. 429-435
    • Boveris, A.1
  • 16
    • 0021996572 scopus 로고
    • Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
    • Turrens J.F., Alexandre A., and Lehninger A.L. Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria. Arch. Biochem. Biophys. 237 (1985) 408-414
    • (1985) Arch. Biochem. Biophys. , vol.237 , pp. 408-414
    • Turrens, J.F.1    Alexandre, A.2    Lehninger, A.L.3
  • 17
    • 0034442070 scopus 로고    scopus 로고
    • The nature and mechanism of superoxide production by the electron transport chain: its relevance to aging
    • Muller F. The nature and mechanism of superoxide production by the electron transport chain: its relevance to aging. J. Am. Aging Assoc. 23 (2000) 227-253
    • (2000) J. Am. Aging Assoc. , vol.23 , pp. 227-253
    • Muller, F.1
  • 18
    • 0142195820 scopus 로고    scopus 로고
    • Superoxide anion generation by the cytochrome bc1 complex
    • Sun J., and Trumpower B.L. Superoxide anion generation by the cytochrome bc1 complex. Arch. Biochem. Biophys. 419 (2003) 198-206
    • (2003) Arch. Biochem. Biophys. , vol.419 , pp. 198-206
    • Sun, J.1    Trumpower, B.L.2
  • 19
    • 0034951169 scopus 로고    scopus 로고
    • Mitochondria, oxygen free radicals, and apoptosis
    • Raha S., and Robinson B.H. Mitochondria, oxygen free radicals, and apoptosis. Am. J. Med. Genet. 106 (2001) 62-70
    • (2001) Am. J. Med. Genet. , vol.106 , pp. 62-70
    • Raha, S.1    Robinson, B.H.2
  • 20
    • 0141815741 scopus 로고    scopus 로고
    • Production of reactive oxygen species by mitochondria: central role of complex III
    • Chen Q., Vazquez E.J., Moghaddas S., Hoppel C.L., and Lesnefsky E.J. Production of reactive oxygen species by mitochondria: central role of complex III. J. Biol. Chem. 278 (2003) 36027-36031
    • (2003) J. Biol. Chem. , vol.278 , pp. 36027-36031
    • Chen, Q.1    Vazquez, E.J.2    Moghaddas, S.3    Hoppel, C.L.4    Lesnefsky, E.J.5
  • 23
    • 0035078258 scopus 로고    scopus 로고
    • Effects of mutations in mitochondrial cytochrome b in yeast and man - deficiency, compensation and disease
    • Fisher N., and Meunier B. Effects of mutations in mitochondrial cytochrome b in yeast and man - deficiency, compensation and disease. Eur. J. Biochem. 268 (2001) 1155-1162
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1155-1162
    • Fisher, N.1    Meunier, B.2
  • 24
    • 48749143707 scopus 로고
    • The electrochemical domain of photosynthesis
    • Crofts A.R., and Wraight C.A. The electrochemical domain of photosynthesis. Biochim. Biophys. Acta 726 (1983) 149-186
    • (1983) Biochim. Biophys. Acta , vol.726 , pp. 149-186
    • Crofts, A.R.1    Wraight, C.A.2
  • 26
    • 0002658350 scopus 로고
    • How rapid are the internal reactions of the ubiquinol:cytochrome c2 oxidoreductase?
    • Crofts A.R., and Wang Z. How rapid are the internal reactions of the ubiquinol:cytochrome c2 oxidoreductase?. Photosynth. Res. 22 (1989) 69-87
    • (1989) Photosynth. Res. , vol.22 , pp. 69-87
    • Crofts, A.R.1    Wang, Z.2
  • 30
    • 0035979755 scopus 로고    scopus 로고
    • 1 complex: crystallization of membrane proteins with antibody fragments
    • 1 complex: crystallization of membrane proteins with antibody fragments. FEBS Lett. 504 (2001) 126-132
    • (2001) FEBS Lett. , vol.504 , pp. 126-132
    • Hunte, C.1
  • 33
    • 0041401742 scopus 로고    scopus 로고
    • Structure of the yeast cytochrome bc1 complex with a hydroxyquinone anion Qo site inhibitor bound
    • Palsdottir H., Lojero C.G., Trumpower B.L., and Hunte C. Structure of the yeast cytochrome bc1 complex with a hydroxyquinone anion Qo site inhibitor bound. J. Biol. Chem. 278 (2003) 31303-31311
    • (2003) J. Biol. Chem. , vol.278 , pp. 31303-31311
    • Palsdottir, H.1    Lojero, C.G.2    Trumpower, B.L.3    Hunte, C.4
  • 36
    • 0032825183 scopus 로고    scopus 로고
    • Steered molecular dynamics simulation of the Rieske subunit motion in the cytochrome bc1 complex
    • Izrailev S., Crofts A.R., Berry E.A., and Schulten K. Steered molecular dynamics simulation of the Rieske subunit motion in the cytochrome bc1 complex. Biophys. J. 77 (1999) 1753-1768
    • (1999) Biophys. J. , vol.77 , pp. 1753-1768
    • Izrailev, S.1    Crofts, A.R.2    Berry, E.A.3    Schulten, K.4
  • 42
    • 0037055973 scopus 로고    scopus 로고
    • Interactions of quinone with the iron-sulfur protein of the bc(1) complex: is the mechanism spring-loaded?
    • Crofts A.R., Shinkarev V.P., Dikanov S.A., Samoilova R.I., and Kolling D. Interactions of quinone with the iron-sulfur protein of the bc(1) complex: is the mechanism spring-loaded?. Biochim. Biophys. Acta 1555 (2002) 48-53
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 48-53
    • Crofts, A.R.1    Shinkarev, V.P.2    Dikanov, S.A.3    Samoilova, R.I.4    Kolling, D.5
  • 44
    • 0142063412 scopus 로고    scopus 로고
    • The reduction potentials of Rieske clusters: the importance of the coupling between oxidation state and histidine protonation state
    • Zu Y., Manon M.-J., Couture M.M.-J., Kolling D.R.J., Crofts A.R., Eltis L.D., Fee J.A., and Hirst J. The reduction potentials of Rieske clusters: the importance of the coupling between oxidation state and histidine protonation state. Biochemistry 42 (2003) 12400-12408
    • (2003) Biochemistry , vol.42 , pp. 12400-12408
    • Zu, Y.1    Manon, M.-J.2    Couture, M.M.-J.3    Kolling, D.R.J.4    Crofts, A.R.5    Eltis, L.D.6    Fee, J.A.7    Hirst, J.8
  • 46
    • 33748744224 scopus 로고    scopus 로고
    • Identification of hydrogen bonds to the Rieske cluster through the weakly coupled nitrogens detected by electron spin echo envelope modulation spectroscopy
    • Dikanov S.A., Kolling D.R.J., Endeward B., Samoilova R.I., Prisner T.F., Nair S.K., and Crofts A.R. Identification of hydrogen bonds to the Rieske cluster through the weakly coupled nitrogens detected by electron spin echo envelope modulation spectroscopy. J. Biol. Chem. 281 (2006) 27416-27425
    • (2006) J. Biol. Chem. , vol.281 , pp. 27416-27425
    • Dikanov, S.A.1    Kolling, D.R.J.2    Endeward, B.3    Samoilova, R.I.4    Prisner, T.F.5    Nair, S.K.6    Crofts, A.R.7
  • 47
    • 46449128640 scopus 로고    scopus 로고
    • 1 complex: exploring the roles of hydrogen bonding in tuning the redox potential of iron-sulfur clusters
    • 1 complex: exploring the roles of hydrogen bonding in tuning the redox potential of iron-sulfur clusters. Structure 15 (2007) 1-10
    • (2007) Structure , vol.15 , pp. 1-10
    • Kolling, D.R.J.1    Brunzelle, J.S.2    Lhee, S.3    Crofts, A.R.4    Nair, S.K.5
  • 50
    • 0036933444 scopus 로고    scopus 로고
    • Density functional calculation of pKa values and redox potentials in the bovine Rieske iron-sulfur protein
    • Ullmann G.M., Noodleman L., and Case D.A. Density functional calculation of pKa values and redox potentials in the bovine Rieske iron-sulfur protein. J. Biol. Inorg. Chem. 7 (2002) 632-639
    • (2002) J. Biol. Inorg. Chem. , vol.7 , pp. 632-639
    • Ullmann, G.M.1    Noodleman, L.2    Case, D.A.3
  • 51
    • 0034480510 scopus 로고    scopus 로고
    • A cluster exposed: structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins
    • Colbert C., Couture M.M.-J., Eltis L.D., and Bolin J.T. A cluster exposed: structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins. Structure 8 (2000) 1267-1278
    • (2000) Structure , vol.8 , pp. 1267-1278
    • Colbert, C.1    Couture, M.M.-J.2    Eltis, L.D.3    Bolin, J.T.4
  • 55
    • 0030861648 scopus 로고    scopus 로고
    • 1 complex: the "proton-gated affinity change" mechanism
    • 1 complex: the "proton-gated affinity change" mechanism. FEBS Lett. 412 (1997) 257-264
    • (1997) FEBS Lett. , vol.412 , pp. 257-264
    • Link, T.A.1
  • 58
    • 0032502711 scopus 로고    scopus 로고
    • Alteration of the midpoint potential of the Rieske iron-sulfur protein by changes of amino acids forming H-bonds to the iron-sulfur cluster
    • Denke E., Merbitzzahradnik T., Hatzfeld O.M., Snyder C.H., Link T.A., and Trumpower B.L. Alteration of the midpoint potential of the Rieske iron-sulfur protein by changes of amino acids forming H-bonds to the iron-sulfur cluster. J. Biol. Chem. 273 (1998) 9085-9093
    • (1998) J. Biol. Chem. , vol.273 , pp. 9085-9093
    • Denke, E.1    Merbitzzahradnik, T.2    Hatzfeld, O.M.3    Snyder, C.H.4    Link, T.A.5    Trumpower, B.L.6
  • 62
    • 33747797654 scopus 로고    scopus 로고
    • 15N NMR titration study demonstrates the role of iron-ligated histidines in the pH dependence of the reduction potential
    • 15N NMR titration study demonstrates the role of iron-ligated histidines in the pH dependence of the reduction potential. J. Am. Chem. Soc. 128 (2006) 10672-10673
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 10672-10673
    • Lin, I.-J.1    Chen, Y.2    Fee, J.A.3    Song, J.4    Westler, W.M.5    Markley, J.L.6
  • 63
    • 15544382668 scopus 로고    scopus 로고
    • Direct observation of redox-linked histidine protonation changes in the iron-sulfur protein of the cytochrome bc(1) complex by ATR-FTIR spectroscopy
    • Iwaki M., Yakovlev G., Hirst J., Osyczka A., Dutton P.L., Marshall D., and Rich P.R. Direct observation of redox-linked histidine protonation changes in the iron-sulfur protein of the cytochrome bc(1) complex by ATR-FTIR spectroscopy. Biochemistry 44 (2005) 4230-4237
    • (2005) Biochemistry , vol.44 , pp. 4230-4237
    • Iwaki, M.1    Yakovlev, G.2    Hirst, J.3    Osyczka, A.4    Dutton, P.L.5    Marshall, D.6    Rich, P.R.7
  • 81
    • 0007715338 scopus 로고
    • A new effect of antimycin on the b-cytochromes of Rps. sphaeroides
    • Sybesma C. (Ed), Martinus Nijhoff/Dr. W. Junk Publishers, The Hague
    • Meinhardt S.W., and Crofts A.R. A new effect of antimycin on the b-cytochromes of Rps. sphaeroides. In: Sybesma C. (Ed). Advances in Photosynthesis Research vol. 1 (1984), Martinus Nijhoff/Dr. W. Junk Publishers, The Hague 649-652
    • (1984) Advances in Photosynthesis Research , vol.1 , pp. 649-652
    • Meinhardt, S.W.1    Crofts, A.R.2
  • 86
    • 22544467474 scopus 로고    scopus 로고
    • 1 complex: a new crystal structure reveals an altered intramolecular hydrogen-bonding pattern
    • 1 complex: a new crystal structure reveals an altered intramolecular hydrogen-bonding pattern. J. Mol. Biol. 351 (2005) 573-597
    • (2005) J. Mol. Biol. , vol.351 , pp. 573-597
    • Huang, L.S.1    Cobessi, D.2    Tung, E.Y.3    Berry, E.A.4
  • 88
    • 16244392086 scopus 로고    scopus 로고
    • When X-rays modify the protein structure: radiation damage at work
    • Carugo O., and Carugo K.D. When X-rays modify the protein structure: radiation damage at work. Trends Biochem. Sci. 30 (2005) 213-219
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 213-219
    • Carugo, O.1    Carugo, K.D.2
  • 89
    • 20644465999 scopus 로고    scopus 로고
    • On the influence of the incident photon energy on the radiation damage in crystalline biological samples
    • Weiss M.S., et al. On the influence of the incident photon energy on the radiation damage in crystalline biological samples. J. Synchrotron Radiat. 12 (2005) 304-309
    • (2005) J. Synchrotron Radiat. , vol.12 , pp. 304-309
    • Weiss, M.S.1
  • 91
    • 0015497373 scopus 로고
    • Thermodynamic and kinetics characterization of electron-transfer components in situ in Rps. spheroides and Rhodospirillum rubrum
    • Dutton P.L., and Jackson J.B. Thermodynamic and kinetics characterization of electron-transfer components in situ in Rps. spheroides and Rhodospirillum rubrum. Eur. J. Biochem. 30 (1972) 495-510
    • (1972) Eur. J. Biochem. , vol.30 , pp. 495-510
    • Dutton, P.L.1    Jackson, J.B.2
  • 92
    • 0018115502 scopus 로고
    • Redox potentiometry in biological systems
    • Dutton P.L., and Wilson D.M. Redox potentiometry in biological systems. Methods Enzymol. 54 (1976) 411-435
    • (1976) Methods Enzymol. , vol.54 , pp. 411-435
    • Dutton, P.L.1    Wilson, D.M.2
  • 93
    • 46449083638 scopus 로고    scopus 로고
    • 1 complex from Rhodobacter sphaeroides. Ph.D. Thesis, University of Illinois at Urbana-Champaign., 1984.
    • 1 complex from Rhodobacter sphaeroides. Ph.D. Thesis, University of Illinois at Urbana-Champaign., 1984.
  • 95
    • 0021368185 scopus 로고
    • Thermodynamic properties of the semiquinone and its binding site in the ubiquinol-cytochrome c (c2) oxidoreductase of respiratory and photosynthetic systems
    • Robertson D., Prince R., Bowyer J., Matsuura K., Dutton P., and Ohnishi T. Thermodynamic properties of the semiquinone and its binding site in the ubiquinol-cytochrome c (c2) oxidoreductase of respiratory and photosynthetic systems. J. Biol. Chem. 259 (1984) 1758-1763
    • (1984) J. Biol. Chem. , vol.259 , pp. 1758-1763
    • Robertson, D.1    Prince, R.2    Bowyer, J.3    Matsuura, K.4    Dutton, P.5    Ohnishi, T.6
  • 96
    • 0025316271 scopus 로고
    • Inhibitor effects on redox-linked protonations of the b haems of the mitochondrial bc1 complex
    • Rich P.R., Jeal A.E., Madgwick S.A., and Moody A.J. Inhibitor effects on redox-linked protonations of the b haems of the mitochondrial bc1 complex. Biochim. Biophys. Acta 1018 (1990) 29-40
    • (1990) Biochim. Biophys. Acta , vol.1018 , pp. 29-40
    • Rich, P.R.1    Jeal, A.E.2    Madgwick, S.A.3    Moody, A.J.4
  • 97
    • 0024971005 scopus 로고
    • The pathway of the quinol/quinone transhydrogenation reaction in ubiquinol: cytochrome-c reductase of Neurospora mitochondria
    • Zweck A., Bechmann G., and Weiss H. The pathway of the quinol/quinone transhydrogenation reaction in ubiquinol: cytochrome-c reductase of Neurospora mitochondria. Eur. J. Biochem. 183 (1989) 199-203
    • (1989) Eur. J. Biochem. , vol.183 , pp. 199-203
    • Zweck, A.1    Bechmann, G.2    Weiss, H.3
  • 98
    • 0025780587 scopus 로고
    • The interactions of duroquinol, DBMIB and NQNO with the chloroplast cytochrome bf complex
    • Rich P.R., Madgwick S.A., and Moss D.A. The interactions of duroquinol, DBMIB and NQNO with the chloroplast cytochrome bf complex. Biochim. Biophys. Acta 1058 (1991) 312-328
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 312-328
    • Rich, P.R.1    Madgwick, S.A.2    Moss, D.A.3
  • 99
    • 0035940440 scopus 로고    scopus 로고
    • The electric field generated by photosynthetic reaction center induces rapid reversed electron transfer in the bc(1) complex
    • Shinkarev V.P., Crofts A.R., and Wraight C.A. The electric field generated by photosynthetic reaction center induces rapid reversed electron transfer in the bc(1) complex. Biochemistry 40 (2001) 12584-12590
    • (2001) Biochemistry , vol.40 , pp. 12584-12590
    • Shinkarev, V.P.1    Crofts, A.R.2    Wraight, C.A.3
  • 100
    • 0017879979 scopus 로고
    • The preparation and characterization of highly purified enzymically active complex III from baker's yeast
    • Siedow J.N., Power S., del la Rosa F.F., and Palmer G. The preparation and characterization of highly purified enzymically active complex III from baker's yeast. J. Biol. Chem. 253 (1978) 2392-2399
    • (1978) J. Biol. Chem. , vol.253 , pp. 2392-2399
    • Siedow, J.N.1    Power, S.2    del la Rosa, F.F.3    Palmer, G.4
  • 101
    • 0021116793 scopus 로고
    • Reductive titration of CoQ-depleted complex III from baker's yeast: evidence for an exchange-coupled complex between QHand low-spin ferricytochrome b
    • de la Rosa F.F., and Palmer G. Reductive titration of CoQ-depleted complex III from baker's yeast: evidence for an exchange-coupled complex between QHand low-spin ferricytochrome b. FEBS Lett. 163 (1983) 140-143
    • (1983) FEBS Lett. , vol.163 , pp. 140-143
    • de la Rosa, F.F.1    Palmer, G.2
  • 105
  • 107
    • 0019368928 scopus 로고
    • On the mechanism of photosynthetic electron transfer in Rps. capsulata and Rps. sphaeroides
    • Bowyer J.R., and Crofts A.R. On the mechanism of photosynthetic electron transfer in Rps. capsulata and Rps. sphaeroides. Biochim. Biophys. Acta 636 (1981) 218-233
    • (1981) Biochim. Biophys. Acta , vol.636 , pp. 218-233
    • Bowyer, J.R.1    Crofts, A.R.2
  • 110
    • 0021774551 scopus 로고
    • Electron transport in chromatophores from Rhodopseudomonas sphaeroides GA fused with liposomes
    • Snozzi M., and Crofts A.R. Electron transport in chromatophores from Rhodopseudomonas sphaeroides GA fused with liposomes. Biochim. Biophys. Acta, Bioenerg. 766 (1984) 451-463
    • (1984) Biochim. Biophys. Acta, Bioenerg. , vol.766 , pp. 451-463
    • Snozzi, M.1    Crofts, A.R.2
  • 113
    • 33746911977 scopus 로고    scopus 로고
    • 1 complex components in situ: a simple and robust alternative to the traditional difference wavelength approach
    • 1 complex components in situ: a simple and robust alternative to the traditional difference wavelength approach. Biochim. Biophys. Acta 1757 (2006) 273-283
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 273-283
    • Shinkarev, V.P.1    Crofts, A.R.2    Wraight, C.A.3
  • 114
    • 0023040886 scopus 로고
    • Determination of partition and lateral diffusion coefficients of ubiquinones by fluorescence quenching of n-(9-anthroyloxy)stearic acids in phospholipid vesicles and mitochondrial membranes
    • Fato R., Battino M., Degli Esposti M., Parenti Castelli G., and Lenaz G. Determination of partition and lateral diffusion coefficients of ubiquinones by fluorescence quenching of n-(9-anthroyloxy)stearic acids in phospholipid vesicles and mitochondrial membranes. Biochemistry 25 (1986) 3378-3390
    • (1986) Biochemistry , vol.25 , pp. 3378-3390
    • Fato, R.1    Battino, M.2    Degli Esposti, M.3    Parenti Castelli, G.4    Lenaz, G.5
  • 116
    • 0014199203 scopus 로고
    • On the antimycin-sensitive cleavage of complex III of the mitochondrial respiratory chain
    • Rieske J.S., Baum H., Stoner C.D., and Lipton S.H. On the antimycin-sensitive cleavage of complex III of the mitochondrial respiratory chain. J. Biol. Chem. 242 (1967) 4854-4866
    • (1967) J. Biol. Chem. , vol.242 , pp. 4854-4866
    • Rieske, J.S.1    Baum, H.2    Stoner, C.D.3    Lipton, S.H.4
  • 117
  • 118
    • 0022004980 scopus 로고
    • Electron transfers in chemistry and biology
    • Marcus R.A., and Sutin N. Electron transfers in chemistry and biology. Biochim. Biophys. Acta 811 (1985) 265-322
    • (1985) Biochim. Biophys. Acta , vol.811 , pp. 265-322
    • Marcus, R.A.1    Sutin, N.2
  • 119
    • 0019084947 scopus 로고
    • Quantum mechanical tunnelling in biological systems
    • DeVault D. Quantum mechanical tunnelling in biological systems. Q. Rev. Biophys. 13 (1980) 387-564
    • (1980) Q. Rev. Biophys. , vol.13 , pp. 387-564
    • DeVault, D.1
  • 124
    • 33748343422 scopus 로고    scopus 로고
    • Darwin at the molecular scale: selection and variance in electron tunnelling proteins including cytochrome c oxidase
    • Moser C.C., Page C.C., and Dutton P.L. Darwin at the molecular scale: selection and variance in electron tunnelling proteins including cytochrome c oxidase. Philos. Trans. R. Soc. 361 (2006) 1295-1305
    • (2006) Philos. Trans. R. Soc. , vol.361 , pp. 1295-1305
    • Moser, C.C.1    Page, C.C.2    Dutton, P.L.3
  • 125
    • 34047201634 scopus 로고    scopus 로고
    • 1 complex dimer is controlled by the energized state and by impaired electron transfer between low and high potential hemes
    • 1 complex dimer is controlled by the energized state and by impaired electron transfer between low and high potential hemes. FEBS Lett. 581 (2007) 1535-1541
    • (2007) FEBS Lett. , vol.581 , pp. 1535-1541
    • Shinkarev, V.P.1    Wraight, C.A.2
  • 126
    • 0037073797 scopus 로고    scopus 로고
    • 1 complex is independent of the Rieske protein redox state - consequences for semiquinone stabilization in the quinol oxidation site
    • 1 complex is independent of the Rieske protein redox state - consequences for semiquinone stabilization in the quinol oxidation site. J. Biol. Chem. 277 (2002) 48449-48455
    • (2002) J. Biol. Chem. , vol.277 , pp. 48449-48455
    • Covián, R.1    Juan Pablo Pardo, J.P.2    Moreno-Sánchez, R.3
  • 127
    • 3042767574 scopus 로고    scopus 로고
    • The Q-cycle, - a personal perspective
    • Crofts A.R. The Q-cycle, - a personal perspective. Photosynth. Res. 80 (2003) 223-243
    • (2003) Photosynth. Res. , vol.80 , pp. 223-243
    • Crofts, A.R.1
  • 128
    • 0015607377 scopus 로고
    • The kinetics of the redox reactions of ubiquinone related to the electron-transport activity in the respiratory chain
    • Kröger A., and Klingenberg M. The kinetics of the redox reactions of ubiquinone related to the electron-transport activity in the respiratory chain. Eur. J. Biochem. 34 (1973) 358-368
    • (1973) Eur. J. Biochem. , vol.34 , pp. 358-368
    • Kröger, A.1    Klingenberg, M.2
  • 129
    • 0015909789 scopus 로고
    • Further evidence for the pool function of ubiquinone as derived from the inhibition of the electron transport by antimycin
    • Kröger A., and Klingenberg M. Further evidence for the pool function of ubiquinone as derived from the inhibition of the electron transport by antimycin. Eur. J. Biochem. 39 (1973) 313-323
    • (1973) Eur. J. Biochem. , vol.39 , pp. 313-323
    • Kröger, A.1    Klingenberg, M.2
  • 131
    • 0026674915 scopus 로고
    • Nonlinear inhibition curves for tight-binding inhibitors of dimeric ubiquinol-cytochrome c oxidoreductase - evidence for rapid inhibitor mobility
    • Bechmann G., Weiss H., and Rich P. Nonlinear inhibition curves for tight-binding inhibitors of dimeric ubiquinol-cytochrome c oxidoreductase - evidence for rapid inhibitor mobility. Eur. J. Biochem. 208 (1992) 315-325
    • (1992) Eur. J. Biochem. , vol.208 , pp. 315-325
    • Bechmann, G.1    Weiss, H.2    Rich, P.3
  • 133
    • 0023666405 scopus 로고
    • Kinetic measurements of electron transfer in coupled chromatophores from photosynthetic bacteria: a method of correction for the electrochromic effects
    • Venturoli G., Virgili M., Melandri B.A., and Crofts A.R. Kinetic measurements of electron transfer in coupled chromatophores from photosynthetic bacteria: a method of correction for the electrochromic effects. FEBS Lett. 219 (1987) 477-484
    • (1987) FEBS Lett. , vol.219 , pp. 477-484
    • Venturoli, G.1    Virgili, M.2    Melandri, B.A.3    Crofts, A.R.4
  • 136
    • 0032542006 scopus 로고    scopus 로고
    • 6f complex in the purple bacteria Rhodobacter sphaeroides: an example of the structural plasticity of a membrane cytochrome
    • 6f complex in the purple bacteria Rhodobacter sphaeroides: an example of the structural plasticity of a membrane cytochrome. Biochemistry 37 (1998) 16280-16288
    • (1998) Biochemistry , vol.37 , pp. 16280-16288
    • Kuras, R.1    Guergova-Kuras, M.2    Crofts, A.R.3
  • 137
    • 34848821939 scopus 로고    scopus 로고
    • Marcus treatment of endergonic reactions: a commentary
    • Crofts A.R., and Rose S. Marcus treatment of endergonic reactions: a commentary. Biochim. Biophys. Acta 1767 (2007) 1228-1232
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1228-1232
    • Crofts, A.R.1    Rose, S.2
  • 138
    • 0023180298 scopus 로고
    • Electron tunneling paths in proteins
    • Kuki A., and Wolynes P.G. Electron tunneling paths in proteins. Science 236 (1987) 1647-1652
    • (1987) Science , vol.236 , pp. 1647-1652
    • Kuki, A.1    Wolynes, P.G.2
  • 139
    • 0034613172 scopus 로고    scopus 로고
    • Dynamically controlled protein tunneling paths in photosynthetic reaction centers
    • Balabin I.A., and Onuchic J.N. Dynamically controlled protein tunneling paths in photosynthetic reaction centers. Science 290 (2000) 114-117
    • (2000) Science , vol.290 , pp. 114-117
    • Balabin, I.A.1    Onuchic, J.N.2
  • 140
    • 33645793013 scopus 로고    scopus 로고
    • Conformationally averaged score functions for electronic propagation in proteins
    • Kawatsu T., Beratan D.N., and Kakitani T. Conformationally averaged score functions for electronic propagation in proteins. J. Phys. Chem. B 110 (2006) 5747-5757
    • (2006) J. Phys. Chem. B , vol.110 , pp. 5747-5757
    • Kawatsu, T.1    Beratan, D.N.2    Kakitani, T.3
  • 141
    • 33846849448 scopus 로고    scopus 로고
    • Coupling coherence distinguishes structure sensitivity in protein electron transfer
    • Prytkova T.R., Kurnikov I.V., and Beratan D.N. Coupling coherence distinguishes structure sensitivity in protein electron transfer. Science 315 (2007) 622-625
    • (2007) Science , vol.315 , pp. 622-625
    • Prytkova, T.R.1    Kurnikov, I.V.2    Beratan, D.N.3
  • 143
    • 13544270860 scopus 로고    scopus 로고
    • Interference, fluctuation, and alternation of electron tunneling in protein media. 1. two tunneling routes in photosynthetic reaction center alternate due to thermal fluctuation of protein conformation
    • Nishioka H., Kimura A., Yamato T., Kawatsu T., and Kakitani T. Interference, fluctuation, and alternation of electron tunneling in protein media. 1. two tunneling routes in photosynthetic reaction center alternate due to thermal fluctuation of protein conformation. J. Phys. Chem. B 109 (2005) 1978-1987
    • (2005) J. Phys. Chem. B , vol.109 , pp. 1978-1987
    • Nishioka, H.1    Kimura, A.2    Yamato, T.3    Kawatsu, T.4    Kakitani, T.5
  • 144
    • 0033464509 scopus 로고    scopus 로고
    • Magnetic spectroscopic (EPR, ESEEM, Mössbauer, MCD and NMR) studies of low-spin ferriheme centers and their corresponding heme proteins
    • Walker F.A. Magnetic spectroscopic (EPR, ESEEM, Mössbauer, MCD and NMR) studies of low-spin ferriheme centers and their corresponding heme proteins. Coord. Chem. Rev. 185-186 (1999) 471-534
    • (1999) Coord. Chem. Rev. , vol.185-186 , pp. 471-534
    • Walker, F.A.1
  • 145
    • 1542334744 scopus 로고    scopus 로고
    • Models of the bis-histidine-ligated electron-transferring cytochromes. Comparative geometric and electronic structure of low-spin ferro- and ferrihemes
    • Walker F.A. Models of the bis-histidine-ligated electron-transferring cytochromes. Comparative geometric and electronic structure of low-spin ferro- and ferrihemes. Chem. Rev. 104 (2004) 589-615
    • (2004) Chem. Rev. , vol.104 , pp. 589-615
    • Walker, F.A.1
  • 146
    • 0025913125 scopus 로고
    • 1 complex from Rb. sphaeroides by site-directed mutagenesis
    • 1 complex from Rb. sphaeroides by site-directed mutagenesis. Biochemistry 30 (1991) 6747-6754
    • (1991) Biochemistry , vol.30 , pp. 6747-6754
    • Yun, C.-H.1    Crofts, A.R.2    Gennis, R.B.3
  • 148
    • 0030963762 scopus 로고    scopus 로고
    • Role of deprotonation events in ubihydroquinone:cytochrome c oxidoreductase from bovine heart and yeast mitochondria
    • Brandt U., and Okun J.G. Role of deprotonation events in ubihydroquinone:cytochrome c oxidoreductase from bovine heart and yeast mitochondria. Biochemistry 36 (1997) 11234-11240
    • (1997) Biochemistry , vol.36 , pp. 11234-11240
    • Brandt, U.1    Okun, J.G.2


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