{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,28]],"date-time":"2026-03-28T03:12:51Z","timestamp":1774667571212,"version":"3.50.1"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1991,6,15]]},"abstract":"<jats:p>Attack by hydroxyl radicals (.OH) upon salicylate (2-hydroxybenzoate) leads to formation of both 2,3-dihydroxybenzoate (2,3-DHB) and 2,5-dihydroxybenzoate (gentisate, 2,5-DHB). It has been suggested that formation of 2,3-DHB from salicylate is a means of monitoring .OH formation. Production of 2,3-DHB and 2,5-DHB by liver microsomal fractions and isoforms of cytochrome P-450 was investigated. Liver microsomes prepared from variously treated rats and rabbits catalysed the formation of 2,5-DHB but not 2,3-DHB. Formation of 2,5-DHB was inhibited by CO, metyrapone and SKF-525A, but not by the .OH scavengers mannitol and formate or by the iron chelator desferrioxamine. Purified P-450s IIE1, IIB4 or IA2 from rabbit liver microsomes, reconstituted together with NADPH-cytochrome P-450 reductase, led to formation of equal amounts of 2,3-DHB and 2,5-DHB in reactions that were almost completely inhibited by mannitol or formate. Addition of Fe3+\/EDTA either to microsomes or to membranes containing reconstituted P-450 caused formation of approximately equal amounts of 2,3-DHB and 2,5-DHB, consistent with an .OH-dependent attack on salicylate. The data indicate that the microsomal P-450 system catalyses hydroxylation of salicylate to 2,5-DHB, but not formation of 2,3-DHB. Hence measurement of 2,3-DHB might provide a means of monitoring .OH formation. Care must be taken in studies of substrate hydroxylation by microsomes or reconstituted P-450 systems to avoid artefacts resulting from .OH generation.<\/jats:p>","DOI":"10.1042\/bj2760753","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:21:36Z","timestamp":1439241696000},"page":"753-757","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":113,"title":["Hydroxylation of salicylate by microsomal fractions and cytochrome <i>P<\/i>-450. Lack of production of 2,3-dihydroxybenzoate unless hydroxyl radical formation is permitted"],"prefix":"10.1042","volume":"276","author":[{"given":"M","family":"Ingelman-Sundberg","sequence":"first","affiliation":[{"name":"Department of Physiological Chemistry, Karolinska Institutet, S-10401 Stockholm, Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"H","family":"Kaur","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of London King's College, Strand Campus, London WC2R 2LS, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Y","family":"Terelius","sequence":"additional","affiliation":[{"name":"Department of Physiological Chemistry, Karolinska Institutet, S-10401 Stockholm, Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J O","family":"Persson","sequence":"additional","affiliation":[{"name":"Department of Physiological Chemistry, Karolinska Institutet, S-10401 Stockholm, Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"B","family":"Halliwell","sequence":"additional","affiliation":[{"name":"Division of Pulmonary-Critical Care Medicine, University of California, Davis Medical Center, 4301 X Street, Rm 2120, Sacramento, CA 95817, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/276\/3\/753\/603461\/bj2760753.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/276\/3\/753\/603461\/bj2760753.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,23]],"date-time":"2021-11-23T15:14:58Z","timestamp":1637680498000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/276\/3\/753\/26910\/Hydroxylation-of-salicylate-by-microsomal"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1991,6,15]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1991,6,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj2760753","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1991,6,15]]}}}