Document Detail

Blocking one non-catalytic ADP binding site results in complete inhibition of the F-type ATPase from the thermophilic Bacillus PS3.
MedLine Citation:
PMID:  8695629     Owner:  NLM     Status:  MEDLINE    
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.
P Richard
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1275     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1996 Jul 
Date Detail:
Created Date:  1996-09-05     Completed Date:  1996-09-05     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  141-4     Citation Subset:  IM    
Département de Biologie Cellulaire et Moléculaire, CEA Saclay, Gif-sur-Yvette, France.
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MeSH Terms
Adenosine Diphosphate / metabolism
Affinity Labels
Amino Acid Sequence
Bacillus / enzymology*
Bacterial Proteins / metabolism
Bacteriorhodopsins / metabolism
Binding Sites
Biological Transport, Active
Enzyme Inhibitors / pharmacology
Membranes, Artificial
Molecular Sequence Data
Proton-Translocating ATPases / antagonists & inhibitors*,  chemistry,  metabolism
Reg. No./Substance:
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 ATPases

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