Adenine nucleotide-binding sites on mitochondrial F1-ATPase: Studies of the inactive complex formed upon binding ADP at a catalytic site
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference32 articles.
1. An inhibitory high affinity binding site for ADP in the oligomycin-sensitive ATPase of beef heart submitochondrial particles
2. Mg2+-Induced ADP-dependent inhibition of the ATPase activity of beef heart mitochondrial coupling factor F1
3. Modulation by divalent metal ions of the autocatalytic reactivity of adenosine triphosphatase from chloroplasts
4. The role of tightly bound ADP on chloroplast ATPase.
5. Kinetic mechanism of mitochondrial adenosine triphosphatase. Inhibition by azide and activation by sulphite
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1. High-Affinity Metal-Binding Site in Beef Heart Mitochondrial F1ATPase: An EPR Spectroscopy Study;Biochemistry;2004-09-25
2. Energy-dependent Transformation of F0·F1-ATPase in Paracoccus denitrificans Plasma Membranes;Journal of Biological Chemistry;2004-03
3. The βG156C Substitution in the F1-ATPase from the Thermophilic Bacillus PS3 Affects Catalytic Site Cooperativity by Destabilizing the Closed Conformation of the Catalytic Site;Biochemistry;2002-11-08
4. The presence of phosphate at a catalytic site suppresses the formation of the MgADP-inhibited form of F1-ATPase;European Journal of Biochemistry;2002-01
5. The Activity of the ATP Synthase from Escherichia coli Is Regulated by the Transmembrane Proton Motive Force;Journal of Biological Chemistry;2000-09
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