Results 301 to 310 of about 329,086 (345)
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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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ATP synthase: structure-function relationships
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1992Recent work has focused on obtaining a better understanding of the three-dimensional structural relationships between the alpha and beta subunits of the F1 moiety and the location of nucleotide binding domains within these subunits. Four types of approach are currently being pursued: X-ray crystallographic, chemical, molecular biological and ...
P J, Thomas +5 more
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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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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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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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2004
F1-F= ATP synthases are large protein complexes located in the inner mitochondrial membrane,in the chloroplast thylakoid membrane and in the bacterial plasma membrane. They are the major ATP suppliers of most cells. Structural, biochemical and molecular biological studies have contributed to the knowledge of the architecture and catalytic mechanism of ...
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F1-F= ATP synthases are large protein complexes located in the inner mitochondrial membrane,in the chloroplast thylakoid membrane and in the bacterial plasma membrane. They are the major ATP suppliers of most cells. Structural, biochemical and molecular biological studies have contributed to the knowledge of the architecture and catalytic mechanism of ...
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Assaying ATP Synthase Rotor Activity
2006With the development of laser excitation and detection systems, it has become possible to consider analyses that have otherwise been beyond the capacity of experimentalists. In this investigation, a case is made for the development of a device to analyse ATP synthase activity in-vivo.
Maguire, D, Shah, J, McCabe, M
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Biophysical studies on ATP synthase
Advances in Biophysics, 1999The isolation of ATP synthase (F0F1) (82) and F0 (83) 34 years ago finally revealed that F0F1 is a motor composed of F0 (ion-motor, abc subunits) and F1 (ATP-motor, alpha 3 beta 3 gamma delta epsilon subunits) (Fig. 1). The single molecule videotape (4, 5, 65, 66) revealed that gamma epsilon axis of F1 rotates counterclockwise, proceeds by each 2 pi/3 ...
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Chemical & Engineering News Archive, 2001
By observing a gold bead attached to the rotor of the energy-converting enzyme ATP synthase, Japanese researchers have found that the rotor takes two steps per hydrolysis cycle [Nature, 410,898 (2001)]. The results will help "solve the mechanism of this highly efficient, reversible motor," says Ryohei Yasuda, a physicist at Teikyo University ...
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By observing a gold bead attached to the rotor of the energy-converting enzyme ATP synthase, Japanese researchers have found that the rotor takes two steps per hydrolysis cycle [Nature, 410,898 (2001)]. The results will help "solve the mechanism of this highly efficient, reversible motor," says Ryohei Yasuda, a physicist at Teikyo University ...
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