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Difference between revisions of "Walker 1994 Curr Opin Struct Biol"

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(Created page with "{{Publication |title=Walker JE (1994) The regulation of catalysis in ATP synthase. Curr Opin Struct Biol 4:912-8. |info=[https://pubmed.ncbi.nlm.nih.gov/7712295/ PMID:7712295...")
 
 
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|abstract=ATP synthase is regulated so as to prevent futile hydrolysis of ATP when the transmembrane proton electrochemical gradient, delta mu H+, falls. Mitochondria and chloroplasts have different mechanisms for inhibition of ATP synthase: by binding an inhibitor protein, and by stabilization of the ADP-inhibited state by making an intramolecular disulphide bond, respectively. The recently determined structure of bovine F1-ATPase is locked in a conformation that probably represents the ADP-inhibited state of the enzyme.
|abstract=ATP synthase is regulated so as to prevent futile hydrolysis of ATP when the transmembrane proton electrochemical gradient, delta mu H+, falls. Mitochondria and chloroplasts have different mechanisms for inhibition of ATP synthase: by binding an inhibitor protein, and by stabilization of the ADP-inhibited state by making an intramolecular disulphide bond, respectively. The recently determined structure of bovine F1-ATPase is locked in a conformation that probably represents the ADP-inhibited state of the enzyme.
}}
}}
== Cited by ==
{{Template:Cited by Komlodi 2022 MitoFit pmF}}
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Latest revision as of 09:18, 5 April 2022

Publications in the MiPMap
Walker JE (1994) The regulation of catalysis in ATP synthase. Curr Opin Struct Biol 4:912-8.

» PMID:7712295 Open Access

Walker JE (1994) Curr Opin Struct Biol

Abstract: ATP synthase is regulated so as to prevent futile hydrolysis of ATP when the transmembrane proton electrochemical gradient, delta mu H+, falls. Mitochondria and chloroplasts have different mechanisms for inhibition of ATP synthase: by binding an inhibitor protein, and by stabilization of the ADP-inhibited state by making an intramolecular disulphide bond, respectively. The recently determined structure of bovine F1-ATPase is locked in a conformation that probably represents the ADP-inhibited state of the enzyme.

Cited by

  • Komlódi et al (2022) The protonmotive force - not merely membrane potential. MitoFit Preprints 2022 (in prep)

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MitoFit 2022 pmF