{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T11:34:51Z","timestamp":1773660891685,"version":"3.50.1"},"reference-count":30,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2000,2,23]],"date-time":"2000-02-23T00:00:00Z","timestamp":951264000000},"content-version":"vor","delay-in-days":1843,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["FEBS Letters"],"published-print":{"date-parts":[[1995,2,6]]},"abstract":"<jats:p>2\u2010<jats:italic>n<\/jats:italic>\u2010Heptyl4\u2010hydroxyquinoline\u2010<jats:italic>N<\/jats:italic>\u2010oxide (HOQNO) inhibits the succinate:quinone oxidoreductase activity of isolated and membrane\u2010bound succinate:menaquinone oxidoreductase of <jats:italic>B. subtilis<\/jats:italic>. The inhibition pattern resembles closely that observed for \u03b1\u2010thenoyltrifluoroacetone and carboxins in the mitochondrial succinate:ubiquinone oxidoreductase: ca. 90% of the activity is highly sensitive to HOQNO (<jats:italic>K<\/jats:italic>\n<jats:sub>\n<jats:italic>i<\/jats:italic>\n<\/jats:sub> ca. 0.2 \u03bcM for the isolated enzyme) whereas the rest 10% proves to be resistant to the inhibitor. HOQNO binding is shown to perturb the absorption spectrum of the ferrous di\u2010heme cytochrome <jats:italic>b<\/jats:italic> of the <jats:italic>B. subtilis<\/jats:italic> succinate:quinone oxidoreductase both in the \u03b1 and Soret bands. In addition, the inhibitor is shown to bring about a negative shift of <jats:italic>E<\/jats:italic>\n<jats:sub>m<\/jats:sub> of the low\u2010potential heme <jats:italic>b<\/jats:italic>. It is suggested that HOQNO interacts with a menasemiquinone binding site near the low\u2010potential heme and suppresses the MQ<jats:sup>.\u2212<\/jats:sup>\u2010to\u2010MQH<jats:sub>2<\/jats:sub> step of the quinone reductase reaction but allows partly for the MQ\u2010to\u2010MQ<jats:sup>.\u2212<\/jats:sup> transition to occur; dismutation of MQ<jats:sup>.<\/jats:sup> formed in the latter reaction to MQ and MQH<jats:sub>2<\/jats:sub> may account for the 10% of the enzyme activity insensitive to HOQNO.<\/jats:p>","DOI":"10.1016\/0014-5793(94)01442-4","type":"journal-article","created":{"date-parts":[[2003,5,19]],"date-time":"2003-05-19T17:32:55Z","timestamp":1053365575000},"page":"23-26","source":"Crossref","is-referenced-by-count":67,"title":["HOQNO interaction with cytochrome <i>b<\/i> in succinate:menaquinone oxidoreductase from <i>Bacillus subtilis<\/i>"],"prefix":"10.1002","volume":"359","author":[{"given":"Irina A.","family":"Smirnova","sequence":"first","affiliation":[]},{"given":"Cecilia","family":"H\u00e4gerh\u00e4ll","sequence":"additional","affiliation":[]},{"given":"Alexandre A.","family":"Konstantinov","sequence":"additional","affiliation":[]},{"given":"Lars","family":"Hederstedt","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2000,2,23]]},"reference":[{"key":"e_1_2_1_2_1","first-page":"229","volume-title":"Chemistry and Biochemistry of Flavoenzymes","author":"Ackrell B.A.C.","year":"1992"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0167-7306(08)60175-1"},{"key":"e_1_2_1_4_1","volume-title":"PhD Thesis","author":"Hagerhall C.","year":"1994"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00147a028"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/0003-9861(77)90220-X"},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/0006-2952(60)90094-0"},{"key":"e_1_2_1_8_1","first-page":"375","volume":"50","author":"Grivennikova V.G.","year":"1985","journal-title":"Biochemistry (Moscow)"},{"key":"e_1_2_1_9_1","first-page":"586","volume":"21","author":"Ruuge E.K.","year":"1976","journal-title":"Bophysics (Moscow)"},{"key":"e_1_2_1_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(77)80946-0"},{"key":"e_1_2_1_11_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj1640617"},{"key":"e_1_2_1_12_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj1920769"},{"key":"e_1_2_1_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0005-2728(05)80213-0"},{"key":"e_1_2_1_14_1","doi-asserted-by":"publisher","DOI":"10.1007\/978-3-642-46158-3_24"},{"key":"e_1_2_1_15_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(85)81120-0"},{"key":"e_1_2_1_16_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(82)80611-X"},{"key":"e_1_2_1_17_1","first-page":"241","volume-title":"Biochim. 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