Energization of the membrane prevents the formation of tight inactive complexes of ATPase with MgADP in submitochondrial particles
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(89)81013-0/fullpdf
Reference12 articles.
1. Regulation of H+-ATPases in oxidative- and photophosphorylation
2. Regulation of the mitochondrial ATP synthase/ATPase complex
3. Three adenine nucleotide binding sites in F1-F0mitochondrial ATPase as revealed by presteady-state and steady-state kinetics of ATP hydrolysis Evidence for two inhibitory ADP-specific noncatalytic sites
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1. The effect of amphiphilic compounds on the secretion of levansucrase by Zymomonas mobilis;Process Biochemistry;2005-12
2. Enzyme turnover is essential for deactivation of F0F1-ATPase in plant mitochondria;Biochimica et Biophysica Acta (BBA) - Bioenergetics;1995-04
3. Adenine nucleotide-binding sites on mitochondrial F1-ATPase: Studies of the inactive complex formed upon binding ADP at a catalytic site;Archives of Biochemistry and Biophysics;1992-06
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