Acceleration of unisite catalysis of mitochondrial F1-adenosinetriphosphatase by ATP, ADP and pyrophosphate Hydrolysis and release of the previously bound [γ-32P]ATP

European Journal of Biochemistry

Volumn 249, Issue 2, 1997, Pages 622-629

  García, José J ^a   Gómez Puyou, Armando ^b   Maldonado, Ernesto ^b   Tuena De Gómez Puyou, Marietta ^b  

^a INSTITUTO NACIONAL DE CARDIOLOGÍA IGNACIO CHÁVEZ   (Mexico)

^b INSTITUTO DE FISIOLOGÍA CELULAR   (Mexico)

Author keywords

ATP release; Cooperativity; F1 adenosinetriphosphatase; Pyrophosphate; Unisite catalysis

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; PYROPHOSPHATE;

ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME BINDING; HEART MITOCHONDRION; HUMAN; IN VITRO STUDY; ISOTOPE LABELING; NONHUMAN; PRIORITY JOURNAL;

BOVINAE;

EID: 0030682426     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00622.x     Document Type: Article

References (61)

1. 1-ATPase from bovine heart mitochondria, Nature 370, 621-628.
2. 1-ATPase, J. Biol. Chem. 263, 19640-19648.
3. 1-ATPases from Escherichia coli, J. Biol Chem. 264, 15376-15383.
4. 1-ATPases, J. Biol. Chem. 265, 4402-4410.
5. 1-ATPase can use endogenous bound phosphate to synthesize ATP in dimethyl sulfoxide, FEBS Lett. 291, 282-284.
6. 1-ATPase, Biochem. Cell Biol. 69, 291-296.
7. 1-ATPase during ATP synthesis in dimethyl sulfoxide, Biochem. Biophys. Res. Commun. 182, 697-702.
8. Boyer, P. D. (1987) The unusual enzymology of ATP synthase, Biochemistry 26, 8503-8507.
9. Boyer, P. D. (1989) A perspective for the binding change mechanism for ATP synthesis, FASEB J. 3, 2164-2178.
10. Boyer, P. D. (1993) The binding change mechanism for ATP synthase - Some probabilities and possibilities, Biochim. Biophys. Acta. 1140, 215-250.
11. 1-ATPase, J. Biol. Chem. 262, 11675-11683.
12. Cross, R. L., Grubmeyer, C. & Penefsky, H. S. (1982) Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate enhancements resulting from cooperative interactions between multiple catalytic sites. J. Biol. Chem. 257, 12101-12105.
13. 1-ATPase, Proc. Natl Acad. Sci. USA 92, 10964-10968.
14. Duncan, T. M. & Senior, A. E. (1985) The defective proton-ATPase of uncD mutants of Escherichia coli. Two mutations which affect the catalytic mechanism, J. Biol. Chem. 260, 4901-4907.
15. 1-ATPase and its release by excess ADP and ATP. Effect of trifluoperazine, J. Bioenerg. Biomembr. 29, 61-70.
16. 32P-labelled adenosine triphosphate of high specific activity, Biochem. J. 90, 147-149.
17. 1-ATPase revealed by cryoelectron microscopy, Proc. Natl Acad. Sci. USA 87, 9585-9589.
18. 1-inhibitor-protein complex in the presence of organic solvents, Eur. J. Biochem. 159, 133-140.
19. Grubmeyer, C., Cross, R. L. & Penefsky, H. S. (1982) Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate constants tor elementary steps in catalysis at a single site, J. Biol. Chem. 257, 12092-12100.
20. Grubmeyer, C. & Penefsky, H. S. (1981a) The presence of two hydrolytic sites on beef heart mitochondrial adenosine triphosphatase, J. Biol. Chem. 256, 3718-3727.
21. Grubmeyer, C. & Penefsky, H. S. (1981b) Cooperatively betwen catalytic sites in the mechanism of action of beef heart adenosine triphosphatase, J. Biol. Chem. 256, 3728-3734.
22. Hackney, D. D. & Boyer, P. D. (1978) Subunit interaction during catalysis. Implications of concentration dependency of oxygen exchanges accompanying oxidative phosphorylation for alternating site cooperatively, J. Biol. Chem. 253, 3164-3170.
23. 1-ATPase, Biochim. Biophys. Acta 974, 156-162.
24. Hutton, R. L. & Boyer, P. D. (1979) Subunit interaction during catalysis. Alternating site cooperativity of mitochondrial adenosine triphosphatase, J. Biol. Chem. 254, 9990-9993.
25. Issartel, J.-P., Favre-Bulle, O., Lunardi, J. & Vignais, P. V. (1987) Is pyrophosphate an analog of adenosine diphosphate for beef heart mitochondrial F1-ATPase? J. Biol. Chem. 262, 13538-13544.
26. 1-ATPase by decreasing the affinity of a catalytic site for inhibitory MgADP, Biochemistry 33, 14979-14985.
27. 1-ATPase, Eur. J. Biochem. 177, 213-218.
28. 1 adenosine triphosphatse in the presence of dimethyl sulfoxide, Biochemistry 31, 2088-2092.
29. Kayalar, C., Rosing, J. & Boyer, P. D. (1977) An alternating site sequence for oxidative phosphorylation suggested by measurement of substrate binding patterns and exchange reaction inhibitor, J. Biol. Chem. 252, 2486-2491.
30. 1-ATPase. Conditions that affect occupancy of catalytic and non-catalytic sites, J. Biol. Chem. 261, 12544-12549.
31. Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951) Protein measurement with the folin phenol reagent, J. Biol. Chem. 193, 265-275.
32. 1-ATPase, Eur. J. Biochem. 143, 483-490.
33. 1-ATPase, Biochemistry 28, 10022-10028.
34. 32P]pyrophosphate, Biochim. Biophys, Acta 1228, 67-72.
35. 1-ATPase turnover during ATP hydrolysis by the single catalytic site. Evidence that hydrolysis with a slow rate of product release does not occur at the alternating active site, FEBS Lett. 222, 32-36.
36. 1-ATPase, FEBS Lett. 219, 156-160.
37. 1-ATPase, Nature 386, 299-302.
38. 1 through modification with adenosine tri- or tetraphosphopyridoxal, J. Biol. Chem. 262, 7686-7692.
39. +-ATPase of Escherichia coli, FEBS Lett. 213, 381-384.
40. 1-ATPase? Biochemistry 31, 2088-2092.
41. 1 by beef heart mitochondrial adenosine triphosphatase, J. Biol. Chem. 252, 2891-2899.
42. Penefsky, H. S. (1985) Energy-dependent dissociation of ATP from high-affinity catalytic sites of beef heart mitochondrial adenosine triphosphatase, J. Biol. Chem. 260, 13735-13741.
43. Penefsky, H. S. (1988) Rate of chase-promoted hydrolysis of ATP in the high-affinity catalytic site of beef heart mitochondrial ATPase. J. Biol. Chem. 263, 6020-6022.
44. 1-type ATP synthases and ATPases, Adv. Enzymol. 64, 173-214.
45. Penefsky, H. S., Pullman, M. E., Datta, A. & Racker, F. (1960) Partial resolution of the enzymes calyzing oxidative phosphorylation. II. Participation of a soluble adenosine triphosphatase in oxidative phosphorylation. J. Biol. Chem. 235, 3330-3336.
46. 1 moiety are kinetically equivalent in hydrolyzing ATP, J. Biol. Chem. 271, 32546-32550.
47. Sabbert, D., Engelbrecht, S. & Junge, W. (1996) Intersubunit rotation in active F-ATPase, Nature 381, 623-625.
48. 1-ATPase. J. Biochem. (Tokyo) 96, 475-481.
49. 1-ATPase, J. Biochem. (Tokyo) 96, 483-487.
50. 1-ATPase in the presence of dimethyl sulfoxide, J. Biochem. (Tokyo) 93, 1601-1614.
51. Souid, A.-K. & Penefsky, H. S. (1995) Energetics of ATP dissociation from the mitochondrial ATPase during oxidative phosphorylation, J. Biol. Chem. 270, 9074-9082.
52. Tuena de Gómez-Puyou, M. & Gómez-Puyou, A. (1977) A simple method of purification of a soluble olygomycin-insensitive mitochondrial ATPase, Arch. Biochem. Biophys. 182, 82-86.
53. 1. Biochemistry 32, 2213-2218.
54. 1 through dimethyl sulfoxide-water transitions, J. Biol. Chem. 270, 16820-16825.
55. 1: characterisation of high-affinity binding sites, Biochim. Biophys. Acta 850, 359-368.
56. 1-ATPase. An approach by photolabeling and equilibrium binding studies, Eur. J. Biochem. 148, 41-47.
57. 1-ATPase, J. Biol. Chem. 270, 12653-12658.
58. 1-ATPase examined by cryoelectron microscopy, Arch. Biochem. Biophys. 299, 105-109.
59. 1-ATPase with a new photoafinty probe, 3′-O-(4-benzoyl)benzoyl adenosine 5′-triphosphate, J. Biol. Chem. 257, 2834-2841.
60. 1-ATPase from the thermophilic bacterium PS3 in 50% dimethyl sulfoxide, Biochem. Biophys. Res. Commun. 114, 907-912.
61. 1 causes rotation of the γ subunit relative to the β subunits, Biochim. Biophys. Acta 1275, 96-100.