Bioenergetic Processes of Cyanobacteria 2011
DOI: 10.1007/978-94-007-0388-9_10
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ATP Synthase: Structure, Function and Regulation of a Complex Machine

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Cited by 4 publications
(4 citation statements)
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“…7). Some bacteria use this reversed reaction to transport protons for maintaining the PMF under low oxygen conditions [27]. The F1-ATPase molecule, 8 nm in diameter and 14 nm in length, is capable of producing; 80 to 100 pN of rotary torque [11,12].…”
Section: Comparison Of Molecular Motorsmentioning
confidence: 99%
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“…7). Some bacteria use this reversed reaction to transport protons for maintaining the PMF under low oxygen conditions [27]. The F1-ATPase molecule, 8 nm in diameter and 14 nm in length, is capable of producing; 80 to 100 pN of rotary torque [11,12].…”
Section: Comparison Of Molecular Motorsmentioning
confidence: 99%
“…F1 subunit synthesize ATP when γ shaft rotates clockwise, but interestingly this enzyme subunit gives reversible rotation (anti-clockwise) of γ shaft by consuming hydrolyzing ATP separately (Fig.7). Some bacteria use this reversed reaction to transport protons for maintaining the PMF under low oxygen conditions [27]. The F1-ATPase molecule, 8 nm in diameter and 14 nm in length, is capable of producing; 80 to 100 pN of rotary torque [11,12].…”
Section: Comparison Of Molecular Motorsmentioning
confidence: 99%
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“…ATP synthase is the smallest rotary motor and is embedded in membranes. In bacteria it is located on the cytoplasmic membrane whereas in eukaryotes it is embedded in the membrane of specialized organalles called mitochondria (in animal cells) and chloroplasts (in plant cells) [1848,1849,1850,1851,1852,1853,1854,1855,1856,1857,1858,1859,1861] (see appendix E for a brief introduction to these organelles and ref. [1862,1863] for the history of the discovery of ATP synthase and its mechanism from the personal perspective of some of leading contributors).…”
Section: Rotary Motor F 0 F 1 -Atpasementioning
confidence: 99%