메뉴 건너뛰기




Volumn 427, Issue 6975, 2004, Pages 607-612

Reversible redox energy coupling in electron transfer chains

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CATALYSIS; ELECTRON TRANSITIONS; ELECTRON TUNNELING; ION EXCHANGE; ORGANIC COMPOUNDS; PHOTOSYNTHESIS; REDOX REACTIONS;

EID: 1342325555     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature02242     Document Type: Article
Times cited : (232)

References (49)
  • 1
    • 78651141624 scopus 로고
    • The interaction of energy and electron transfer reactions in mitochondria
    • Chance, B. & Hollunger, G. The interaction of energy and electron transfer reactions in mitochondria. J. Biol. Chem. 236, 1562-1568 (1961).
    • (1961) J. Biol. Chem. , vol.236 , pp. 1562-1568
    • Chance, B.1    Hollunger, G.2
  • 2
    • 0028089328 scopus 로고
    • 1 complex reconstituted into potassium-loaded phospholipid vesicles
    • 1 complex reconstituted into potassium-loaded phospholipid vesicles. J. Biol. Chem. 269, 1827-1833 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 1827-1833
    • Miki, T.1    Miki, M.2    Orii, Y.3
  • 3
    • 0034123440 scopus 로고    scopus 로고
    • 1 and NADH-Q oxidoreductase complexes of the acidophilic obligate chemolithotrophic ferrous ion-oxidizing bacterium Thiobacillus ferrooxidans
    • 1 and NADH-Q oxidoreductase complexes of the acidophilic obligate chemolithotrophic ferrous ion-oxidizing bacterium Thiobacillus ferrooxidans. J. Bacteriol. 182, 3602-3606 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 3602-3606
    • Elbehti, A.1    Brasseur, G.2    Lemesle-Meunier, D.3
  • 5
    • 0030861648 scopus 로고    scopus 로고
    • 1 complex. The 'proton-gated affinity change' mechanism
    • 1 complex. The 'proton-gated affinity change' mechanism. FEBS Lett. 412, 257-264 (1997).
    • (1997) FEBS Lett. , vol.412 , pp. 257-264
    • Link, T.A.1
  • 7
    • 0030001519 scopus 로고    scopus 로고
    • 1 complex by proton-gated charge transfer
    • 1 complex by proton-gated charge transfer. FEBS Lett. 387, 1-6 (1996).
    • (1996) FEBS Lett. , vol.387 , pp. 1-6
    • Brandt, U.1
  • 9
    • 0028971417 scopus 로고
    • 1 complex
    • 1 complex, Biochemistry 34, 15979-15996 (1995).
    • (1995) Biochemistry , vol.34 , pp. 15979-15996
    • Ding, H.1
  • 11
    • 0033619678 scopus 로고    scopus 로고
    • 1 complex: Different domains of the quinol binding pocket and their role in the mechanism and binding of inhibitors
    • 1 complex: different domains of the quinol binding pocket and their role in the mechanism and binding of inhibitors, Biochemistry 38, 15807-15826 (1999).
    • (1999) Biochemistry , vol.38 , pp. 15807-15826
    • Crofts, A.R.1
  • 18
    • 0034624079 scopus 로고    scopus 로고
    • 1 complex by the formation of an intersubunit disulfide bond between cytochrome b and the iron-sulfur protein
    • 1 complex by the formation of an intersubunit disulfide bond between cytochrome b and the iron-sulfur protein. J. Biol. Chem. 275, 38597-38604 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 38597-38604
    • Xiao, K.1    Yu, L.2    Yu, C.A.3
  • 22
    • 0025913125 scopus 로고
    • 1 complex from Rhodobacter sphaeroides by site-directed mutagenesis
    • 1 complex from Rhodobacter sphaeroides by site-directed mutagenesis. Biochemistry 30, 6747-6754 (1991).
    • (1991) Biochemistry , vol.30 , pp. 6747-6754
    • Yun, C.-H.1    Crofts, A.R.2    Gennis, R.B.3
  • 23
    • 0016754421 scopus 로고
    • The protonmotive Q cycle: A general formulation
    • Mitchell, P. The protonmotive Q cycle: a general formulation. FEBS Lett. 59, 137-139 (1975).
    • (1975) FEBS Lett. , vol.59 , pp. 137-139
    • Mitchell, P.1
  • 24
    • 0017148721 scopus 로고
    • Possible molecular mechanisms of the proton motive function of cytochrome systems
    • Mitchell, P. Possible molecular mechanisms of the proton motive function of cytochrome systems. J. Theor. Biol. 62, 327-367 (1976).
    • (1976) J. Theor. Biol. , vol.62 , pp. 327-367
    • Mitchell, P.1
  • 25
    • 0030867866 scopus 로고    scopus 로고
    • 1 complex from bovine heart mitochondria
    • 1 complex from bovine heart mitochondria. Science 277, 60-66 (1997).
    • (1997) Science , vol.277 , pp. 60-66
    • Xia, D.1
  • 26
    • 0032479524 scopus 로고    scopus 로고
    • 1 complex
    • 1 complex. Science 281, 64-71 (1998).
    • (1998) Science , vol.281 , pp. 64-71
    • Iwata, S.1
  • 27
    • 0032537117 scopus 로고    scopus 로고
    • 1
    • 1. Nature 392, 677-684 (1998).
    • (1998) Nature , vol.392 , pp. 677-684
    • Zhang, Z.1
  • 28
    • 0034660152 scopus 로고    scopus 로고
    • 1 complex from the yeast Saccharomyces cerevisiae co-crystalized with an antibody F, fragment
    • 1 complex from the yeast Saccharomyces cerevisiae co-crystalized with an antibody F, fragment. Structure 8, 669-684 (2000).
    • (2000) Structure , vol.8 , pp. 669-684
    • Hunte, C.1    Koepke, J.2    Lange, C.3    Roßmanith, T.4    Michel, H.5
  • 29
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page, C. C., Moser, C. C. & Dutton, P. L. Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature 402, 47-52 (1999).
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Dutton, P.L.3
  • 30
    • 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. & 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, 202-218 (1983).
    • (1983) Biochim. Biophys. Acta , vol.723 , pp. 202-218
    • Crofts, A.R.1    Meinhardt, S.W.2    Jones, K.R.3    Snozzi, M.4
  • 31
    • 0015526672 scopus 로고
    • The allosteric binding of antimycin to cytochrome b in the mitochondrial membrane
    • Berden, J. A. & Slater, E. C. The allosteric binding of antimycin to cytochrome b in the mitochondrial membrane. Biochim. Biophys. Acta 256, 199-215 (1971).
    • (1971) Biochim. Biophys. Acta , vol.256 , pp. 199-215
    • Berden, J.A.1    Slater, E.C.2
  • 33
    • 0032493297 scopus 로고    scopus 로고
    • 1 complex from bovine heart
    • 1 complex from bovine heart. Proc. Natl Acad. Sci. USA 95, 8026-8033 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 8026-8033
    • Kim, H.1
  • 34
  • 35
    • 0037022594 scopus 로고    scopus 로고
    • 1 complex with its bound substratz cytochrome c
    • 1 complex with its bound substratz cytochrome c. Proc. Natl Acad. Sci. USA 99, 2800-2805 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 2800-2805
    • Lange, C.1    Hunte, C.2
  • 38
    • 0032830370 scopus 로고    scopus 로고
    • Structure of quinone-binding sites in be complexes: Functional implications
    • Berry, E. A., Zhang, Z., Huang, L.-S. & Kim, S.-H. Structure of quinone-binding sites in be complexes: functional implications. Biochem. Soc. Trans. 27, 565-572 (1999).
    • (1999) Biochem. Soc. Trans. , vol.27 , pp. 565-572
    • Berry, E.A.1    Zhang, Z.2    Huang, L.-S.3    Kim, S.-H.4
  • 39
    • 0037031511 scopus 로고    scopus 로고
    • Simultaneous two-electron transfer in electrode kinetics
    • Gileadi, E. Simultaneous two-electron transfer in electrode kinetics. J. Electroanal. Chem. 532, 181-189 (2002).
    • (2002) J. Electroanal. Chem. , vol.532 , pp. 181-189
    • Gileadi, E.1
  • 40
    • 0033599369 scopus 로고    scopus 로고
    • Kinetics of bond shift and charge transfer in dialkynylphenylene-bridged dicyclooctatetraenes and their dianions
    • Boman, P. et al. Kinetics of bond shift and charge transfer in dialkynylphenylene-bridged dicyclooctatetraenes and their dianions. J. Am. Chem. Soc. 121, 1558-1564 (1999).
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 1558-1564
    • Boman, P.1
  • 41
    • 0042331013 scopus 로고    scopus 로고
    • Concerted two-electron-transfer processes in mixed-valence species with square topology
    • Lambert, C. Concerted two-electron-transfer processes in mixed-valence species with square topology. Chemphyschem 4, 877-880 (2003).
    • (2003) Chemphyschem , vol.4 , pp. 877-880
    • Lambert, C.1
  • 42
    • 0027385123 scopus 로고
    • The concerted reduction of the high- and low-potential chains of the bf complex by plastoquinol
    • Kramer, D. M. & Crofts, A. R. The concerted reduction of the high- and low-potential chains of the bf complex by plastoquinol. Biochim. Biophys. Acta 1183, 72-84 (1993).
    • (1993) Biochim. Biophys. Acta , vol.1183 , pp. 72-84
    • Kramer, D.M.1    Crofts, A.R.2
  • 43
    • 0020353465 scopus 로고
    • Electron and proton transfers in chemical and biological quinone systems
    • Rich, P. R. Electron and proton transfers in chemical and biological quinone systems. Discuss. Faraday Soc. 74, 349-364 (1982).
    • (1982) Discuss. Faraday Soc. , vol.74 , pp. 349-364
    • Rich, P.R.1
  • 44
    • 0033550541 scopus 로고    scopus 로고
    • Control of one-versus two-electron reduction of ubiquinone via redox-dependent recognition
    • Greaves, M. D., Niemz, A. & Rotello, V. M. Control of one-versus two-electron reduction of ubiquinone via redox-dependent recognition. J. Am. Chem. Soc. 121, 266-267 (1999).
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 266-267
    • Greaves, M.D.1    Niemz, A.2    Rotello, V.M.3
  • 45
    • 0008843559 scopus 로고    scopus 로고
    • Three-state model for two-electron transfer reactions
    • Zusman, L. D. & Beratan, D. N. Three-state model for two-electron transfer reactions. J. Phys. Chem. A 101, 4136-4141 (1997).
    • (1997) J. Phys. Chem. A , vol.101 , pp. 4136-4141
    • Zusman, L.D.1    Beratan, D.N.2
  • 46
    • 0037160091 scopus 로고    scopus 로고
    • Topology of superoxide production from different sites in the mitochondrial electron transport chain
    • St-Pierre, J., Buckingham, J. A., Roebuck, S. J. & Brand, M. D. Topology of superoxide production from different sites in the mitochondrial electron transport chain. J. Biol. Chem. 277, 44784-44790 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 44784-44790
    • St-Pierre, J.1    Buckingham, J.A.2    Roebuck, S.J.3    Brand, M.D.4
  • 48
    • 0035807846 scopus 로고    scopus 로고
    • 1 complex through disulfide anchoring of a loop and a β-branched amino acid near the heme-ligating methionine
    • 1 complex through disulfide anchoring of a loop and a β-branched amino acid near the heme-ligating methionine. Biochemistry 40, 14547-14556 (2001).
    • (2001) Biochemistry , vol.40 , pp. 14547-14556
    • Osyczka, A.1    Dutton, P.L.2    Moser, C.C.3    Darrouzet, E.4    Daldal, F.5
  • 49
    • 0022599392 scopus 로고
    • 2 oxidoreductase of Rhodopseudomonas capsulata
    • 2 oxidoreductase of Rhodopseudomonas capsulata. J. Biol. Chem. 261, 584-591 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 584-591
    • Robertson, D.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.