{"id":760,"date":"2026-04-15T13:22:38","date_gmt":"2026-04-15T13:22:38","guid":{"rendered":"https:\/\/citations.tools.bio-logic.fr\/?p=760"},"modified":"2026-04-15T13:22:38","modified_gmt":"2026-04-15T13:22:38","slug":"the-millisecond-intermediate-in-the-reaction-of-nitric-oxide-with-oxymyoglobin-is-an-ironiii%e2%88%92nitrato-complex-not-a-peroxynitrite","status":"publish","type":"post","link":"https:\/\/citations.tools.bio-logic.fr\/?p=760","title":{"rendered":"The Millisecond Intermediate in the Reaction of Nitric Oxide with Oxymyoglobin is an Iron(III)\u2212Nitrato Complex, Not a Peroxynitrite"},"content":{"rendered":"<h4>DOI:<\/h4>\n<p><a href=\"https:\/\/doi.org\/10.1021\/ja9026924\" target=\"_blank\" rel=\"noopener\">10.1021\/ja9026924<\/a><\/p>\n<h4>Authors:<\/h4>\n<p>Erik T. Yukl, Simon de Vries, Pierre Mo\u00ebnne\u2010Loccoz<\/p>\n<h4>Abstract:<\/h4>\n<p>The dioxygenation of nitric oxide by oxyheme in globin proteins is a major route for NO detoxification in aerobic biological systems. In myoglobin, this reaction is thought to proceed through an iron(III)-bound peroxynitrite before homolytic cleavage of the O-O bond to form an iron(IV)-oxo and NO(2) radical followed by recombination and nitrate production. Single turnover experiments at alkaline pH have revealed the presence of a millisecond high-spin heme intermediate. It is widely presumed that this species is an iron(III)-peroxynitrite species, but detailed characterization of the intermediate is lacking. Using resonance Raman spectroscopy and rapid-freeze quench techniques, we identify the millisecond intermediate as an iron(III)-nitrato complex with a symmetric NO(2) stretch at 1282 cm(-1). Greater time resolution techniques will be required to detect the putative iron(III) peroxynitrite complex.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>DOI: 10.1021\/ja9026924 Authors: Erik T. Yukl, Simon de Vries, Pierre Mo\u00ebnne\u2010Loccoz Abstract: The dioxygenation of nitric oxide by oxyheme in globin proteins is a major route for NO detoxification in aerobic biological systems. In myoglobin, this reaction is thought to proceed through an iron(III)-bound peroxynitrite before homolytic cleavage of the O-O bond to form an [&hellip;]<\/p>\n","protected":false},"author":1,"featured_media":0,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[5],"tags":[],"class_list":["post-760","post","type-post","status-publish","format-standard","hentry","category-freeze-quench"],"_links":{"self":[{"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=\/wp\/v2\/posts\/760","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=%2Fwp%2Fv2%2Fcomments&post=760"}],"version-history":[{"count":0,"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=\/wp\/v2\/posts\/760\/revisions"}],"wp:attachment":[{"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=760"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=%2Fwp%2Fv2%2Fcategories&post=760"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=%2Fwp%2Fv2%2Ftags&post=760"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}