Effect of denaturants on multisite and unisite ATP hydrolysis by bovine heart submitochondrial particles with and without inhibitor protein

2005 ◽  
Vol 439 (1) ◽  
pp. 129-137 ◽  
Author(s):  
Marietta Tuena de Gómez-Puyou ◽  
Lenin Domínguez-Ramírez ◽  
Gerardo Pérez-Hernández ◽  
Armando Gómez-Puyou
Keyword(s):  
Atp Hydrolysis ◽  
Inhibitor Protein ◽  
Submitochondrial Particles ◽  
Bovine Heart

scholarly journals The adenosine triphosphatase-inhibitor content of bovine heart submitochondrial particles. Influence of the inhibitor on adenosine triphosphate-dependent reactions

1977 ◽  
Vol 162 (2) ◽  
pp. 351-357 ◽  
Author(s):  
S J Ferguson ◽  
D A Harris ◽  
G K Radda
Keyword(s):  
Atpase Activity ◽  
Adenosine Triphosphatase ◽  
Type I ◽  
Type Ii ◽  
Inhibitor Protein ◽  
Isolation Method ◽  
Atpase Inhibitor ◽  
Submitochondrial Particles ◽  
Bovine Heart ◽  
Tightly Bound Nucleotides

1. The activity of the ATPase (adenosine triphosphatase) of phosphorylating particles prepared by sonication of bovine heart mitochondria in the presence of MgCl2 and ATP is influenced by the isolation method for the mitochondria used in the preparation of particles. Type-I particles, made from mitochondria isolated in a medium lacking succinate, have a lower ATPase activity than to Type-II particles, which are prepared from mitochondria isolated in a medium containing succinate. 2. Centrifugation under appropriate energized conditions increases the ATPase activity of Type-I particles almost to that of the Type-II particles. The ATPase activity of Type-II particles was only slightly stimulated by this procedure. These data are interpreted as indicating a higher content of the ATPase-inhibitor protein in the Type-I particles. 3. A comparison was made of the ATP-driven enhancement of 8-anilinonaphthalene-1-sulphonate fluorescence and the exchange of the endogenous tightly bound nucleotides of the ATPase in Type-I and Type-II particles. The effect of exogenous inhibitor protein on both these reactions was also studied. 4. The time-scale on which the inhibitor protein can exchange between ATPase molecules is discussed.

scholarly journals MgATP-induced inhibition of the adenosine triphosphatase activity of submitochondrial particles

1981 ◽  
Vol 196 (2) ◽  
pp. 443-449 ◽  
Author(s):  
P N Lowe ◽  
R B Beechey
Keyword(s):  
Atpase Activity ◽  
Conformational Change ◽  
Atp Hydrolysis ◽  
Hydrolytic Activity ◽  
Inhibitor Protein ◽  
Endogenous Inhibitor ◽  
Submitochondrial Particles ◽  
Hydrolysis Products ◽  
Enzyme Species ◽  
Partial Release

1. The ATP-hydrolytic activity of ox heart submitochondrial particles can be increased from 2-3 mumol/min per mg of protein to 10-12 mumol/min per mg of protein by incubation in media containing 50 mM-Na2B4O7. This process appears to be due to the partial release of inhibitor protein from the particles. 2. The ATPase activity of submitochondrial particles can be inhibited by incubation with the substrate, MgATP. This inhibition is not due to the accumulation of the hydrolysis products, MgADP and Pi, but could involve the process of ATP hydrolysis. 3. The mechanism of MgATP-induced inhibition of ATPase activity is proposed to involve a conformational change in one of the intermediate enzyme species of the ATP-hydrolytic sequence. 4. MgATP inhibits the ATPase activity of control submitochondrial particles at a higher rate and to a greater extent than it does that of inhibitor-protein-depleted submitochondrial particles, suggesting that the conformational change involves the endogenous inhibitor protein.

Binding of adenine nucleotides to the F1-inhibitor protein complex of bovine heart submitochondrial particles

Biochemistry ◽  
1992 ◽  
Vol 31 (25) ◽  
pp. 5784-5790 ◽  
Author(s):  
Orlando B. Martins ◽  
Ione Salgado-Martins ◽  
M. Angela B. Grieco ◽  
A. Gomez-Puyou ◽  
M. Tuena de Gomez-Puyou
Keyword(s):  
Protein Complex ◽  
Adenine Nucleotides ◽  
Inhibitor Protein ◽  
Submitochondrial Particles ◽  
Bovine Heart

scholarly journals Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria

1980 ◽  
Vol 191 (2) ◽  
pp. 421-427 ◽  
Author(s):  
J F Turrens ◽  
A Boveris
Keyword(s):  
Cytochrome B ◽  
Nadh Dehydrogenase ◽  
Submitochondrial Particles ◽  
Bovine Heart ◽  
Biphasic Effect ◽  
Carbonyl Cyanide ◽  
Autocatalytic Process ◽  
Ph Range ◽  
Energy Dependent ◽  
O2 Production

Submitochondrial particles from bovine heart in which NADH dehydrogenase is reduced by either addition of NADH and rotenone or by reversed electron transfer generate 0.9 +/- 0.1 nmol of O2-/min per mg of protein at pH 7.4 and at 30 degrees C. When NADH is used as substrate, rotenone, antimycin and cyanide increase O2- production. In NADH- and antimycin-supplemented submitochondrial particles, rotenone has a biphasic effect: it increases O2- production at the NADH dehydrogenase and it inhibits O2- production at the ubiquinone-cytochrome b site. The generation of O2- by the rotenone, the uncoupler carbonyl cyanide rho-trifluoromethoxyphenylhydrazone and oligomycin at concentrations similar to those required to inhibit energy-dependent succinate-NAD reductase. Cyanide did not affect O2- generation at the NADH dehydrogenase, but inhibited O2- production at the ubiquinone-cytochrome b site. Production of O2- at the NADH dehydrogenase is about 50% of the O2- generation but the ubiquinone-cytochrome b area at pH 7.4. Additivity of the two mitochondrial sites of O2- generation was observed over the pH range from 7.0 to 8.8. AN O2–dependent autocatalytic process that requires NADH, submitochondrial particles and adrenaline is described.

scholarly journals A simple and rapid method for the preparation of adenosine triphosphatase from submitochondrial particles

1975 ◽  
Vol 148 (3) ◽  
pp. 533-537 ◽  
Author(s):  
R B Beechey ◽  
S A Hubbard ◽  
P E Linnett ◽  
A D Mitchell ◽  
E A Munn
Keyword(s):  
Electron Microscopy ◽  
Rapid Method ◽  
Adenosine Triphosphatase ◽  
Pure Form ◽  
Heart Mitochondria ◽  
Polyacrylamide Gels ◽  
Submitochondrial Particles ◽  
Bovine Heart

An almost pure form of the bovine heart mitochondrial adenosine triphosphatase (ATPase) is released from the membrane by shaking submitochondrial particles with chloroform. Analyses on polyacrylamide gels and by electron microscopy, and also sensitivity to inhibitors, show that the chloroform-released enzyme is similar to other ATPase preparations from bovine heart mitochondria.

scholarly journals The inhibitor protein of the cyclic AMP-dependent protein kinase-catalytic subunit interaction. Composition of multiple complexes

1988 ◽  
Vol 256 (3) ◽  
pp. 785-789 ◽  
Author(s):  
S M Van Patten ◽  
A Hotz ◽  
V Kinzel ◽  
D A Walsh
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Catalytic Subunit ◽  
Inhibitor Protein ◽  
Multiple Forms ◽  
Subunit Interaction ◽  
Dependent Protein Kinase ◽  
Bovine Heart ◽  
Dependent Protein ◽  
Multiple Species

It has been previously demonstrated that the combination of pure preparations of the inhibitor protein of the cyclic AMP-dependent protein kinase and the catalytic subunit of this enzyme resulted in the formation of multiple complexes [Van Patten, Fletcher & Walsh (1986) J. Biol. Chem. 261, 5514-5523]. In the present study it is demonstrated that these multiple species occur because the bovine heart protein kinase preparation contains multiple forms of catalytic subunit [Kinzel, Hotz, König, Gagelmann, Pyerin, Reed, Köbler, Hofmann, Obst, Gensheimer, Goldblatt & Shaltiel (1987) Arch. Biochem. Biophys. 253, 341-349].

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