Rotary catalysis of F<sub>o</sub>F<sub>1</sub>-ATP synthase
نویسندگان
چکیده
منابع مشابه
Rotary catalysis of FoF1-ATP synthase
The synthesis of ATP, the key reaction of biological energy metabolism, is accomplished by the rotary motor protein; FoF1-ATP synthase (FoF1). In vivo, FoF1, located on the cell membrane, carries out ATP synthesis by using the proton motive force. This heterologous energy conversion is supposed to be mediated by the mechanical rotation of FoF1; however, it still remained unclear. Recently, we d...
متن کاملThe rotary mechanism of ATP synthase.
Since 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. Recently, significant progress has been made towards establishing the complete structure of ATP synthase and revea...
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Adenosine triphosphate (ATP) synthase contains a rotary motor involved in biological energy conversion. Its membrane-embedded F0 sector has a rotation generator fueled by the proton-motive force, which provides the energy required for the synthesis of ATP by the F1 domain. An electron density map obtained from crystals of a subcomplex of yeast mitochondrial ATP synthase shows a ring of 10 c sub...
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ATP synthaseÑalso called FoF1 ATPase, or simply F-ATPaseÑis the universal protein that terminates oxidative phosphorylation by synthesizing ATP from ADP and phosphate. Nearly identical proteins are found in eukaryotic mitochondria and bacteria, and they all operate on the same principle. Electron driven ion pumps set up concentration and electrical gradients across a membrane. ATP synthase util...
متن کاملCoupling H(+) transport to rotary catalysis in F-type ATP synthases: structure and organization of the transmembrane rotary motor.
H(+)-transporting F(1)F(o)-type ATP synthases utilize a transmembrane H(+) potential to drive ATP formation by a rotary catalytic mechanism. ATP is formed in alternating beta subunits of the extramembranous F(1) sector of the enzyme, synthesis being driven by rotation of the gamma subunit in the center of the F(1) molecule between the alternating catalytic sites. The H(+) electrochemical potent...
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ژورنال
عنوان ژورنال: BIOPHYSICS
سال: 2013
ISSN: 1349-2942
DOI: 10.2142/biophysics.9.51