{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,13]],"date-time":"2026-02-13T14:39:22Z","timestamp":1770993562114,"version":"3.50.1"},"reference-count":21,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2001,11,14]],"date-time":"2001-11-14T00:00:00Z","timestamp":1005696000000},"content-version":"vor","delay-in-days":2949,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["FEBS Letters"],"published-print":{"date-parts":[[1993,10,18]]},"abstract":"<jats:p>The interaction of ascorbate with different heme iron redox states of myoglobin (ferrylmyoglobin, Fe<jats:sup>IV<\/jats:sup>=O; metmyoglobin, Fe<jats:sup>III<\/jats:sup>; and oxymyoglobin Fe<jats:sup>II<\/jats:sup>O<jats:sub>2<\/jats:sub>) was examined by e.s.r. and absorption spectroseopy. The reaction of ascorbate with ferryl\u2010 or met\u2010myoglobin resulted in ascorbyl radical production. The interaction of ascorbate with oxymyoglobin proceeded with formation of ascorbyl radical, hydrogen peroxide, and an overall oxidation of oxymyoglobin to metmyoglobin. The latter reaction proceeded via an oxoferryl complex intermediate \u2010 corresponding to ferrylmyoglobin and identified by treatment of the reaction mixture with Na<jats:sub>2<\/jats:sub>S. These observations are consistent with a concerted electron transfer mechanism, whereby the two electrons required for the reduction of oxygen to hydrogen peroxide are donated by ascorbic acid and the heme iron. The antioxidant and prooxidant aspects of these redox transitions are discussed in terms of their kinetic properties.<\/jats:p>","DOI":"10.1016\/0014-5793(93)80651-a","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T09:09:11Z","timestamp":1027588151000},"page":"287-290","source":"Crossref","is-referenced-by-count":97,"title":["The reaction of ascorbic acid with different heme iron redox states of myoglobin"],"prefix":"10.1002","volume":"332","author":[{"given":"Cecilia","family":"Giulivi","sequence":"first","affiliation":[]},{"given":"Enrique","family":"Cadenas","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2001,11,14]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj0520511"},{"key":"e_1_2_1_3_1","first-page":"233","volume":"88","author":"King N.K.","year":"1967","journal-title":"Biochim. Biophys. 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