메뉴 건너뛰기




Volumn 174, Issue 1-2, 1997, Pages 131-135

Regulation of respiration and energy transduction in cytochrome c oxidase isozymes by allosteric effecters

Author keywords

ATP derivative; Cytochrome c oxidase; Energy transduction; H+ e stoichiometry; Nucleotide binding sites; Proton translocation

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE DERIVATIVE; CYTOCHROME C OXIDASE; HEART ENZYME; ISOENZYME; LIVER ENZYME; TRINITROPHENYL;

EID: 0030809573     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006819416358     Document Type: Article
Times cited : (18)

References (25)
  • 1
    • 0018789705 scopus 로고
    • Non-equilibrium thermodynamics of energy conversion in bioenergetics
    • Rottenberg H: Non-equilibrium thermodynamics of energy conversion in bioenergetics. Biochim Biophys Acta 549: 225-253, 1979
    • (1979) Biochim Biophys Acta , vol.549 , pp. 225-253
    • Rottenberg, H.1
  • 2
    • 0024422115 scopus 로고
    • Slip and leak in mitochondrial oxidative phosphorylation
    • Murphy MP: Slip and leak in mitochondrial oxidative phosphorylation. Biochim Biophys Acta 977: 123-141, 1989
    • (1989) Biochim Biophys Acta , vol.977 , pp. 123-141
    • Murphy, M.P.1
  • 3
    • 0021759406 scopus 로고
    • Non-ohmic proton conductance of mitochondria and liposomes
    • Krishnamoorthy G, Hinkle PC: Non-ohmic proton conductance of mitochondria and liposomes. Biochemistry 23: 1640-1645, 1984
    • (1984) Biochemistry , vol.23 , pp. 1640-1645
    • Krishnamoorthy, G.1    Hinkle, P.C.2
  • 4
    • 0021426610 scopus 로고
    • The current-voltage relationships in liposomes and mitochondria
    • O'Shea PS, Petrone G, Casey RP, Azzi A: The current-voltage relationships in liposomes and mitochondria. Biochem J 219: 719-726, 1984
    • (1984) Biochem J , vol.219 , pp. 719-726
    • O'Shea, P.S.1    Petrone, G.2    Casey, R.P.3    Azzi, A.4
  • 5
    • 0024417971 scopus 로고
    • The relative proton stoichiometries of the mitochondrial proton pumps are independent of the proton motive force
    • Brown GC: The relative proton stoichiometries of the mitochondrial proton pumps are independent of the proton motive force. J Biol Chem 264: 14704-14709, 1989
    • (1989) J Biol Chem , vol.264 , pp. 14704-14709
    • Brown, G.C.1
  • 7
    • 0024276114 scopus 로고
    • Membrane-potential-dependent changes in the stoichiometry of charge translocation by the mitochondrial electron transport chain
    • Murphy MP, Brand MD: Membrane-potential-dependent changes in the stoichiometry of charge translocation by the mitochondrial electron transport chain. Eur J Biochem 173: 637-644, 1988
    • (1988) Eur J Biochem , vol.173 , pp. 637-644
    • Murphy, M.P.1    Brand, M.D.2
  • 8
    • 0024276134 scopus 로고
    • 1 complex of mitochondria at high membrane potential
    • 1 complex of mitochondria at high membrane potential. Eur J Biochem 173: 645-651, 1988
    • (1988) Eur J Biochem , vol.173 , pp. 645-651
    • Murphy, M.P.1    Brand, M.D.2
  • 10
    • 0023321462 scopus 로고
    • On the role of subunit III in proton translocation in cytochrome c oxidase
    • Prochaska LJ, Fink PS: On the role of subunit III in proton translocation in cytochrome c oxidase. J Bioenerg Biomembr 19: 143-166, 1987
    • (1987) J Bioenerg Biomembr , vol.19 , pp. 143-166
    • Prochaska, L.J.1    Fink, P.S.2
  • 11
    • 0025858290 scopus 로고
    • Influence of N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinolin modification on proton translocation and membrane potential of reconstituted cytochrome c oxidase support 'proton slippage'
    • Steverding D, Kadenbach B : Influence of N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinolin modification on proton translocation and membrane potential of reconstituted cytochrome c oxidase support 'proton slippage'. J Biol Chem 266: 8097-8101, 1991
    • (1991) J Biol Chem , vol.266 , pp. 8097-8101
    • Steverding, D.1    Kadenbach, B.2
  • 12
    • 0027481132 scopus 로고
    • Proton slippage in cytochrome c oxidase of Paracoccus denitrificans. Membrane potential measurements with the two-and three-subunit enzyme
    • Steverding D, Köhnke D, Ludwig B, Kadenbach B: Proton slippage in cytochrome c oxidase of Paracoccus denitrificans. Membrane potential measurements with the two-and three-subunit enzyme. Eur J Biochem 212: 827-831, 1993
    • (1993) Eur J Biochem , vol.212 , pp. 827-831
    • Steverding, D.1    Köhnke, D.2    Ludwig, B.3    Kadenbach, B.4
  • 14
    • 0027166168 scopus 로고
    • Tissue-specific regulation of cytochrome c oxidase efficiency by nucleotides
    • Rohdich F, Kadenbach B : Tissue-specific regulation of cytochrome c oxidase efficiency by nucleotides. Biochemistry 32: 8499-8503, 1993
    • (1993) Biochemistry , vol.32 , pp. 8499-8503
    • Rohdich, F.1    Kadenbach, B.2
  • 16
    • 0022821996 scopus 로고
    • Cytochrome c oxidase from Paracoccus denitrificans
    • Ludwig B : Cytochrome c oxidase from Paracoccus denitrificans. Meth Enzymol 126: 153-159, 1986
    • (1986) Meth Enzymol , vol.126 , pp. 153-159
    • Ludwig, B.1
  • 17
    • 0029557464 scopus 로고
    • On the number of nucleotide binding sites in cytochrome c oxidase
    • Rieger T, Napiwotzki J, Kadenbach B : On the number of nucleotide binding sites in cytochrome c oxidase. Biochem Biophys Res Commun 217: 34-40, 1995
    • (1995) Biochem Biophys Res Commun , vol.217 , pp. 34-40
    • Rieger, T.1    Napiwotzki, J.2    Kadenbach, B.3
  • 18
    • 0029670481 scopus 로고    scopus 로고
    • --stoichiometry of cytochrome c oxidase from bovine heart by intramitochondrial ATP/ADP ratios
    • --stoichiometry of cytochrome c oxidase from bovine heart by intramitochondrial ATP/ADP ratios. FEBS Lett 382: 121-124, 1996
    • (1996) FEBS Lett , vol.382 , pp. 121-124
    • Frank, V.1    Kadenbach, B.2
  • 19
    • 0027406438 scopus 로고
    • Tissue-specific regulation of bovine heart cytochrome c oxidase by ADP via interaction with subunit Via
    • Anthony G, Reimann A, Kadenbach B: Tissue-specific regulation of bovine heart cytochrome c oxidase by ADP via interaction with subunit Via. Proc Natl Acad Sci USA 90: 1652-1656, 1993
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1652-1656
    • Anthony, G.1    Reimann, A.2    Kadenbach, B.3
  • 20
    • 0026633086 scopus 로고
    • Stoichiometric binding of 2¢ (or 3¢)-0-(2,4,6 trinitrophenyl)-adenosine-5-triphosphate to bovine heart cytochrome c oxidase
    • Reimann A, Kadenbach B: Stoichiometric binding of 2¢ (or 3¢)-0-(2,4,6 trinitrophenyl)-adenosine-5-triphosphate to bovine heart cytochrome c oxidase. FEBS Lett 307: 294-296, 1992
    • (1992) FEBS Lett , vol.307 , pp. 294-296
    • Reimann, A.1    Kadenbach, B.2
  • 21
    • 0023768509 scopus 로고
    • Mitochondrial ATP synthase. Overexpression in Escherichia coli of a rat liver β subunit peptide and its interaction with adenine nucleotides
    • Garboczi DM, Hullihen JH, Pedersen PL: Mitochondrial ATP synthase. Overexpression in Escherichia coli of a rat liver β subunit peptide and its interaction with adenine nucleotides. J Biol Chem 263: 15694-15698, 1988
    • (1988) J Biol Chem , vol.263 , pp. 15694-15698
    • Garboczi, D.M.1    Hullihen, J.H.2    Pedersen, P.L.3
  • 22
    • 0027945401 scopus 로고
    • Regulation of cytochrome c oxidase by interaction of ATP at two binding sites, one on subunit Via
    • Taanman J-W, Turina P, Capaldi RA: Regulation of cytochrome c oxidase by interaction of ATP at two binding sites, one on subunit Via. Biochemistry 33: 11833-11841, 1994
    • (1994) Biochemistry , vol.33 , pp. 11833-11841
    • Taanman, J.-W.1    Turina, P.2    Capaldi, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.