Adenosine triphosphatase and nucleotide binding activity of isolated beta-subunit preparations from Escherichia coli F1F0-ATP synthase.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference44 articles.
1. Complete kinetic and thermodynamic characterization of the unisite catalytic pathway of Escherichia coli F1-ATPase. Comparison with mitochondrial F1-ATPase and application to the study of mutant enzymes.
2. Kinetic characterization of the unisite catalytic pathway of seven β-subunit mutant F1-ATPases from Escherichia coli
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1. Assembly of the Escherichia coli FoF1 ATP synthase involves distinct subcomplex formation;Biochemical Society Transactions;2013-09-23
2. Subunit δ Is the Key Player for Assembly of the H+-translocating Unit of Escherichia coli FOF1 ATP Synthase;Journal of Biological Chemistry;2013-09
3. Two ATPases;Journal of Biological Chemistry;2012-08
4. Role of short conserved segments of α- and β-subunits that link F1-ATPase catalytic and noncatalytic sites;Biochemistry (Moscow);2010-01
5. Catalysis by isolated β-subunits of the ATP Synthase/ATPase from Thermophilic bacillus PS3. Hydrolysis of Pyrophosphate;Journal of Bioenergetics and Biomembranes;2008-12
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