Kinetic properties of a single nucleotide binding site on chloroplast coupling factor 1 (CF1)

European Journal of Biochemistry

Volumn 258, Issue 2, 1998, Pages 710-715

  Günther, Stephan ^a   Huchzermeyer, Bernhard ^a  

^a UNIVERSITY OF VETERINARY MEDICINE HANNOVER   (Germany)

Author keywords

ATP synthase; Binding kinetics; Binding sites; F1 ATPase; Nucleotide binding

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; MAGNESIUM; NUCLEOTIDE BINDING PROTEIN;

ALPHA CHAIN; ARTICLE; BETA CHAIN; BINDING AFFINITY; BINDING KINETICS; BINDING SITE; CHLOROPLAST; COUPLING FACTOR; CRYSTAL STRUCTURE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SPINACH; THYLAKOID; ULTRAVIOLET SPECTROPHOTOMETRY;

ADENOSINE DIPHOSPHATE; ALUMINUM; BINDING SITES; ENZYME INHIBITORS; FLUORESCENT DYES; FLUORINE; KINETICS; NUCLEOTIDES; PROTEIN BINDING; PROTON-TRANSLOCATING ATPASES; SPECTROPHOTOMETRY; SPINACIA OLERACEA;

SPINACIA OLERACEA;

EID: 0032403884     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2580710.x     Document Type: Article

References (39)

1. 1-ATPase from bovine heart mitochondria, Nature 370, 621-628.
2. Khan, S. (1997) Rotary chemiosmotic machines, Biochim. Biophys. Acta 1322, 86-105
3. Boyer, P. D. (1993) The binding change mechanism for ATP synthase - some probabilities and possibilities, Biochim. Biophys. Acta 1140, 215-250.
4. Boyer, P. D. (1997) The ATP synthase - a splendid molecular machine, Annu. Rev. Biochem. 66, 717-749.
5. Sabbert, D., Engelbrecht, S. & Junge, W. (1996) Intersubunit rotation in active F-ATPase, Nature 381, 623-625.
6. 1-ATPase: evidence that ATP synthase is a rotary motor enzyme, J. Bioenerg. Biomembr. 29, 207-209.
7. 1-ATPase, Proc. Natl Acad. Sci. USA 92, 10964-10968.
8. 1, Biochem. Biophys. Res. Commun. 240, 247-256.
9. Shapiro, A. B., Huber, A. H. & McCarty, R. E. (1991) Four tight nucleotide binding sites of chloroplast coupling factor 1, J. Biol. Chem. 266, 4194-4200.
10. Strotmann, H. (1986) Evaluation of results on nucleotide-binding sites of the ATPase complex, Encycl. Plant Physiol. 19, 584-594.
11. 1-ATPase, J. Bioenerg. Biomembr. 26, 573-581.
12. Hiratsuka, T. & Uchida, K. (1973) Preparation and properties of 2′(or 3′)-O-(2,4,6-tri-nitrophenyl) adenosine 5′-triphosphate, an analog of adenosine triphosphate, Biochim. Biophys. Acta 320, 635-647.
13. 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.
14. 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.
15. 1-ATPase. J. Biol. Chem. 271, 3474-3477.
16. 3H]ADP entrapped as fluorometal complexes into the catalytic sites of the enzyme, Biochemistry 33, 3772-3777.
17. +-transporting ATPase by forming of a tight nucleoside diphosphate-fluoroaluminate complex at the catalytic site, Proc. Natl Acad. Sci. USA 85, 8958-8962.
18. Linnett, P. E., Mitchell, A. D., Partis, M. D. & Beechey, R. B. (1979) Preparation of the soluble ATPase from mitochondria, chloroplasts, and bacteria by the chloroform technique, Methods Enzymol. 55, 337-343.
19. Penefsky, H. S. (1977) Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase, J. Biol. Chem. 252, 2891-2899.
20. Andreo, C. S., Patrie, W. J. & McCarty, R. E. (1982) Effects of ATPase activation and the δ subunit of coupling factor 1 on reconstitution of photophosphorylation, J. Biol. Chem. 257, 9968-9975.
21. Levine, R. L. & Federici, M. M. (1982) Quantitation of aromatic residues in proteins: model compounds for second-derivative spectroscopy, Biochemistry 21, 2600-2606.
22. Gill, S. C. & von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data, Anal. Biochem. 182, 319-326.
23. Bairoch, A. & Apweiler, R. (1996) The SWISS-PROT protein sequence databank and its new supplement TREMBL, Nucleic Acids Res. 24, 21-25.
24. Beaven, G. H. & Holiday, H. R. (1952) Ultraviolet absorption spectra of proteins and amino acids, Adv. Protein Chem. 7, 319-386.
25. Powell, M. J. D. (1964) A method for minimizing a sum of squares of non-linear functions without calculating derivatives, Comput. J. 7, 303-307.
26. 1-ATPase, J. Biol. Chem. 269, 11261-11268.
27. 1-ATPase is required for expression of the enzyme activity, J. Biol. Chem. 265, 18725-18728.
28. Motulsky, H. J. & Ransnas, L. A. (1987) Filting curves to data using nonlinear regression: a practical and nonmathematical review, FASEB J. 1, 365-374.
29. 1) cannot be explained by a two site model, Ber. Bunsenges. Phys. Chem. 100, 2020-2023.
30. Girault, G., Berger, G., Galmiche, J.-M. & Andre, F. (1988) Characterization of six nucleotide-binding sites on chloroplast couplins factor 1 and one on its purified β subunit, J. Biol. Chem. 263, 14690-14695.
31. Shapiro, A. B., Gibson, K. D., Scheraga, H. A. & McCarty, R. F., (1991) Fluorescence resonance energy transfer mapping of the fourth of six nucleotide-binding sites of chloroplast coupling factor 1, J. Biol. Chem. 266, 17276-17285.
32. Labahn, A., Fromme, P. & Gräber, P. (1990) Uni-site ATP synthesis in thylakoids, FEBS Lett. 271, 116-118.
33. 1-ATPase. J. Biol. Chem. 266, 11551-11558.
34. 1-ATPase, J. Biol. Chem. 268, 1558-1566.
35. Wetzel, C. M. & McCarty, R. E. (1993) Aspects of subunit interactions in the chloroplast ATP Synthase. I. Isolation of a chloroplast coupling factor 1-subunit III complex from spinach thylakoids, Plant Physiol. 102, 251-259.
36. 1-ATPase asymmetry and subunit location, J. Biol. Chem. 262, 3488-3495.
37. 1-ATPase. Evidence for an adenylate kinase-like orientation of catalytic and noncatalytic sites, J. Biol. Chem. 266, 6101-6105.
38. Strotmann, H., Kleefeld, S. & Lohse, D. (1987) Control at ATP hydrolysis in chloroplasts, FEBS Lett. 221, 265-269.
39. Strotmann, H., Bickel, S. & Huchzermeyer, B. (1976) Energy-dependent release of adenine nucleotides tightly bound to chloroplast coupling factor CF1. FEBS Lett. 61, 194-198.