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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1978-2-18
|
| pubmed:abstractText |
1. The synthesis of dibutylchloromethyltin chloride, a new covalent inhibitor of the mitochondrial ATP synthase [oligomycin-sensitive ATPase (adenosine triphosphatase)] complex is described, together with a method for preparing dibutylchloro[(3)H]methyltin chloride. 2. Studies with the yeast mitochondrial oligomycin-sensitive ATPase complex show that dibutylchloromethyltin chloride inhibits both the membrane-bound enzyme and also the purified Triton X-100-dispersed preparation. 3. F(1)-ATPase is not inhibited even at 500nmol of dibutylchloromethyltin chloride/mg of protein, and the general inhibitory properties are similar to those of triethyltin, oligomycin and dicyclohexylcarbodi-imide, known energy-transfer inhibitors of oxidative phosphorylation. 4. Binding studies with yeast submitochondrial particles show that dibutylchloromethyltin chloride antagonizes the binding of triethyl[(113)Sn]tin, indicating that there is an interaction between the two inhibitor-binding sites. 5. Unlike triethyltin, inhibition by dibutylchloromethyltin chloride is due to a covalent interaction which titrates a component of the inner mitochondrial membrane present at a concentration of 8-9nmol/mg of protein. 6. All of the labelled component can be extracted with chloroform/methanol (2:1, v/v), and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis of the chloroform/methanol extract indicates that the labelled component has an apparent mol.wt. of 6000-8000. However, t.l.c. reveals the presence of only one labelled component which is lipophilic and non-protein and is distinct from the free inhibitor, mitochondrial phospholipids and the dicyclohexylcarbodi-imide-binding protein (subunit 9). 7. Inhibition of mitochondrial ATPase and oxidative phosphorylation is correlated with specific interaction with a non-protein lipophilic component of the mitochondrial inner membrane which is proposed to be a co-factor or intermediate of oxidative phosphorylation.
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| pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-125200,
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-126152,
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-13269376,
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-13667399,
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-138419,
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-141273,
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-14228485,
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-142482,
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-14272657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-180003,
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-187465,
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-238835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-330275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-4220923,
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-4234148,
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-4256832,
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-4294775,
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-5073753,
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-5158902,
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-5451902,
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-5472149,
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-5806584,
http://linkedlifedata.com/resource/pubmed/commentcorrection/145860-814874
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| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0264-6021
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
166
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
593-602
|
| pubmed:dateRevised |
2009-11-18
|
| pubmed:meshHeading | |
| pubmed:year |
1977
|
| pubmed:articleTitle |
Dibutylchloromethyltin chloride, a covalent inhibitor of the adenosine triphosphate synthase complex.
|
| pubmed:publicationType |
Journal Article
|