Results 261 to 270 of about 191,822 (304)
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ATP regeneration by thermostable ATP synthase
Biotechnology and Bioengineering, 1996We investigated the possibility of using thermostable ATP synthase (TF(0)F(1)) for a new ATP regeneration method. TF(0)F(1) was purified from a thermophilic bacterium, PS3, and reconstituted into liposomes. ATP synthesis experiments showed that TF(0)F(1) liposomes could synthesize ATP in micromole concentrations by acid-base change.
K Y, Nam, D K, Struck, M T, Holtzapple
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Synthesis and hydrolysis of ATP by the mitochondrial ATP synthase
Biochemistry and Cell Biology, 1988A brief summary of the factors that control synthesis and hydrolysis of ATP by the mitochondrial H+-ATP synthase is made. Particular emphasis is placed on the role of the natural ATPase inhibitor protein. It is clear from the existing data obtained with a number of agents that there is no correlation between variations of the rate of ATP hydrolysis ...
M T, Tuena Gómez-Puyou +2 more
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Biology Bulletin Reviews, 2021
This review presents a collection and analysis of the currently available data on the structure and organization, localization, working mechanisms, and functions of the enzyme that synthesizes adenosine triphosphate (ATP), ATP synthase. It is universal (present in all prokaryotic and eukaryotic cells) in nature and is unique in its characteristics. The
E. V. Uzlova, S. M. Zimatkin
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This review presents a collection and analysis of the currently available data on the structure and organization, localization, working mechanisms, and functions of the enzyme that synthesizes adenosine triphosphate (ATP), ATP synthase. It is universal (present in all prokaryotic and eukaryotic cells) in nature and is unique in its characteristics. The
E. V. Uzlova, S. M. Zimatkin
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ATP Synthase: The machine that makes ATP
Current Biology, 1994The recently determined crystal structure of the F1 part of mitochondrial ATP synthase provides new insights into the workings of one of the most remarkable and complex biochemical machines.
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Energy transduction in ATP synthase
Nature, 1998Mitochondria, bacteria and chloroplasts use the free energy stored in transmembrane ion gradients to manufacture ATP by the action of ATP synthase. This enzyme consists of two principal domains. The asymmetric membrane-spanning F0 portion contains the proton channel, and the soluble F1 portion contains three catalytic sites which cooperate in the ...
T, Elston, H, Wang, G, Oster
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Current Opinion in Structural Biology, 2018
ATP synthases are rotary enzymes found in bacteria, chloroplasts, and mitochondria. These complexes produce the majority of cellular ATP in aerobic cells using energy from the transmembrane proton motive force established by the electron transport chain.
Hui Guo, John L Rubinstein
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ATP synthases are rotary enzymes found in bacteria, chloroplasts, and mitochondria. These complexes produce the majority of cellular ATP in aerobic cells using energy from the transmembrane proton motive force established by the electron transport chain.
Hui Guo, John L Rubinstein
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Structure and genes of ATP synthase
Biochemical Society Transactions, 1987ATP synthase (proton-translocating ATPase, H + -ATPase, F, F, ATPase) is a component of the cytoplasmic membrane of eubacteria, the thylakoid membrane of chloroplasts and the inner membrane of mitochondria. The Escherichia coli enzyme the simplest so far defined, is a complex of eight different polypeptides; five of them, M , f i , 7, 6 and E ...
J E, Walker +5 more
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The rotary mechanism of ATP synthase
Current Opinion in Structural Biology, 2000Since the chemiosmotic theory was proposed by Peter Mitchell in the 1960s, a major objective has been to elucidate the mechanism of coupling of the transmembrane proton motive force, created by respiration or photosynthesis, to the synthesis of ATP from ADP and inorganic phosphate.
D, Stock +4 more
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Trends in Biochemical Sciences, 1997
ATP synthase (F0F1-ATPase) uses proton- or sodium-motive force to produce ATP form ADP and P(i). Three lines of experiment have recently demonstrated large-scale intersubunit rotation during ATP hydrolysis by F1. We discuss how ion flow through the membrane-intrinsic portion, F0, may generate torque and how this might be transmitted between stator and ...
Junge, Wolfgang +2 more
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ATP synthase (F0F1-ATPase) uses proton- or sodium-motive force to produce ATP form ADP and P(i). Three lines of experiment have recently demonstrated large-scale intersubunit rotation during ATP hydrolysis by F1. We discuss how ion flow through the membrane-intrinsic portion, F0, may generate torque and how this might be transmitted between stator and ...
Junge, Wolfgang +2 more
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The Saccharomyces cerevisiae ATP Synthase
Journal of Bioenergetics and Biomembranes, 2000The ATP synthase of the yeast Saccharomyces cerevisiae is composed of 20 different subunits whose primary structure is known. The organization of proteins that constitute the membranous domain is now under investigation. Cysteine insertions combined with the use of nonpermeant maleimide reagents and cross-linking reagents showing different lengths and ...
J, Velours, G, Arselin
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