F1-ATPase-catalyzed synthesis of ATP from oleoylphosphate and ADP.
نویسندگان
چکیده
Purified preparations of F1-ATPase (ATP phosphohydrolase; EC 3.6.1.3) isolated from yeast mitochondria catalyze the reaction of oleoylphosphate with ADP to yield ATP and oleic acid. Formation of ATP is specifically inhibited by the F1-ATPase inhibitor 1799 and by dinitrophenol. In the presence of F1, dinitrophenol "uncouples" the synthase reaction by causing rapid hydrolysis of oleoylphosphate without ATP formation. It is proposed that this F1 catalyzed ATP synthesis reaction corresponds to the terminal chemical step in oxidative phosphorylation.
منابع مشابه
STUDIES OF NUCLEOTIDE BINDING SITES, BOUND AUROVERTIN FLUORESCENCE, AND LABELING OF ESSENTIAL RESIDUES OF THE PURIFIED FI-ATPase*
The Escherichia coli uncA gene codes for the a subunit of the F1-sector of the membrane proton-ATPase. Mutations in this gene cause loss of ATPase and ATP synthesis activity and, in some instances, derangement of F1 structure. From three mutants (uncA401, uncA453, and uncA447), an F1 of normal size and subunit structure may be purified. In this work, purified soluble F1 from these three mutants...
متن کاملATP synthesis catalyzed by the mitochondrial F1-F0 ATP synthase is not a reversal of its ATPase activity.
The ADP(Mg2+)-deactivated oligomycin-sensitive F1-F0 ATPase of coupled submitochondrial particles treated with the substoichiometric amount of oligomycin was studied to test whether ATP synthesis and hydrolysis proceed in either direction through the same intermediates. The initial rates of ATP hydrolysis, oxidative phosphorylation, ATP-dependent, succinate-supported NAD+ reduction, and ATP-ind...
متن کاملRemoval of "tightly bound" nucleotides from soluble mitochondrial adenosine triphosphatase (F1).
Soluble mitochondrial ATPase (F1) from beef heart prepared in this laboratory contained approximately 1.8 mol of ADP and 0 mol of ATP/mol of F1 which were not removed by repeated precipitation of the enzyme with ammonium sulfate solution or by gel filtration in low ionic strength buffer containing EDTA. This enzyme had full coupling activity. Treatment of the enzyme with trypsin (5 mug/mg of F1...
متن کاملCatalysis of partial reactions of ATP synthesis by beef heart mitochondrial adenosine triphosphatase.
We have found that when the ATP hydrolysis activity of beef heart mitochondrial adenosine triphosphatase (F1) is eliminated by either cold treatment or chemical modification, the enzyme attains the ability to catalyze the Pi in equilibrium ATP exchange reaction. The ATP hydrolysis activity of isolated F1 was lost upon chemical modification by phenyglyoxal, butanedione, or 7-chloro-4-nitrobenzen...
متن کاملControlled rotation of the F1-ATPase reveals differential and continuous binding changes for ATP synthesis
F(1)-ATPase is an ATP-driven rotary molecular motor that synthesizes ATP when rotated in reverse. To elucidate the mechanism of ATP synthesis, we imaged binding and release of fluorescently labelled ADP and ATP while rotating the motor in either direction by magnets. Here we report the binding and release rates for each of the three catalytic sites for 360° of the rotary angle. We show that the...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 74 11 شماره
صفحات -
تاریخ انتشار 1977