{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,15]],"date-time":"2026-09-15T20:21:44Z","timestamp":1789503704707,"version":"build-2803163510"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1977,9,15]]},"abstract":"<jats:p>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[3H]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. F1-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[113Sn]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\u20139nmol\/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\u20138000. 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.<\/jats:p>","DOI":"10.1042\/bj1660593","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T20:08:11Z","timestamp":1439237291000},"page":"593-602","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":41,"title":["Dibutylchloromethyltin chloride, a covalent inhibitor of the adenosine triphosphate synthase complex"],"prefix":"10.1042","volume":"166","author":[{"given":"Kelvin","family":"Cain","sequence":"first","affiliation":[{"name":"Department of Molecular Sciences, University of Warwick, Coventry CV4 7AL, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael D.","family":"Partis","sequence":"additional","affiliation":[{"name":"Department of Molecular Sciences, University of Warwick, Coventry CV4 7AL, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David E.","family":"Griffiths","sequence":"additional","affiliation":[{"name":"Department of Molecular Sciences, University of Warwick, Coventry CV4 7AL, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/166\/3\/593\/569548\/bj1660593.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/166\/3\/593\/569548\/bj1660593.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,26]],"date-time":"2021-11-26T17:51:53Z","timestamp":1637949113000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/166\/3\/593\/11686\/Dibutylchloromethyltin-chloride-a-covalent"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1977,9,15]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1977,9,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj1660593","relation":{},"ISSN":["0264-6021"],"issn-type":[{"value":"0264-6021","type":"print"}],"subject":[],"published":{"date-parts":[[1977,9,15]]}}}