{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T00:14:31Z","timestamp":1791850471699,"version":"4.3.4"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1980,11,1]]},"abstract":"<jats:p>Submitochondrial particles from bovine heart in which NADH dehydrogenase is reduced by either addition of NADH and rotenone or by reversed electron transfer generate 0.9 +\/- 0.1 nmol of O2-\/min per mg of protein at pH 7.4 and at 30 degrees C. When NADH is used as substrate, rotenone, antimycin and cyanide increase O2- production. In NADH- and antimycin-supplemented submitochondrial particles, rotenone has a biphasic effect: it increases O2- production at the NADH dehydrogenase and it inhibits O2- production at the ubiquinone-cytochrome b site. The generation of O2- by the rotenone, the uncoupler carbonyl cyanide rho-trifluoromethoxyphenylhydrazone and oligomycin at concentrations similar to those required to inhibit energy-dependent succinate-NAD reductase. Cyanide did not affect O2- generation at the NADH dehydrogenase, but inhibited O2- production at the ubiquinone-cytochrome b site. Production of O2- at the NADH dehydrogenase is about 50% of the O2- generation but the ubiquinone-cytochrome b area at pH 7.4. Additivity of the two mitochondrial sites of O2- generation was observed over the pH range from 7.0 to 8.8. AN O2\u2013dependent autocatalytic process that requires NADH, submitochondrial particles and adrenaline is described.<\/jats:p>","DOI":"10.1042\/bj1910421","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T20:24:57Z","timestamp":1439238297000},"page":"421-427","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":1275,"title":["Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria"],"prefix":"10.1042","volume":"191","author":[{"given":"J F","family":"Turrens","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A","family":"Boveris","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/191\/2\/421\/575334\/bj1910421.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/191\/2\/421\/575334\/bj1910421.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,25]],"date-time":"2021-11-25T14:12:19Z","timestamp":1637849539000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/191\/2\/421\/17773\/Generation-of-superoxide-anion-by-the-NADH"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1980,11,1]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1980,11,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj1910421","relation":{},"ISSN":["0264-6021"],"issn-type":[{"value":"0264-6021","type":"print"}],"subject":[],"published":{"date-parts":[[1980,11,1]]}}}