| Blocking one non-catalytic ADP binding site results in complete inhibition of the F-type ATPase from the thermophilic Bacillus PS3. | |
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MedLine Citation:
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PMID: 8695629 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The F-type ATPase, TF0F1, from the thermophilic Bacillus PS3, which is free of nucleotides after isolation, was specifically loaded with one 2-azido ADP on a non-catalytic site. The enzyme was covalently modified to various extents and the rate of ATP synthesis and ATP hydrolysis was measured. Both ATP synthesis and ATP hydrolysis extrapolated to zero for covalently binding one nucleotide per enzyme. This was interpreted such that the non-catalytic sites are involved in the coupled catalytic process. |
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Authors:
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P Richard |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: 1275 ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 1996 Jul |
Date Detail:
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Created Date: 1996-09-05 Completed Date: 1996-09-05 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 141-4 Citation Subset: IM |
Affiliation:
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Département de Biologie Cellulaire et Moléculaire, CEA Saclay, Gif-sur-Yvette, France. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adenosine Diphosphate
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metabolism Affinity Labels Amino Acid Sequence Azides Bacillus / enzymology* Bacterial Proteins / metabolism Bacteriorhodopsins / metabolism Binding Sites Biological Transport, Active Enzyme Inhibitors / pharmacology Kinetics Liposomes Membranes, Artificial Molecular Sequence Data Proton-Translocating ATPases / antagonists & inhibitors*, chemistry, metabolism |
| Chemical | |
Reg. No./Substance:
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0/Affinity Labels; 0/Azides; 0/Bacterial Proteins; 0/Enzyme Inhibitors; 0/Liposomes; 0/Membranes, Artificial; 53026-44-1/Bacteriorhodopsins; 58-64-0/Adenosine Diphosphate; EC 3.6.3.14/Proton-Translocating ATPases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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