Home
  >  
Section 43
  >  
Chapter 42,469

Catalytic properties of the ATPase on submitochondrial particles after exchange of tightly bound nucleotides under different steady state conditions

Myers, J.A.; Boyer, P.D.

Febs Letters 162(2): 277-281

1983

ISSN/ISBN: 0014-5793
PMID: 6226536
DOI: 10.1016/0014-5793(83)80771-6
Accession: 042468090
Download citation:  
Text
  |  
BibTeX
  |  
RIS
Energized submitochondrial particles were subjected to high or low [3H]ATP/[3H]ADP ratios, maintained during steady state by a pyruvate kinase or hexokinase regenerating system, respectively. Under both steady state conditions, about 1.4 mol [3H]nucleotide/mol ATPase was retained but considerably more [3H]ATP was retained with the high [3H]ATP/[3H]ADP ratio. The ATPase activity and the oxygen exchange of these differentially labeled SMP were the same, suggesting a lack of control function of non-catalytic tightly bound nucleotides.

PDF emailed within 0-6 h: $19.90




Related References

Leimgruber, R.M.; Senior, A.E. 1976: Removal of "tightly bound" nucleotides from phosphorylating submitochondrial particles Journal of Biological Chemistry 251(22): 7110-7113
Martínez, F.; Meaney, A.; Espinosa-García, M.T.; Pardo, J.P.; Uribe, A.; Flores-Herrera, O. 1996: Characterization of the F1F0-ATPase and the tightly-bound ATPase activities in submitochondrial particles from human term placenta Placenta 17(5-6): 345-350
Van Dongen, M.B.; Berden, J.A. 1987: Exchange and hydrolysis of tightly bound nucleotides in normal and photolabelled bovine heart mitochondrial F1-ATPase Biochimica et Biophysica Acta 893(1): 22-32
Tiefert, M.A.; Shavit, N. 1983: Evaluation by steady-state enzyme kinetics of the role of tightly bound nucleotides during photophosphorylation Journal of Bioenergetics and Biomembranes 15(5): 257-276
Leimgruber, R.M.; Senior, A.E. 1978: Tightly-bound ATP and ADP in reconstituted submitochondrial particles Biochemical and Biophysical Research Communications 83(3): 837-842
Guerrero, K.J.; Boyer, P.D. 1988: Tightly bound 2-azido-adenine nucleotides at catalytic and noncatalytic sites of the rat liver F1 ATPase label adjacent tryptic peptides of the beta subunit Biochemical and Biophysical Research Communications 154(3): 854-860
Xing, L.; Yang, J.; Zhang, Y.; Ni, B.-J.; Yang, C.; Yuan, C.; Li, A. 2022: Model-based evaluation of the impacts of aeration on tightly bound and loosely bound extracellular polymeric substance production under non-steady-state conditions Science of the Total Environment 852: 158566
Henderson, P.J. 1972: A linear equation that describes the steady-state kinetics of enzymes and subcellular particles interacting with tightly bound inhibitors Biochemical Journal 127(2): 321-333
Leimgruber, R.M.; Senior, A.E. 1977: Tightly bound nucleotides on mitochondrial atpase Biophysical Journal 17(2): 66A
Wong, S.Y.; Matsuno-Yagi, A.; Hatefi, Y. 1984: Kinetics of ATP hydrolysis by F1-ATPase and the effects of anion activation, removal of tightly bound nucleotides, and partial inhibition of the ATPase by covalent modification Biochemistry 23(21): 5004-5009
Wang, Y.L.; Taylor, D.L. 1981: Exchange of 1,N6-etheno-ATP with actin-bound nucleotides as a tool for studying the steady-state exchange of subunits in F-actin solutions Proceedings of the National Academy of Sciences of the United States of America 78(9): 5503-5507
Kozlov, I.A.; Vulfson, E.N. 1985: Tightly bound nucleotides affect phosphate binding to mitochondrial F1-ATPase Febs Letters 182(2): 425-428
Ward, D.G.; Schoner, W.; Cavieres, J.D. 1997: Nucleotides trigger the release of Co 4ATP tightly bound to inactivated Na,K-ATPase Beauge, L A, Gadsby, D C, Garrahan, P J Annals of the New York Academy of Sciences; Na/K-ATPase and related transport ATPases: Structure, mechanism, and regulation 432-434
Ward, D.G.; Schoner, W.; Cavieres, J.D. 1997: Nucleotides trigger the release of Co(NH3)4ATP tightly bound to inactivated Na,K-ATPase Annals of the new York Academy of Sciences 834: 432-434
Wilson, S.B.; Bonner, W.D. 1970: Preparation and some properties of submitochondrial particles from tightly coupled mung bean mitochondria Plant Physiology 46(1): 25-30
Mil'grom Y.M.; Murataliev, M.B. 1988: Interaction of inorganic phosphate with the membrane bound f 1 atpase of submitochondrial particles Biologicheskie Membrany 5(1): 5-12
Harris, D.A.; Slater, E.D. 1975: Tightly bound nucleotides of the energy-transducing ATPase of chloroplasts and their role in photophosphorylation Biochimica et Biophysica Acta 387(2): 335-348
Penefsky, H.S. 1985: Reaction mechanism of the membrane-bound ATPase of submitochondrial particles from beef heart Journal of Biological Chemistry 260(25): 13728-13734
Krull, K.W.; Schuster, S.M. 1981: Control of beef heart submitochondrial particle-catalyzed Pi goes to and comes from ATP exchange by nucleotides and the ATPase inhibitor protein Journal of Biological Chemistry 256(13): 6641-6645
Schumann, J. 1984: The exchange of tightly bound nucleotides on the membrane associated chloroplast atp synthase complex Biochimica et Biophysica Acta 766(2): 334-342