Document Detail

Sulphydryl groups in photosynthetic energy conservation. IV. Inhibition of the ATPase of chloroplast coupling factor 1 by sulphydryl reagents.
MedLine Citation:
PMID:  137745     Owner:  NLM     Status:  MEDLINE    
1. O-Iodosobenzoate and 2,2'-dithio bis-(5-nitropyridine) inhibited by about fifty per cent the ATPase activity of heat-activated chloroplast coupling factor 1 only when present during the heating but were without effect when added before or after the activation. Reversion of this inhibition was only obtained by a second heat treatment with 10 mM dithioerythritol. 2. The inhibition of the Ca2+-ATPase of coupling factor 1 by o-iodosobenzoate or 2,2'-dithio bis-(5-nitropyridine) was not additive with similar inhibitions obtained with the alkylating reagents iodoacetamide and N-ethylmaleimide. 3. The heat-activated ATPase of o-iodosobenzoate-treated coupling factor 1 had a higher Km for ATP, without modification of V. The modified enzyme was desensitized against the allosteric inhibitor ADP.
R H Vallejos; R A Ravizzini; C S Andreo
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  459     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1977 Jan 
Date Detail:
Created Date:  1977-03-31     Completed Date:  1977-03-31     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  20-6     Citation Subset:  IM    
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MeSH Terms
Adenosine Triphosphatases / metabolism*
Calcium / pharmacology
Chloroplasts / drug effects,  enzymology*
Disulfides / pharmacology
Enzyme Activation / drug effects
Iodobenzoates / pharmacology*
Nitro Compounds / pharmacology*
Photosynthesis / drug effects*
Plant Proteins / metabolism*
Pyridines / pharmacology*
Reg. No./Substance:
0/Disulfides; 0/Iodobenzoates; 0/Nitro Compounds; 0/Plant Proteins; 0/Pyridines; 7440-70-2/Calcium; EC 3.6.1.-/Adenosine Triphosphatases

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