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
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(88)80085-1/fullpdf
Reference28 articles.
1. Subunit structure of adenosine triphosphatase. Comparison of the structure in thermophilic bacterium PS3 with those in mitochondria, chloroplasts, and Escherichia coli.
2. The number and localisation of adenine nucleotide-binding sites in beef-heart mitochondrial ATPase (F1) determined by photolabelling with 8-azido-ATP and 8-azido-ADP
3. Identification of the Nucleotide-Binding Site for ATP Synthesis and Hydrolysis in Mitochondrial Soluble F1-ATPase1
4. Demonstration of two exchangeable non-catalytic and two cooperative catalytic sites in isolated bovine heart mitochondrial F1, using the photoaffinity labels [2-3H]8-azido-ATP and [2-3H]8-azido-ADP
5. Adenine nucleotide-binding sites on beef heart F1-ATPase. Conditions that affect occupancy of catalytic and noncatalytic sites.
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1. Energy-dependent Transformation of F0·F1-ATPase in Paracoccus denitrificans Plasma Membranes;Journal of Biological Chemistry;2004-03
2. The use of HPLC for the Study of Chloroplast ATPase Enzymatic Activity and ATP Binding;Journal of Liquid Chromatography & Related Technologies;1998-07
3. Nucleotide binding sites on beef heart mitochondrial F1-ATPase. Cooperative interactions between sites and specificity of noncatalytic sites.;Journal of Biological Chemistry;1993-11
4. Nucleotide/H+-dependent change in Mg2+affinity at the ATPase inhibitory site of the mitochondrial F1-F0ATP synthase;FEBS Letters;1993-08-09
5. Adenine nucleotide binding at a noncatalytic site of mitochondrial F1-ATPase accelerates a magnesium- and ADP-dependent inactivation during ATP hydrolysis;Biochemistry;1992-12
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