메뉴 건너뛰기




Volumn 1757, Issue 5-6, 2006, Pages 304-310

Requirement of medium ADP for the steady-state hydrolysis of ATP by the proton-translocating Paracoccus denitrificans Fo·F1-ATP synthase

Author keywords

ATP hydrolysis; Fo F1 ATP synthase; Paracoccus denitrificans

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; PHOSPHOENOLPYRUVATE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; PYRUVATE KINASE;

EID: 33745626133     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2006.03.001     Document Type: Article
Times cited : (9)

References (43)
  • 1
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock D., Leslie A.G.W., and Walker J.E. Molecular architecture of the rotary motor in ATP synthase. Science 286 (1999) 1700-1705
    • (1999) Science , vol.286 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.W.2    Walker, J.E.3
  • 2
  • 4
    • 0027492268 scopus 로고
    • The binding change mechanism for ATP synthase. Some probabilities and possibilities
    • Boyer P.D. The binding change mechanism for ATP synthase. Some probabilities and possibilities. Biochim. Biophys. Acta 1140 (1993) 215-250
    • (1993) Biochim. Biophys. Acta , vol.1140 , pp. 215-250
    • Boyer, P.D.1
  • 5
    • 0034738153 scopus 로고    scopus 로고
    • The rotary binding change mechanism of ATP synthases
    • Cross R.L. The rotary binding change mechanism of ATP synthases. Biochim. Biophys. Acta 1458 (2000) 270-275
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 270-275
    • Cross, R.L.1
  • 6
    • 0028114231 scopus 로고
    • Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams J.P., Leslie A.G.W., Lutter R., and Walker J.E. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature 370 (1994) 621-628
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.W.2    Lutter, R.3    Walker, J.E.4
  • 7
    • 0032529839 scopus 로고    scopus 로고
    • The 2.8 Å structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis
    • Bianchet M.A., Hullihen J., Pedersen P.L., and Amzel L.M. The 2.8 Å structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 11065-11070
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 11065-11070
    • Bianchet, M.A.1    Hullihen, J.2    Pedersen, P.L.3    Amzel, L.M.4
  • 9
    • 0035846822 scopus 로고    scopus 로고
    • 1-ATPase at 3.2 Å resolution
    • 1-ATPase at 3.2 Å resolution. J. Biol. Chem. 276 (2001) 1345-1352
    • (2001) J. Biol. Chem. , vol.276 , pp. 1345-1352
    • Groth, G.1    Pohl, E.2
  • 13
    • 0033953115 scopus 로고    scopus 로고
    • 1-ATPase: is ATP synthase a reversible molecular machine?
    • 1-ATPase: is ATP synthase a reversible molecular machine?. J. Exp. Biol. 203 (2000) 41-49
    • (2000) J. Exp. Biol. , vol.203 , pp. 41-49
    • Vinogradov, A.D.1
  • 14
    • 0016296730 scopus 로고
    • Flip-flop model of energy interconversion by ATP synthase
    • Repke K.R.H., and Schön R. Flip-flop model of energy interconversion by ATP synthase. Acta Biol. Med. Ger. 33 (1974) K27-K38
    • (1974) Acta Biol. Med. Ger. , vol.33
    • Repke, K.R.H.1    Schön, R.2
  • 15
    • 0015219564 scopus 로고
    • Flip-flop mechanisms in enzymology. A model: the alkaline phosphatase of Escherichia coli
    • Lazdunski M., Petitclerc C., Chappelet D., and Lazdunski C. Flip-flop mechanisms in enzymology. A model: the alkaline phosphatase of Escherichia coli. Eur. J. Biochem. 20 (1971) 124-139
    • (1971) Eur. J. Biochem. , vol.20 , pp. 124-139
    • Lazdunski, M.1    Petitclerc, C.2    Chappelet, D.3    Lazdunski, C.4
  • 16
    • 0019325489 scopus 로고
    • Kinetics of interaction of adenosine diphosphate and adenosine triphosphate with ATPase of bovine heart submitochondrial particles
    • Vasilyeva E.A., Fitin A.F., Minkov I.B., and Vinogradov A.D. Kinetics of interaction of adenosine diphosphate and adenosine triphosphate with ATPase of bovine heart submitochondrial particles. Biochem. J. 188 (1980) 807-815
    • (1980) Biochem. J. , vol.188 , pp. 807-815
    • Vasilyeva, E.A.1    Fitin, A.F.2    Minkov, I.B.3    Vinogradov, A.D.4
  • 17
    • 33745614998 scopus 로고
    • 1-ATPase is due to saturation of noncatalytic sites with ADP which blocks activation of the enzyme by ATP
    • 1-ATPase is due to saturation of noncatalytic sites with ADP which blocks activation of the enzyme by ATP. J. Biol. Chem. 268 (1994) 1558-1566
    • (1994) J. Biol. Chem. , vol.268 , pp. 1558-1566
    • Jault, J.-M.1    Allison, W.S.2
  • 18
    • 0014811439 scopus 로고
    • The critical electric potential difference for photophosphorylation
    • Junge W. The critical electric potential difference for photophosphorylation. Eur. J. Biochem. 14 (1970) 582-592
    • (1970) Eur. J. Biochem. , vol.14 , pp. 582-592
    • Junge, W.1
  • 19
    • 0027982270 scopus 로고
    • +-ATPase from chloroplasts: energetic of the catalytic cycle
    • +-ATPase from chloroplasts: energetic of the catalytic cycle. Biochim. Biophys. Acta 1187 (1994) 171-174
    • (1994) Biochim. Biophys. Acta , vol.1187 , pp. 171-174
    • Gräber, P.1
  • 21
    • 0034730636 scopus 로고    scopus 로고
    • The activity of the ATP synthase from Escherichia coli is regulated by the transmembrane proton motive force
    • Fisher S., Gräber P., and Turina P. The activity of the ATP synthase from Escherichia coli is regulated by the transmembrane proton motive force. J. Biol. Chem. 275 (2000) 30157-30162
    • (2000) J. Biol. Chem. , vol.275 , pp. 30157-30162
    • Fisher, S.1    Gräber, P.2    Turina, P.3
  • 22
    • 1842478082 scopus 로고    scopus 로고
    • 1-ATPase in Paracoccus denitrificans plasma membranes
    • 1-ATPase in Paracoccus denitrificans plasma membranes. J. Biol. Chem. 279 (2004) 12319-12324
    • (2004) J. Biol. Chem. , vol.279 , pp. 12319-12324
    • Zharova, T.V.1    Vinogradov, A.D.2
  • 23
    • 0020069242 scopus 로고
    • Kinetic mechanism of mitochondrial adenosine triphosphatase. Inhibition by azide and activation by sulphite
    • Vasilyeva E.A., Minkov I.B., Fitin A.F., and Vinogradov A.D. Kinetic mechanism of mitochondrial adenosine triphosphatase. Inhibition by azide and activation by sulphite. Biochem. J. 202 (1982) 15-23
    • (1982) Biochem. J. , vol.202 , pp. 15-23
    • Vasilyeva, E.A.1    Minkov, I.B.2    Fitin, A.F.3    Vinogradov, A.D.4
  • 25
    • 0035519250 scopus 로고    scopus 로고
    • Inhibition of steady-state mitochondrial ATP synthesis by bicarbonate, an activating anion of ATP hydrolysis
    • Lodeyro A.F., Calcaterra N.B., and Roveri O.A. Inhibition of steady-state mitochondrial ATP synthesis by bicarbonate, an activating anion of ATP hydrolysis. Biochim. Biophys. Acta 1506 (2001) 236-243
    • (2001) Biochim. Biophys. Acta , vol.1506 , pp. 236-243
    • Lodeyro, A.F.1    Calcaterra, N.B.2    Roveri, O.A.3
  • 26
    • 0000361210 scopus 로고
    • Differential effects of ADP on ATPase and oxidative phosphorylation in submitochondrial particles
    • Minkov I.B., Vasilyeva E.A., Fitin A.F., and Vinogradov A.D. Differential effects of ADP on ATPase and oxidative phosphorylation in submitochondrial particles. Biochem. Int. 1 (1980) 478-485
    • (1980) Biochem. Int. , vol.1 , pp. 478-485
    • Minkov, I.B.1    Vasilyeva, E.A.2    Fitin, A.F.3    Vinogradov, A.D.4
  • 28
    • 33745633505 scopus 로고    scopus 로고
    • T.V. Zharova, A.D. Vinogradov, The requirement of ADP and Pi for steady-state operation of proton-translocating ATPase in Paracoccus denitrificans membranes, Biochim. Biophys. Acta, 13 EBEC Short reports (2004) I-A, p-36.
  • 29
    • 0014845521 scopus 로고
    • Oxidative phosphorylation coupled to oxygen uptake and nitrate reduction in Micrococcus denitrificans
    • John P., and Whatley F.R. Oxidative phosphorylation coupled to oxygen uptake and nitrate reduction in Micrococcus denitrificans. Biochim. Biophys. Acta 216 (1970) 342-352
    • (1970) Biochim. Biophys. Acta , vol.216 , pp. 342-352
    • John, P.1    Whatley, F.R.2
  • 30
    • 0242449119 scopus 로고
    • Respiratory control in membrane particles from Micrococcus denitrificans
    • John P., and Hamilton W.A. Respiratory control in membrane particles from Micrococcus denitrificans. FEBS Lett. 10 (1970) 246-248
    • (1970) FEBS Lett. , vol.10 , pp. 246-248
    • John, P.1    Hamilton, W.A.2
  • 31
    • 0025072729 scopus 로고
    • Slow active/inactive transition of the mitochondrial NADH-ubiquinone reductase
    • Kotlyar A.B., and Vinogradov A.D. Slow active/inactive transition of the mitochondrial NADH-ubiquinone reductase. Biochim. Biophys. Acta 1019 (1990) 151-158
    • (1990) Biochim. Biophys. Acta , vol.1019 , pp. 151-158
    • Kotlyar, A.B.1    Vinogradov, A.D.2
  • 33
    • 0001571920 scopus 로고
    • Sensitive measurements of changes of hydrogen ion concentration
    • Chance B., and Nishimura M. Sensitive measurements of changes of hydrogen ion concentration. Methods Enzymol. 10 (1967) 641-650
    • (1967) Methods Enzymol. , vol.10 , pp. 641-650
    • Chance, B.1    Nishimura, M.2
  • 34
    • 0018369597 scopus 로고
    • The use of cyanine dyes for the determination of membrane potential in cells, organelles, and vesicles
    • Waggoner A.S. The use of cyanine dyes for the determination of membrane potential in cells, organelles, and vesicles. Methods Enzymol. 55 (1979) 689-695
    • (1979) Methods Enzymol. , vol.55 , pp. 689-695
    • Waggoner, A.S.1
  • 36
    • 0034737965 scopus 로고    scopus 로고
    • ATP synthase: what we know about ATP hydrolysis and what we do not know about ATP synthesis
    • Weber J., and Senior A.E. ATP synthase: what we know about ATP hydrolysis and what we do not know about ATP synthesis. Biochim. Biophys. Acta 1458 (2000) 300-309
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 300-309
    • Weber, J.1    Senior, A.E.2
  • 40
    • 0033623349 scopus 로고    scopus 로고
    • Structure of the γ-ε complex of ATP synthase
    • Rodgers A.J.W., and Wilce M.C.J. Structure of the γ-ε complex of ATP synthase. Nat. Struct. Biol. 7 (2000) 1051-1054
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1051-1054
    • Rodgers, A.J.W.1    Wilce, M.C.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.