Adenosine triphosphatase mitochondrial

Mitochondria (45-56) are organelles possessing a double membrane, the inner of which is invaginated as cristae. An intermembrane space exists between the inner and outer membranes. The inner membrane consists of an unusually high amount of protein and possesses spherically shaped particles approx 9 nm in diameter. These particles appear to be equivalent to F0, Fb and adenosine triphosphatase. In contrast to the inner membrane, the outer membrane is smooth and appears to be connected to the smooth er. This membrane is permeable to all molecules of 10,000 Dalton or less. A mitochondrial matrix is enclosed by the inner membrane and consists of a ground substance of particles, nucleoids, ribosomes, and electron-transparent regions containing DNA. 

Mitchell, P., and J. Moyle, Stoichiometry of proton translocation through the respiratory chain and adenosine triphosphatase systems of rat liver mitochondria. Nature 208 147, 1965. The initial observations that electron transport moves protons outward across the mitochondrial inner membrane and that ATP hydrolysis does the same. 

Schistocephalus solidus has its plerocercoid stage in an ectotherm (the fish Gasterosteus aculeatus) and its adult stage in an endoderm (a fish-eating bird) and it serves as an excellent model for the study of temperature adaptation in parasites. Walker Barrett (922,923) have studied the effect of temperature on (a) the activities of the mitochondrial enzyme adenosine triphosphatase (ATPase) and (b) the physical state of mitochondrial membranes in adult and larval S. solidus. 

C.C. O Neal, P.D. Boyer, Assessment of the rate of bound substrate interconversion and of ATP acceleration of product release during catalysis by mitochondrial adenosine triphosphatase. J. Biol. Chem. 259, 5761-5767 (1984) R. Kagawa, M.G. Montgomery, K. Braig, A.G.W. Leshe, J.E. Walker, The structure of bovine Fi-ATPase inhibited by ADP and beryllium fluoride. EMBO J. 23, 2734-2744 (2004)... 

P5. Pennington, R. J., Biochemistry of dystrophic muscle mitochondrial succinate-tetrazolium reductase and adenosine triphosphatase. Biochem. J. 80, 649-654 (1961). 

Shannon, C., Enns, R., Wheelis, L., Burchiel, K., Criddle, R.S. Alterations in mitochondrial adenosine triphosphatase activity resulting from mutation of mitochondrial deoxyribonucleic acid. J. biol. Chem. 248, 3004-3011(1973)... 

A discussion of all the enzymes known to be associated with the nucleus is unnecessary for the purposes of this text however, it might be valuable to review the nuclear association of some hydrolytic enzymes. The presence of adenosine triphosphatase in the nucleus remains controversial. Although some investigators found it in large amounts, none was present in the nuclear preparations of others but since dinitro-phenol, which activates mitochondrial adenosine triphosphatase, has no effect on the nuclear enzyme, it seems that nuclear adenosine triphosphatase is different from the mitochondrial enzyme. The association of phosphorylase with the nucleus is also puzzling it is not clear what part the enzyme plays in the synthesis or breakdown of nuclear glycogen. 

B. Inhibition of Mitochondrial Proton FoFi-Adenosine Triphosphatase... 

Perlin, D.S., Murant, R.S., Gibson, S.L., and HUf, R., Effects of photosensitization by hematoporphyrin derivative on mitochondrial adenosine triphosphatase-mediated proton transport and membrane integrity of R3230AC mammary adenocarcinoma. Cancer Res., 45,653, 1995. 

Ohta S, Tsuboi M, Yoshida M and Kagawa Y (1980) Inter subunit interaction in proton translocating adenosine triphosphatase as revealed by hydrogen exchange kinetics. Biochemistry 19t 2160-2164. Pullman ME and Monroy GC (1963) A naturally occuring inhibitor of mitochondrial adenosine triphosphtase, J. Biol. Chem. 238, 3762-3769. Rott R and Nelson N (1981) Purification and immunological properties of proton ATPase complexes from yeast and rat liver mitochondria, J. Biol. Chem. 256, 9224-9228. 

Tod RD and Douglas MG (1981) A model for the structure of the yeast mitochondrial adenosine triphosphatase complex, J. Biol. Chem. 256, 6984-6989. 

PENEFSKY H. (1977) Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase, J. Biol. Chem., 252, 2891-2899. 

Schatz G, Penefsky HS, Racker E (1967) Partial resolution of the enzymes catalyzing oxidative phosphorylation XIV Interaction of purified mitochondrial adenosine triphosphatase from Bakers yeast with submitochondrial particles from beef heart. J. Biol. Chem. 242,2552-2560... 

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