Deleting the IF 1 -like ζ subunit from Paracoccus denitrificans ATP synthase is not sufficient to activate ATP hydrolysis.
Autor: | Varghese F; The Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Wellcome Trust/MRC Building, Biomedical Campus, Hills Road, Cambridge CB2 0XY, UK., Blaza JN; The Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Wellcome Trust/MRC Building, Biomedical Campus, Hills Road, Cambridge CB2 0XY, UK., Jones AJY; The Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Wellcome Trust/MRC Building, Biomedical Campus, Hills Road, Cambridge CB2 0XY, UK., Jarman OD; The Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Wellcome Trust/MRC Building, Biomedical Campus, Hills Road, Cambridge CB2 0XY, UK., Hirst J; The Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Wellcome Trust/MRC Building, Biomedical Campus, Hills Road, Cambridge CB2 0XY, UK jh@mrc-mbu.cam.ac.uk. |
---|---|
Jazyk: | angličtina |
Zdroj: | Open biology [Open Biol] 2018 Jan; Vol. 8 (1). |
DOI: | 10.1098/rsob.170206 |
Abstrakt: | In oxidative phosphorylation, ATP synthases interconvert two forms of free energy: they are driven by the proton-motive force across an energy-transducing membrane to synthesize ATP and displace the ADP/ATP ratio from equilibrium. For thermodynamically efficient energy conversion they must be reversible catalysts. However, in many species ATP synthases are unidirectional catalysts (their rates of ATP hydrolysis are negligible), and in others mechanisms have evolved to regulate or minimize hydrolysis. Unidirectional catalysis by Paracoccus denitrificans ATP synthase has been attributed to its unique ζ subunit, which is structurally analogous to the mammalian inhibitor protein IF (© 2018 The Authors.) |
Databáze: | MEDLINE |
Externí odkaz: |