Inactivation of the F1-ATPase from the thermophilic bacterium PS3 by 5′-p-fluorosulfonylbenzoylinosine at 65° C is accompanied by modification of β-tyrosine-364
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference26 articles.
1. A highly stable adenosine triphosphatase from a thermophillie bacterium. Purification, properties, and reconstitution.
2. Reconstitution of the energy transformer, gate and channel subunit reassembly, crystalline ATPase and ATP synthesis
3. Subunit structure of adenosine triphosphatase. Comparison of the structure in thermophilic bacterium PS3 with those in mitochondria, chloroplasts, and Escherichia coli.
4. Characterization of the catalytic and noncatalytic ADP binding sites of the F1-ATPase from the thermophilic bacterium, PS3.
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1. ATP Synthase and the Actions of Inhibitors Utilized To Study Its Roles in Human Health, Disease, and Other Scientific Areas;Microbiology and Molecular Biology Reviews;2008-12
2. Structure and Mechanism of F0F1-Type ATP Synthases and ATPases;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
3. Insights into ATP synthase structure and function using affinity and site-specific spin labeling;Journal of Bioenergetics and Biomembranes;2000
4. Effects of magnesium ions on the relative conformation of nucleotide binding sites of F1-ATPases as studied by electron spin resonance spectroscopy.;Journal of Biological Chemistry;1994-07
5. Location of the ATP gamma-phosphate-binding sites on rat liver carbamoyl-phosphate synthetase I. Studies with the ATP analog 5'-p-fluorosulfonylbenzoyladenosine.;Journal of Biological Chemistry;1992-01
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