{"id":708,"date":"2026-04-15T13:25:29","date_gmt":"2026-04-15T13:25:29","guid":{"rendered":"https:\/\/citations.tools.bio-logic.fr\/?p=708"},"modified":"2026-04-15T13:25:29","modified_gmt":"2026-04-15T13:25:29","slug":"reduction-of-ferric-haemoproteins-by-tetrahydropterins-a-kinetic-study","status":"publish","type":"post","link":"https:\/\/citations.tools.bio-logic.fr\/?p=708","title":{"rendered":"Reduction of ferric haemoproteins by tetrahydropterins: a kinetic study"},"content":{"rendered":"<h4>DOI:<\/h4>\n<p><a href=\"https:\/\/doi.org\/10.1042\/bj20050437\" target=\"_blank\" rel=\"noopener\">10.1042\/bj20050437<\/a><\/p>\n<h4>Authors:<\/h4>\n<p>Chantal Capeill\u00e8re\u2010Blandin, Delphine Mathieu, Daniel Mansuy<\/p>\n<h4>Abstract:<\/h4>\n<p>We previously showed that one-electron transfer from tetrahydropterins to iron porphyrins is a very general reaction, with formation of an intermediate cation radical similar to the one detected in NO synthase. As a model reaction, the rates of reduction of eight haemoproteins by diMePH4 (6,7-dimethyltetrahydropterin) have been studied and correlated with their one-electron reduction potentials, E(m) (Fe(III)\/Fe(II)). On the basis of kinetic data analyses, a bimolecular collisional mechanism is proposed for the electron transfer from diMePH4 to ferrihaemoproteins. Haemoproteins with reduction potentials below -160 mV were shown not to be reduced by diMePH4 to the corresponding ferrohaemoproteins. For haemoproteins with reduction potentials more positive than -160 mV, such as chloroperoxidase, cytochrome b5, methaemoglobin and cytochrome c, there was a good correlation between the second-order reduction rate constant and the redox potential, E(m) (Fe(III)\/Fe(II)): [formula: see text]. The rate of reduction of cytochrome c by BH4 [(6R)-5,6,7,8-tetrahydrobiopterin] was determined to be similar to that of the reduction of cytochrome c by diMePH4. These results confirm the role of tetrahydropterins as one-electron donors to Fe(III) porphyrins.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>DOI: 10.1042\/bj20050437 Authors: Chantal Capeill\u00e8re\u2010Blandin, Delphine Mathieu, Daniel Mansuy Abstract: We previously showed that one-electron transfer from tetrahydropterins to iron porphyrins is a very general reaction, with formation of an intermediate cation radical similar to the one detected in NO synthase. As a model reaction, the rates of reduction of eight haemoproteins by diMePH4 (6,7-dimethyltetrahydropterin) [&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-708","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\/708","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=708"}],"version-history":[{"count":0,"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=\/wp\/v2\/posts\/708\/revisions"}],"wp:attachment":[{"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=708"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=%2Fwp%2Fv2%2Fcategories&post=708"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=%2Fwp%2Fv2%2Ftags&post=708"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}