메뉴 건너뛰기




Volumn 66, Issue , 2004, Pages 689-733

The cytochrome bc1 complex: Function in the context of structure

Author keywords

Antimycin; Mechanism; Myxothiazol; Stigmatellin; Superoxide

Indexed keywords

ADENOSINE TRIPHOSPHATE; CITRININ; FREE RADICAL; MYXOTHIAZOL; REACTIVE OXYGEN METABOLITE; STIGMATELLIN; SUPEROXIDE; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 1942447877     PISSN: 00664278     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.physiol.66.032102.150251     Document Type: Review
Times cited : (391)

References (172)
  • 4
    • 0000724864 scopus 로고    scopus 로고
    • Some new structural aspects and old controversies concerning the cytochrome b6f complex of oxygenic photosynthesis
    • Cramer WA, Soriano GM, Ponomarev M, Huang D, Zhang H, et al. 1996. Some new structural aspects and old controversies concerning the cytochrome b6f complex of oxygenic photosynthesis. Annu. Rev. Plant Physiol. Plant Mol. Biol. 47:477-508
    • (1996) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.47 , pp. 477-508
    • Cramer, W.A.1    Soriano, G.M.2    Ponomarev, M.3    Huang, D.4    Zhang, H.5
  • 5
    • 0023184331 scopus 로고
    • Bacterial evolution
    • Woese CR. 1987. Bacterial evolution. Microbiol. Rev. 51:221-71
    • (1987) Microbiol. Rev. , vol.51 , pp. 221-271
    • Woese, C.R.1
  • 8
    • 0035078258 scopus 로고    scopus 로고
    • Effects of mutations in mitochondrial cytochrome b in yeast and man - Deficiency, compensation and disease
    • Fisher N, Meunier B. 2001. Effects of mutations in mitochondrial cytochrome b in yeast and man - deficiency, compensation and disease. Eur. J. Biochem. 268:1155-62
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1155-1162
    • Fisher, N.1    Meunier, B.2
  • 10
    • 0031932864 scopus 로고    scopus 로고
    • Mitochondrial myopathies. Genetic mechanisms
    • Rose MR. 1998. Mitochondrial myopathies. Genetic mechanisms. Arch. Neurol. 55:17-24
    • (1998) Arch. Neurol. , vol.55 , pp. 17-24
    • Rose, M.R.1
  • 11
    • 0035096954 scopus 로고    scopus 로고
    • Mitochondrial myopathies and the role of the pathologist in the molecular era
    • Vogel H. 2001. Mitochondrial myopathies and the role of the pathologist in the molecular era. J. Neuropathol. Exp. Neurol. 60:217-27
    • (2001) J. Neuropathol. Exp. Neurol. , vol.60 , pp. 217-227
    • Vogel, H.1
  • 12
    • 0021288856 scopus 로고
    • Determination of the production of superoxide radicals and hydrogen-peroxide in mitochondria
    • Boveris A. 1984. Determination of the production of superoxide radicals and hydrogen-peroxide in mitochondria. Methods Enzymol. 105:429-35
    • (1984) Methods Enzymol. , vol.105 , pp. 429-435
    • Boveris, A.1
  • 13
    • 0021996572 scopus 로고
    • Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
    • Turrens JF, Alexandre A, Lehninger AL. 1985. Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria. Arch. Biochem. Biophys. 237:408-14
    • (1985) Arch. Biochem. Biophys. , vol.237 , pp. 408-414
    • Turrens, J.F.1    Alexandre, A.2    Lehninger, A.L.3
  • 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 VP. 1996. Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants. Q. Rev. Biophys. 29:169-202
    • (1996) Q. Rev. Biophys. , vol.29 , pp. 169-202
    • Skulachev, V.P.1
  • 15
    • 0034442070 scopus 로고    scopus 로고
    • The nature and mechanism of superoxide production by the electron transport chain: Its relevance to aging
    • Muller F. 2000. The nature and mechanism of superoxide production by the electron transport chain: its relevance to aging. J. Am. Aging Assoc. 23:227-53
    • (2000) J. Am. Aging Assoc. , vol.23 , pp. 227-253
    • Muller, F.1
  • 16
    • 0141815741 scopus 로고    scopus 로고
    • Production of reactive oxygen species by mitochondria: Central role of Complex III
    • Chen Q, Vazquez EJ, Moghaddas S, Hoppel CL, Lesnefsky EJ. 2003. Production of reactive oxygen species by mitochondria: central role of Complex III. J. Biol. Chem. 278:36027-31
    • (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
  • 18
    • 0031239721 scopus 로고    scopus 로고
    • Mitochondrial electron transport can become a significant source of oxidative injury in cardiomyocytes
    • Hoek TLV, Shao ZH, Li CQ, Schumacker PT, Becker LB. 1997. Mitochondrial electron transport can become a significant source of oxidative injury in cardiomyocytes. J. Mol. Cell. Cardiol. 29:2441-50
    • (1997) J. Mol. Cell. Cardiol. , vol.29 , pp. 2441-2450
    • Hoek, T.L.V.1    Shao, Z.H.2    Li, C.Q.3    Schumacker, P.T.4    Becker, L.B.5
  • 19
    • 0027023063 scopus 로고
    • Free radical theory of aging: History
    • Harman D. 1992. Free radical theory of aging: history. EXS 62:1-10
    • (1992) EXS , vol.62 , pp. 1-10
    • Harman, D.1
  • 20
  • 21
    • 0031916984 scopus 로고    scopus 로고
    • The free radical theory of aging matures
    • Beckman KB, Ames BN. 1998. The free radical theory of aging matures. Physiol. Rev. 78:547-81
    • (1998) Physiol. Rev. , vol.78 , pp. 547-581
    • Beckman, K.B.1    Ames, B.N.2
  • 22
    • 0034951169 scopus 로고    scopus 로고
    • Mitochondria, oxygen free radicals, and apoptosis
    • Raha S, Robinson BH. 2001. Mitochondria, oxygen free radicals, and apoptosis. Am. J. Med. Genet. 106:62-70
    • (2001) Am. J. Med. Genet. , vol.106 , pp. 62-70
    • Raha, S.1    Robinson, B.H.2
  • 23
    • 0034962860 scopus 로고    scopus 로고
    • Mitochondria and degenerative disorders
    • Orth M, Schapira AHV. 2001. Mitochondria and degenerative disorders. Am. J. Med. Genet. 106:27-36
    • (2001) Am. J. Med. Genet. , vol.106 , pp. 27-36
    • Orth, M.1    Schapira, A.H.V.2
  • 24
    • 0030809576 scopus 로고    scopus 로고
    • Reactive oxygen species, mitochondria, apoptosis and aging
    • Papa S, Skulachev VP. 1997. Reactive oxygen species, mitochondria, apoptosis and aging. Mol. Cell. Biochem. 174:305-19
    • (1997) Mol. Cell. Biochem. , vol.174 , pp. 305-319
    • Papa, S.1    Skulachev, V.P.2
  • 26
    • 0020448949 scopus 로고
    • The site and mechanism of action of myxothiazol as an inhibitor of electron transfer in Rhodopseudomonas sphaeroides
    • Meinhardt SW, Crofts AR. 1982. The site and mechanism of action of myxothiazol as an inhibitor of electron transfer in Rhodopseudomonas sphaeroides. FEBS Lett. 149:217-22
    • (1982) FEBS Lett. , vol.149 , pp. 217-222
    • Meinhardt, S.W.1    Crofts, A.R.2
  • 28
    • 0024276081 scopus 로고
    • Characterization of binding of the methoxyacrylate inhibitors to mitochondrial cytochrome c reductase
    • Brandt U, Schagger H, von Jagow G. 1988. Characterization of binding of the methoxyacrylate inhibitors to mitochondrial cytochrome c reductase. Eur. J. Biochem. 173:499-506
    • (1988) Eur. J. Biochem. , vol.173 , pp. 499-506
    • Brandt, U.1    Schagger, H.2    Von Jagow, G.3
  • 29
    • 0021986927 scopus 로고
    • The interaction of yeast Complex III with some respiratory inhibitors
    • Tsai A-L, Kauten R, Palmer G. 1985. The interaction of yeast Complex III with some respiratory inhibitors. Biochim. Biophys. Acta 806:418-26
    • (1985) Biochim. Biophys. Acta , vol.806 , pp. 418-426
    • Tsai, A.-L.1    Kauten, R.2    Palmer, G.3
  • 30
    • 0027245581 scopus 로고
    • What information do inhibitors provide about the structure of the hydroquinone oxidation site of ubiquinol:cytochrome c oxidoreductase
    • Link TA, Haase U, Brandt U, von Jagow G. 1993. What information do inhibitors provide about the structure of the hydroquinone oxidation site of ubiquinol:cytochrome c oxidoreductase. J. Bioenerg. Biomembr. 25:221-32
    • (1993) J. Bioenerg. Biomembr. , vol.25 , pp. 221-232
    • Link, T.A.1    Haase, U.2    Brandt, U.3    Von Jagow, G.4
  • 31
    • 0015911233 scopus 로고
    • The mechanism of action of the respiratory inhibitor, antimycin
    • Slater EC. 1973.The mechanism of action of the respiratory inhibitor, antimycin. Biochim. Biophys. Acta 301:129-54
    • (1973) Biochim. Biophys. Acta , vol.301 , pp. 129-154
    • Slater, E.C.1
  • 32
    • 0032781364 scopus 로고    scopus 로고
    • Resistance mutations reveal the atovaquone-binding domain of cytochrome b in malaria parasites
    • Srivastava IK, Morrisey JM, Darrouzet E, Daldal F, Vaidya AB. 1999. Resistance mutations reveal the atovaquone-binding domain of cytochrome b in malaria parasites. Mol. Microbiol. 33:704-11
    • (1999) Mol. Microbiol. , vol.33 , pp. 704-711
    • Srivastava, I.K.1    Morrisey, J.M.2    Darrouzet, E.3    Daldal, F.4    Vaidya, A.B.5
  • 33
    • 84987156662 scopus 로고
    • Fungicidal Beta-methoxyacrylates - From natural products to novel synthetic agricultural fungicides
    • Beautement K, Clough JM, Defraine PJ, Godfrey CRA. 1991. Fungicidal Beta-methoxyacrylates - from natural products to novel synthetic agricultural fungicides. Pestic. Sci. 31:499-519
    • (1991) Pestic. Sci. , vol.31 , pp. 499-519
    • Beautement, K.1    Clough, J.M.2    Defraine, P.J.3    Godfrey, C.R.A.4
  • 36
    • 0002293353 scopus 로고    scopus 로고
    • Strobilurins - From natural products to a new class of fungicides
    • ed. LG Copping, Cambridge, UK: Thomas Graham House, R. Soc. Chem.
    • Sauter H, Ammermann E, Roehl F. 1996. Strobilurins - from natural products to a new class of fungicides. In Crop Protection Agents from Nature, ed. LG Copping, pp. 50-81. Cambridge, UK: Thomas Graham House, R. Soc. Chem.
    • (1996) Crop Protection Agents from Nature , pp. 50-81
    • Sauter, H.1    Ammermann, E.2    Roehl, F.3
  • 43
    • 0034660152 scopus 로고    scopus 로고
    • 1 complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment
    • 1 complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment. Structure 8:669-84
    • (2000) Structure , vol.8 , pp. 669-684
    • Hunte, C.1    Koepke, J.2    Lange, C.3    Rossmanith, T.4    Michel, H.5
  • 44
    • 0036786230 scopus 로고    scopus 로고
    • 1 in complex with famoxadone: The role of aromatic-aromatic interaction in inhibition
    • 1 in complex with famoxadone: the role of aromatic-aromatic interaction in inhibition. Biochemistry 41:11692-702
    • (2002) Biochemistry , vol.41 , pp. 11692-11702
    • Gao, X.1    Wen, X.2    Yu, C.-A.3    Esser, L.4    Tsao, S.5
  • 49
    • 0017148721 scopus 로고
    • Possible molecular mechanisms of the protonmotive function of cytochrome systems
    • Mitchell P. 1976. Possible molecular mechanisms of the protonmotive function of cytochrome systems. J. Theor. Biol. 62:121-61
    • (1976) J. Theor. Biol. , vol.62 , pp. 121-161
    • Mitchell, P.1
  • 50
    • 0001104663 scopus 로고
    • The role of the quinone pool in the cyclic electron-transfer chain of Rhodopseudomonas sphaeroides: A modified Q-cycle mechanism
    • Crofts AR, Meinhardt SW, Jones KR, Snozzi M. 1983. The role of the quinone pool in the cyclic electron-transfer chain of Rhodopseudomonas sphaeroides: a modified Q-cycle mechanism. Biochim. Biophys. Acta 723:202-18
    • (1983) Biochim. Biophys. Acta , vol.723 , pp. 202-218
    • Crofts, A.R.1    Meinhardt, S.W.2    Jones, K.R.3    Snozzi, M.4
  • 51
    • 0000026361 scopus 로고
    • The mechanism of ubiquinol: Cytochrome c oxidoreductases of mitochondria and of Rhodopseudomonas sphaeroides
    • ed. AN Martonosi, New York: Plenum
    • Crofts AR. 1985. The mechanism of ubiquinol: cytochrome c oxidoreductases of mitochondria and of Rhodopseudomonas sphaeroides. In The Enzymes of Biological Membranes, ed. AN Martonosi, 4:347-82. New York: Plenum
    • (1985) The Enzymes of Biological Membranes , vol.4 , pp. 347-382
    • Crofts, A.R.1
  • 53
    • 1942507631 scopus 로고    scopus 로고
    • The Q-cycle - A personal perspective
    • The Millenium Issues on the History of Photosynthesis. ed. Govindjee. In press
    • Crofts AR. 2003. The Q-cycle - a personal perspective. In The Millenium Issues on the History of Photosynthesis. Photosynth. Res. ed. Govindjee. In press
    • (2003) Photosynth. Res.
    • Crofts, A.R.1
  • 55
    • 0003159212 scopus 로고
    • Electron transfer reactions between quinols and quinones in aqueous and aprotic media
    • Rich PR. 1981. Electron transfer reactions between quinols and quinones in aqueous and aprotic media. Biochim. Biophys. Acta 637:28-33
    • (1981) Biochim. Biophys. Acta , vol.637 , pp. 28-33
    • Rich, P.R.1
  • 57
    • 48749143707 scopus 로고
    • The electrochemical domain of photosynthesis
    • Crofts AR, Wraight CA. 1983. The electrochemical domain of photosynthesis. Biochim. Biophys. Acta 726:149-86
    • (1983) Biochim. Biophys. Acta , vol.726 , pp. 149-186
    • Crofts, A.R.1    Wraight, C.A.2
  • 58
    • 84912437779 scopus 로고
    • Proton-translocating nitrate reductase of Escherichia coli
    • ed. E Quagliariello, S Papa, F Palmieri, EC Slater, N Siliprandi, Amsterdam: North-Holland
    • Garland PB, Clegg RA, Boxer D, Downie JA, Haddock BA. 1975. Proton-translocating nitrate reductase of Escherichia coli. In Electron Transfer Chains and Oxidative Phosphorylation, ed. E Quagliariello, S Papa, F Palmieri, EC Slater, N Siliprandi, pp. 351-58. Amsterdam: North-Holland
    • (1975) Electron Transfer Chains and Oxidative Phosphorylation , pp. 351-358
    • Garland, P.B.1    Clegg, R.A.2    Boxer, D.3    Downie, J.A.4    Haddock, B.A.5
  • 64
    • 0016690480 scopus 로고
    • 1 complex in the respiratory chain: Proton motive ubiquinone cycle
    • 1 complex in the respiratory chain: proton motive ubiquinone cycle. FEBS Lett. 56:1-6
    • (1975) FEBS Lett. , vol.56 , pp. 1-6
    • Mitchell, P.1
  • 75
    • 0020567816 scopus 로고
    • Inhibition of electron transfer by 3-alkyl-2-hydroxy-1,4-naphthoquinones in the ubiquinol-cytochrome c oxidoreductases of Rhodopseudomonas sphaeroides and mammalian mitochondria. Interaction with a ubiquinone-binding site and the Rieske iron-sulfur cluster
    • Matsuura K, Bowyer JR, Ohnishi T, Dutton PL. 1983. Inhibition of electron transfer by 3-alkyl-2-hydroxy-1,4-naphthoquinones in the ubiquinol-cytochrome c oxidoreductases of Rhodopseudomonas sphaeroides and mammalian mitochondria. Interaction with a ubiquinone-binding site and the Rieske iron-sulfur cluster. J. Biol. Chem. 258:1571-77
    • (1983) J. Biol. Chem. , vol.258 , pp. 1571-1577
    • Matsuura, K.1    Bowyer, J.R.2    Ohnishi, T.3    Dutton, P.L.4
  • 76
    • 0002450347 scopus 로고    scopus 로고
    • Malarone treatment failure and in vitro confirmation of resistance of Plasmodium falciparum isolate from Lagos, Nigeria
    • Fivelman QL, Butcher GA, Adagu IS, Warhurst DC, Pasvol G. 2002. Malarone treatment failure and in vitro confirmation of resistance of Plasmodium falciparum isolate from Lagos, Nigeria. Malar. J. 1:1-4
    • (2002) Malar. J. , vol.1 , pp. 1-4
    • Fivelman, Q.L.1    Butcher, G.A.2    Adagu, I.S.3    Warhurst, D.C.4    Pasvol, G.5
  • 77
    • 0017594519 scopus 로고
    • Binding of HQNO to beef-heart sub-mitochondrial particles
    • Van Ark G, Berden JA. 1977. Binding of HQNO to beef-heart sub-mitochondrial particles. Biochim. Biophys. Acta 459:119-27
    • (1977) Biochim. Biophys. Acta , vol.459 , pp. 119-127
    • Van Ark, G.1    Berden, J.A.2
  • 82
    • 0034984506 scopus 로고    scopus 로고
    • Structures and proton-pumping strategies of mitochondrial respiratory enzymes
    • Schultz BE, Chan SI. 2001. Structures and proton-pumping strategies of mitochondrial respiratory enzymes. Annu. Rev. Biophys. Biomol. Struct. 30:23-65
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 23-65
    • Schultz, B.E.1    Chan, S.I.2
  • 84
    • 0030861648 scopus 로고    scopus 로고
    • 1 complex: The "proton-gated affinity change" mechanism
    • 1 complex: the "proton-gated affinity change" mechanism. FEBS Lett. 412:257-64
    • (1997) FEBS Lett. , vol.412 , pp. 257-264
    • Link, T.A.1
  • 88
  • 95
    • 0032321683 scopus 로고    scopus 로고
    • 1 complexes containing site-directed mutants of the Rieske iron-sulfur protein
    • 1 complexes containing site-directed mutants of the Rieske iron-sulfur protein. Biochim. Biophys. Acta 1365:125-34
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 125-134
    • Snyder, C.1    Trumpower, B.L.2
  • 101
    • 0028808109 scopus 로고
    • 1 complex by blocking a protonatable group
    • 1 complex by blocking a protonatable group. J. Biol. Chem. 270:25001-6
    • (1995) J. Biol. Chem. , vol.270 , pp. 25001-25006
    • Link, T.A.1    Von Jagow, G.2
  • 102
    • 0030963762 scopus 로고    scopus 로고
    • Role of deprotonation events in ubihydroquinone: Cytochrome c oxidoreductase from bovine heart and yeast mitochondria
    • Brandt U, Okun JG. 1997. Role of deprotonation events in ubihydroquinone: cytochrome c oxidoreductase from bovine heart and yeast mitochondria. Biochemistry 36:11234-40
    • (1997) Biochemistry , vol.36 , pp. 11234-11240
    • Brandt, U.1    Okun, J.G.2
  • 104
    • 0442331120 scopus 로고    scopus 로고
    • The structures of Rieske and Rieske-type proteins
    • Link TA. 1999. The structures of Rieske and Rieske-type proteins. Adv. Inorg. Chem. 47:83-157
    • (1999) Adv. Inorg. Chem. , vol.47 , pp. 83-157
    • Link, T.A.1
  • 105
    • 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 MM-J, Eltis LD, Bolin JT. 2000. A cluster exposed: structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins. Structure 8:1267-78
    • (2000) Structure , vol.8 , pp. 1267-1278
    • Colbert, C.1    Couture, M.M.-J.2    Eltis, L.D.3    Bolin, J.T.4
  • 107
    • 0142063412 scopus 로고    scopus 로고
    • The reduction potentials of Rieske clusters: The importance of the coupling between oxidation state and histidine protonation state
    • In press
    • Zu Y, Manon M-J, Couture MM-J, Kolling DRJ, Crofts AR, et al. 2003. The reduction potentials of Rieske clusters: the importance of the coupling between oxidation state and histidine protonation state. Biochemistry. In press
    • (2003) Biochemistry
    • Zu, Y.1    Manon, M.-J.2    Couture, M.M.-J.3    Kolling, D.R.J.4    Crofts, A.R.5
  • 108
    • 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. 504:126-32
    • (2001) FEBS Lett. , vol.504 , pp. 126-132
    • Hunte, C.1
  • 114
    • 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. 277:48449-55
    • (2002) J. Biol. Chem. , vol.277 , pp. 48449-48455
    • Covián, R.1    Pardo, J.P.2    Moreno-Sánchez, R.3
  • 120
    • 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 OM, Snyder CH, Link TA, Trumpower BL. 1998. 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. 273:9085-93
    • (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
  • 123
    • 0025913125 scopus 로고
    • 1 complex from Rb. sphaeroides by site-directed mutagenesis
    • 1 complex from Rb. sphaeroides by site-directed mutagenesis. Biochemistry 30:6747-54
    • (1991) Biochemistry , vol.30 , pp. 6747-6754
    • Yun, C.-H.1    Crofts, A.R.2    Gennis, R.B.3
  • 124
  • 127
    • 0029806796 scopus 로고    scopus 로고
    • Unraveling the kinetic complexity of inter-protein electron transfer reactions
    • Davidson VL. 1996. Unraveling the kinetic complexity of inter-protein electron transfer reactions. Biochemistry 35:14036-39
    • (1996) Biochemistry , vol.35 , pp. 14036-14039
    • Davidson, V.L.1
  • 129
    • 0002478857 scopus 로고    scopus 로고
    • Electron transfer within ruthenium(II) polypyridyl-(salt bridge)-dimethylaniline acceptor-donor complexes
    • Roberts JA, Kirby JP, Wall ST, Nocera DG. 1997. Electron transfer within ruthenium(II) polypyridyl-(salt bridge)-dimethylaniline acceptor-donor complexes. Inorgr. Chim. Acta 263:395-405
    • (1997) Inorgr. Chim. Acta , vol.263 , pp. 395-405
    • Roberts, J.A.1    Kirby, J.P.2    Wall, S.T.3    Nocera, D.G.4
  • 131
    • 0033621050 scopus 로고    scopus 로고
    • Observation of the protonated SQ intermediate in isolated reaction centers from Rhodobacter sphaeroides: Implications for the mechanism of electron and proton transfer in proteins
    • Graige MS, Paddock ML, Feher G, Okamura MY. 1999. Observation of the protonated SQ intermediate in isolated reaction centers from Rhodobacter sphaeroides: implications for the mechanism of electron and proton transfer in proteins. Biochemistry 38:11465-73
    • (1999) Biochemistry , vol.38 , pp. 11465-11473
    • Graige, M.S.1    Paddock, M.L.2    Feher, G.3    Okamura, M.Y.4
  • 132
    • 0032823542 scopus 로고    scopus 로고
    • Application of Marcus Rate Theory to proton transfer in enzyme catalyzed reactions
    • Kresge AJ, Silverman DN. 1999. Application of Marcus Rate Theory to proton transfer in enzyme catalyzed reactions. Methods Enzymol. 308:276-97
    • (1999) Methods Enzymol. , vol.308 , pp. 276-297
    • Kresge, A.J.1    Silverman, D.N.2
  • 133
    • 0031587575 scopus 로고    scopus 로고
    • Direct measurement of intrinsic proton transfer rates in diffusion controlled reactions
    • Pines E, Magnes B-Z, Lang MJ, Fleming GR. 1997. Direct measurement of intrinsic proton transfer rates in diffusion controlled reactions. Chem. Phys. Lett. 281:413-20
    • (1997) Chem. Phys. Lett. , vol.281 , pp. 413-420
    • Pines, E.1    Magnes, B.-Z.2    Lang, M.J.3    Fleming, G.R.4
  • 134
    • 18144424145 scopus 로고    scopus 로고
    • 1 complex controls the rate of ubihydroquinone oxidation
    • In press
    • 1 complex controls the rate of ubihydroquinone oxidation. Biochim. Biophys. Acta. In press
    • (2003) Biochim. Biophys. Acta
    • Crofts, A.R.1
  • 135
    • 0022004980 scopus 로고
    • Electron transfers in chemistry and biology
    • Marcus RA, Sutin N. 1985. Electron transfers in chemistry and biology. Biochim. Biophys. Acta 811:265-322
    • (1985) Biochim. Biophys. Acta , vol.811 , pp. 265-322
    • Marcus, R.A.1    Sutin, N.2
  • 136
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page CC, Moser CC, Chen XX, Dutton PL. 1999. Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature 402:47-52
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.X.3    Dutton, P.L.4
  • 137
    • 0019084947 scopus 로고
    • Quantum-mechanical tunnelling in biological systems
    • DeVault D. 1980. Quantum-mechanical tunnelling in biological systems. Q. Rev. Biophys. 13:387-564
    • (1980) Q. Rev. Biophys. , vol.13 , pp. 387-564
    • DeVault, D.1
  • 138
    • 0034624079 scopus 로고    scopus 로고
    • 1 complex by the formation of an inter-subunit disulfide bond between cytochrome b and the iron-sulfur protein
    • 1 complex by the formation of an inter-subunit disulfide bond between cytochrome b and the iron-sulfur protein. J. Biol. Chem. 275:38597-604
    • (2000) J. Biol. Chem. , vol.275 , pp. 38597-38604
    • Xiao, K.1    Yu, L.2    Yu, C.-A.3
  • 145
    • 0011187433 scopus 로고
    • The cytochrome b paradox, the BAL-labile factor and the Q-cycle
    • ed. VP Skulachev, PV Hinkle, Reading, MA: Addison-Wesley
    • Slater EC. 1981. The cytochrome b paradox, the BAL-labile factor and the Q-cycle. In Chemiosmotic Proton Circuits in Biological Membranes, ed. VP Skulachev, PV Hinkle, pp. 69-104. Reading, MA: Addison-Wesley
    • (1981) Chemiosmotic Proton Circuits in Biological Membranes , pp. 69-104
    • Slater, E.C.1
  • 149
    • 0032830370 scopus 로고    scopus 로고
    • Structures of quinone-binding sites in bc complexes: Functional implications
    • Berry EA, Zhang Z, Huang L-S, Kim SH. 1999. Structures of quinone-binding sites in bc complexes: functional implications. Biochem. Soc. Trans. 27:565-72
    • (1999) Biochem. Soc. Trans. , vol.27 , pp. 565-572
    • Berry, E.A.1    Zhang, Z.2    Huang, L.-S.3    Kim, S.H.4
  • 154
    • 0018971809 scopus 로고
    • Differential effects of antimycin on ubisemiquinone bound in different environments in isolated succinate cytochrome c reductase complex
    • Ohnishi T, Trumpower BL. 1980. Differential effects of antimycin on ubisemiquinone bound in different environments in isolated succinate cytochrome c reductase complex. J. Biol. Chem. 255:3278-84
    • (1980) J. Biol. Chem. , vol.255 , pp. 3278-3284
    • Ohnishi, T.1    Trumpower, B.L.2
  • 157
    • 0025335671 scopus 로고
    • Electron nuclear double resonance (ENDOR) of the Q-c.-ubiSQ radical in the mitochondrial electron transport chain
    • Salerno JC, Osgood M, Liu Y, Taylor H, Scholes CP. 1990. Electron nuclear double resonance (ENDOR) of the Q-c.-ubiSQ radical in the mitochondrial electron transport chain. Biochemistry 29:6987-93
    • (1990) Biochemistry , vol.29 , pp. 6987-6993
    • Salerno, J.C.1    Osgood, M.2    Liu, Y.3    Taylor, H.4    Scholes, C.P.5
  • 159
    • 0028004485 scopus 로고
    • 1 complex of Rhodobacter sphaeroides: Two highly conserved residues predicted to be near the cytoplasmic surface of putative transmembrane helices B and C
    • 1 complex of Rhodobacter sphaeroides: two highly conserved residues predicted to be near the cytoplasmic surface of putative transmembrane helices B and C. Biochemistry 33:13022-31
    • (1994) Biochemistry , vol.33 , pp. 13022-13031
    • Hacker, B.1    Barquera, B.2    Gennis, R.B.3    Crofts, A.R.4
  • 162
    • 0024971005 scopus 로고
    • The pathway of the quinol/quinone transhydrogenation reaction in ubiquinol: Cytochrome-c reductase of Neurospora mitochondria
    • Zweck A, Bechmann G, Weiss H. 1989. The pathway of the quinol/quinone transhydrogenation reaction in ubiquinol: cytochrome-c reductase of Neurospora mitochondria. Eur. J. Biochem. 183:199-203
    • (1989) Eur. J. Biochem. , vol.183 , pp. 199-203
    • Zweck, A.1    Bechmann, G.2    Weiss, H.3
  • 163
    • 0025780587 scopus 로고
    • The interactions of duroquinol, DBMIB and NQNO with the chloroplast cytochrome bf complex
    • Rich PR, Madgwick SA, Moss DA. 1991. The interactions of duroquinol, DBMIB and NQNO with the chloroplast cytochrome bf complex. Biochim. Biophys. Acta 1058:312-28
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 312-328
    • Rich, P.R.1    Madgwick, S.A.2    Moss, D.A.3
  • 164
    • 0018115502 scopus 로고
    • Redox potentiometry in biological systems
    • Dutton PL, Wilson DM. 1976. Redox potentiometry in biological systems. Methods Enzymol. 54:411-35
    • (1976) Methods Enzymol. , vol.54 , pp. 411-435
    • Dutton, P.L.1    Wilson, D.M.2
  • 167
    • 0015497373 scopus 로고
    • Thermodynamic and kinetics characterization of electron-transfer components in situ in Rps. spheroides and Rhodospirillum rubrum
    • Dutton PL, Jackson JB. 1972. Thermodynamic and kinetics characterization of electron-transfer components in situ in Rps. spheroides and Rhodospirillum rubrum. Eur. J. Biochem. 30:495-510
    • (1972) Eur. J. Biochem. , vol.30 , pp. 495-510
    • Dutton, P.L.1    Jackson, J.B.2
  • 168
    • 0007715338 scopus 로고
    • A new effect of antimycin on the b-cytochromes of Rps. sphaeroides
    • ed. C Sybesma, The Hague: Nijhoff/Junk
    • Meinhardt SW, Crofts AR. 1984. A new effect of antimycin on the b-cytochromes of Rps. sphaeroides. In Advances in Photosynthesis Research, ed. C Sybesma, 1:649-52. The Hague: Nijhoff/Junk
    • (1984) Advances in Photosynthesis Research , vol.1 , pp. 649-652
    • Meinhardt, S.W.1    Crofts, A.R.2
  • 171
    • 0026674915 scopus 로고
    • Non-linear inhibition curves for tight-binding inhibitors of dimeric ubiquinol-cytochrome c oxidoreductases. Evidence for rapid inhibitor mobility
    • Bechmann G, Weiss H, Rich PR. 1992. Non-linear inhibition curves for tight-binding inhibitors of dimeric ubiquinol-cytochrome c oxidoreductases. Evidence for rapid inhibitor mobility. Eur. J. Biochem. 208(2):315-25
    • (1992) Eur. J. Biochem. , vol.208 , Issue.2 , pp. 315-325
    • Bechmann, G.1    Weiss, H.2    Rich, P.R.3
  • 172
    • 0019316012 scopus 로고
    • The kinetics and thermodynamics of the reduction of cytochrome c by substituted p-benzoquinols in solution
    • Rich PR, Bendall DS. 1980. The kinetics and thermodynamics of the reduction of cytochrome c by substituted p-benzoquinols in solution. Biochim. Biophys. Acta 592:506-18
    • (1980) Biochim. Biophys. Acta , vol.592 , pp. 506-518
    • Rich, P.R.1    Bendall, D.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.