메뉴 건너뛰기




Volumn 267, Issue 2, 2000, Pages 541-548

Nucleotide binding of an ADP analog to cooperating sites of chloroplast F1-ATPase (CF1)

Author keywords

ATPase; CF1; Modelling; Nucleotide binding; Photophosphorylation

Indexed keywords

ADENOSINE TRIPHOSPHATASE; NUCLEOTIDE;

EID: 0033958651     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01029.x     Document Type: Article
Times cited : (2)

References (42)
  • 2
    • 0028148233 scopus 로고
    • Our primary source of ATP
    • 2. Cross, R.L. (1994) Our primary source of ATP. Nature 370, 594-595.
    • (1994) Nature , vol.370 , pp. 594-595
    • Cross, R.L.1
  • 3
    • 0028588948 scopus 로고
    • The regulation of catalysis in ATP synthase
    • 3. Walker, J.E. (1994) The regulation of catalysis in ATP synthase. Curr. Opinion Struct. Biol. 4, 912-918.
    • (1994) Curr. Opinion Struct. Biol. , vol.4 , pp. 912-918
    • Walker, J.E.1
  • 5
    • 0025059562 scopus 로고
    • 1-ATPase is not affected by mutation of bulky residues in the 'glycine-rich loop'
    • 1-ATPase is not affected by mutation of bulky residues in the 'glycine-rich loop'. FEBS Lett. 273, 147-149.
    • (1990) FEBS Lett. , vol.273 , pp. 147-149
    • Pagan, J.1    Senior, A.E.2
  • 7
    • 0008932796 scopus 로고
    • Control af ATP hydrolysis in chloroplasts
    • 7. Strotmann, H., Kleefeld, S. & Lohse, D. (1987) Control af ATP hydrolysis in chloroplasts. FEBS Lett. 221, 265-269.
    • (1987) FEBS Lett. , vol.221 , pp. 265-269
    • Strotmann, H.1    Kleefeld, S.2    Lohse, D.3
  • 8
    • 0015894660 scopus 로고
    • Preparation and properties of 2′ (or 3′)-O-(2,4,6-trinitrophenyl) adenosine 5′-triphosphate, an analog of adenosine triphosphate
    • 8. Hiratsuka, T. & Uchida, K. (1973) Preparation and properties of 2′ (or 3′)-O-(2,4,6-trinitrophenyl) adenosine 5′-triphosphate, an analog of adenosine triphosphate. Biochim. Biophys. Acta 320, 635-647.
    • (1973) Biochim. Biophys. Acta , vol.320 , pp. 635-647
    • Hiratsuka, T.1    Uchida, K.2
  • 9
    • 0008921215 scopus 로고
    • Photophosphorylation of ribose modified ADP analogs by spinach chloroplasts
    • 9. Boos, K.S., Dimke, B., Schlimme, E., Wiedner, H., Edelmann, K. & Strotmann, H. (1981) Photophosphorylation of ribose modified ADP analogs by spinach chloroplasts. FEBS Lett. 130, 73-76.
    • (1981) FEBS Lett. , vol.130 , pp. 73-76
    • Boos, K.S.1    Dimke, B.2    Schlimme, E.3    Wiedner, H.4    Edelmann, K.5    Strotmann, H.6
  • 10
    • 0020476123 scopus 로고
    • Mechanism for catalysis and regulation of adenosine 5′-triphosphate hydrolysis by chloroplast coupling factor 1
    • 10. Bruist, M.F. & Hammes, G.G. (1982) Mechanism for catalysis and regulation of adenosine 5′-triphosphate hydrolysis by chloroplast coupling factor 1. Biochemistry 21, 3370-3377.
    • (1982) Biochemistry , vol.21 , pp. 3370-3377
    • Bruist, M.F.1    Hammes, G.G.2
  • 11
    • 0023052005 scopus 로고
    • Binding of 2′(3′)-O-(2,4,6-trinitrophenyl) adenosine 5′-diphosphate opens the pathway for protons through the chloroplast ATPase complex
    • 11. Wagner, R., Ponse, G. & Strotmann, H. (1986) Binding of 2′(3′)-O-(2,4,6-trinitrophenyl) adenosine 5′-diphosphate opens the pathway for protons through the chloroplast ATPase complex. Eur. J. Biochem. 161, 205-209.
    • (1986) Eur. J. Biochem. , vol.161 , pp. 205-209
    • Wagner, R.1    Ponse, G.2    Strotmann, H.3
  • 13
    • 0031574466 scopus 로고    scopus 로고
    • Rotary chemiosmotic machines
    • 13. Khan, S. (1997) Rotary chemiosmotic machines. Biochim. Biophys. Acta 1322, 86-105.
    • (1997) Biochim. Biophys. Acta , vol.1322 , pp. 86-105
    • Khan, S.1
  • 14
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase - A splendid molecular machine
    • 14. Boyer, P.D. (1997) The ATP synthase - a splendid molecular machine. Annu. Rev. Biochem. 66, 717-749.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 16
    • 0020490602 scopus 로고
    • Quantitation of aromatic residues in proteins: Model compounds for second-derivative spectroscopy
    • 16. Levine, R.L. & Federici, M.M. (1982) Quantitation of aromatic residues in proteins: model compounds for second-derivative spectroscopy. Biochemistry 21, 2600-2606.
    • (1982) Biochemistry , vol.21 , pp. 2600-2606
    • Levine, R.L.1    Federici, M.M.2
  • 17
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • 17. Gill, S.C. & von Hippel, PH. (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 18
    • 0029916911 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence databank and its new supplement TREMBL
    • 18. Bairoch, A. & Apweiler, R. (1996) The SWISS-PROT protein sequence databank and its new supplement TREMBL. Nucleic Acids Res. 24, 21-25.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 21-25
    • Bairoch, A.1    Apweiler, R.2
  • 19
    • 0003904803 scopus 로고
    • Ultraviolet absorption spectra of proteins and amino acids
    • 19. Beaven, G.H. & Holiday, E.R. (1952) Ultraviolet absorption spectra of proteins and amino acids. Advan. Prot. Chem. 7, 319-386.
    • (1952) Advan. Prot. Chem. , vol.7 , pp. 319-386
    • Beaven, G.H.1    Holiday, E.R.2
  • 20
    • 0020740241 scopus 로고
    • Analysis of numerical methods for computer simulations of kinetic processes: Development of KINSIM - A flexible, portable system
    • 20. Barshop, B.A., Wrenn, R.F. & Frieden, C. (1983) Analysis of numerical methods for computer simulations of kinetic processes: development of KINSIM - a flexible, portable system. Anal. Biochem. 130, 134-145.
    • (1983) Anal. Biochem. , vol.130 , pp. 134-145
    • Barshop, B.A.1    Wrenn, R.F.2    Frieden, C.3
  • 21
    • 0001008029 scopus 로고
    • A method for minimizing a sum of squares of non-linear functions without calculating derivatives
    • 21. Powell, M.J.D. (1964) A method for minimizing a sum of squares of non-linear functions without calculating derivatives. Computer J. 7, 303-307.
    • (1964) Computer J. , vol.7 , pp. 303-307
    • Powell, M.J.D.1
  • 22
    • 0023442604 scopus 로고
    • Fitting curves to data using nonlinear regression: A practical and nonmathematical review
    • 22. Motulsky, H.J. & Ransnas, L.A. (1987) Fitting curves to data using nonlinear regression: a practical and nonmathematical review. FASEB J. 1, 365-374.
    • (1987) FASEB J. , vol.1 , pp. 365-374
    • Motulsky, H.J.1    Ransnas, L.A.2
  • 25
    • 0024237430 scopus 로고
    • 1-ATPase. Evidence for alternating high affinity site during steady-state turnover
    • 1-ATPase. Evidence for alternating high affinity site during steady-state turnover. J. Biol. Chem. 263, 18850-18856.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18850-18856
    • Cunningham, D.1    Cross, R.L.2
  • 26
    • 0001905925 scopus 로고
    • 1-ATPase with ADP. Characterization of a high-affinity binding site responsible for ADP-induced inhibition
    • 1-ATPase with ADP Characterization of a high-affinity binding site responsible for ADP-induced inhibition. Biochim. Biophys. Acta 975, 50-58.
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 50-58
    • Milgrom, Y.M.1    Murataliev, M.B.2
  • 28
    • 0018791465 scopus 로고
    • Kinetic analysis of light-dependent exchange of adenine nucleotide on chloroplast coupling factor CF1
    • 28. Startmann, H., Bickel-Sandkötter, S. & Shoshan, V. (1979) Kinetic analysis of light-dependent exchange of adenine nucleotide on chloroplast coupling factor CF1. FEBS Lett. 101, 316-320.
    • (1979) FEBS Lett. , vol.101 , pp. 316-320
    • Startmann, H.1    Bickel-Sandkötter, S.2    Shoshan, V.3
  • 29
    • 0027317040 scopus 로고
    • 1-ATPase provides a direct probe of nucleotide binding: Maximal hydrolysis occurs with three sites occupied
    • 1-ATPase provides a direct probe of nucleotide binding: maximal hydrolysis occurs with three sites occupied. J. Biol. Chem. 268, 20126-20133.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20126-20133
    • Weber, J.1    Wilke-Mounts, S.2    Lee, R.S.-F.3    Grell, E.4    Senior, A.E.5
  • 31
    • 0023253910 scopus 로고
    • Interactions between nucleotide binding sites on chloroplast coupling factor 1 during ATP hydrolysis
    • 31. Leckband, D. & Hammes, G.G. (1987) Interactions between nucleotide binding sites on chloroplast coupling factor 1 during ATP hydrolysis. Biochemistry 26, 2306-2310.
    • (1987) Biochemistry , vol.26 , pp. 2306-2310
    • Leckband, D.1    Hammes, G.G.2
  • 32
    • 0024371966 scopus 로고
    • A perspective of the binding change mechanism for ATP synthesis
    • 32. Boyer, P.D. (1989) A perspective of the binding change mechanism for ATP synthesis. FASEB J. 3, 2164-2178.
    • (1989) FASEB J. , vol.3 , pp. 2164-2178
    • Boyer, P.D.1
  • 35
    • 0022343282 scopus 로고
    • Reaction mechanism of the membrane-bound ATPase of submitochondrial particles from beef heart
    • 35. Penefsky, H.S. (1985) Reaction mechanism of the membrane-bound ATPase of submitochondrial particles from beef heart. J. Biol. Chem. 260, 13728-13734.
    • (1985) J. Biol. Chem. , vol.260 , pp. 13728-13734
    • Penefsky, H.S.1
  • 36
    • 0024279292 scopus 로고
    • Alteration of the nucleotide-binding site asymmetry of chloroplast coupling factor 1 by catalysis
    • 36. Shapiro, A.B. & McCarty, R.E. (1988) Alteration of the nucleotide-binding site asymmetry of chloroplast coupling factor 1 by catalysis. J. Biol. Chem. 263, 14160-14165.
    • (1988) J. Biol. Chem. , vol.263 , pp. 14160-14165
    • Shapiro, A.B.1    McCarty, R.E.2
  • 37
    • 0008897442 scopus 로고
    • Diphenyl ether herbicides, a tool to eludicate the mechanism of photophosphorylatio
    • 37. Huchzermeyer, B. & Löhr, A. (1990) Diphenyl ether herbicides, a tool to eludicate the mechanism of photophosphorylatio. Z. Naturforsch. 45c, 552-557.
    • (1990) Z. Naturforsch. , vol.45 C , pp. 552-557
    • Huchzermeyer, B.1    Löhr, A.2
  • 39
    • 0028957841 scopus 로고
    • In vitro assembly of the core of the chloroplast ATP synthase
    • 39. Gao, F., Lipscomb, B., Wu, I. & Richter, M.L. (1995) In vitro assembly of the core of the chloroplast ATP synthase. J. Biol. Chem. 270, 9763-9769.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9763-9769
    • Gao, F.1    Lipscomb, B.2    Wu, I.3    Richter, M.L.4
  • 40
    • 0029893335 scopus 로고    scopus 로고
    • Intersubunit rotation in active F-ATPase
    • 40. Sabbert, D., Engelbrecht, S. & Junge, W. (1996) Intersubunit rotation in active F-ATPase. Nature 381, 623-625.
    • (1996) Nature , vol.381 , pp. 623-625
    • Sabbert, D.1    Engelbrecht, S.2    Junge, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.