Document Detail

The interaction of N,N'-dicyclohexylcarbodiimide with chloroplast coupling factor 1.
MedLine Citation:
PMID:  6444296     Owner:  NLM     Status:  MEDLINE    
1. Incubation of soluble spinach Coupling Factor 1 (CF1) with dicyclohexylcarbodiimide (DCCD) results in the inactivation of the ATPase. The DCCD inactivation is time- and concentration-dependent. Complete inactivation of the CF1-ATPase activity requires the binding of 2 mol of DCCD/mol of CF1. The binding sites of DCCD are located on the beta subunit of CF1. 2. DCCD modification of soluble CF1 eliminates one adenine nucleotide binding site which is exposed by dithiothreitol activation or by incubation with tentoxin. The inactivation of both the ATPase activity and the adenine nucleotide binding site are pH-dependent. The inactivation of both the ATPase activity and the adenine nucleotide binding site are pH-dependent. Half-maximal inhibition occurs at about pH 7.5. 3. The DCCD-modified CF1, reconstituted with EDTA-treated chloroplasts, is fully active is restoring proton uptake but not in restoring ATP synthesis or light-dependent adenine nucleotide exchange.
V Shoshan; B R Selman
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  255     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1980 Jan 
Date Detail:
Created Date:  1980-03-24     Completed Date:  1980-03-24     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  384-9     Citation Subset:  IM    
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MeSH Terms
Adenosine Triphosphatases / metabolism
Adenylyl Imidodiphosphate / pharmacology
Binding Sites
Macromolecular Substances
Plants / enzymology
Protein Binding
Proton-Translocating ATPases* / metabolism
Reg. No./Substance:
0/Carbodiimides; 0/Macromolecular Substances; 25612-73-1/Adenylyl Imidodiphosphate; 538-75-0/Dicyclohexylcarbodiimide; EC 3.6.1.-/Adenosine Triphosphatases; EC ATPases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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