Notes on the Mechanism of ATP Synthesis |
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Authors: | M. A. Bianchet Peter L. Pedersen L. Mario Amzel |
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Affiliation: | (1) Department of Biophysics and Biophysical Chemistry, Johns Hopkins School of Medicine, Baltimore, Maryland, 21205;(2) Department of Biophysics and Biophysical Chemistry, Johns Hopkins School of Medicine, Baltimore, Maryland, 21205 |
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Abstract: | The most commonly quoted mechanism of the coupling between the electrochemical proton gradient and the formation of ATP from ADP and Pi assumes that all states of the F1 portion of the ATP synthase have subunits in tight, loose, and open conformations. Models based on this assumption are inconsistent with some of the available experimental evidence. A mechanism that includes an additional subunit conformation, closed, observed in the rat liver structure overcomes these difficulties. |
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Keywords: | F1— ATPase ATP synthesis conformational changes |
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