{"id":449,"date":"2020-10-06T09:54:11","date_gmt":"2020-10-06T08:54:11","guid":{"rendered":"http:\/\/lclac.chimie.unistra.fr\/?page_id=449"},"modified":"2020-10-06T10:29:11","modified_gmt":"2020-10-06T09:29:11","slug":"strapped-porphyrins-and-hemoprotein-models","status":"publish","type":"page","link":"https:\/\/clic.chimie.unistra.fr\/?page_id=449","title":{"rendered":"Strapped Porphyrins and Hemoprotein Models"},"content":{"rendered":"

This is a long lasting research axis which started prior to the resolution of the X-ray structure of cytochrome c Oxidase in 1995.<\/span><\/p>\n

\"\"<\/span><\/p>\n

Fig. 1.<\/strong> (left) Cytochrome c oxidase (CcO) active site,1<\/sup> (center) phenanthroline strapped zinc-copper complex2<\/sup> and (right) a functional CcO model ligand in the form of a Zn complex.3<\/sup> <\/em><\/span><\/p>\n

Some thirty years ago, based on the information from EXAFS measurements on the enzyme, a phenanthroline strapped porphyrin was designed4<\/sup> to simultaneously bind zinc or iron in the porphyrin and copper in the phenanthroline. Nowadays, the phenanthroline strapped porphyrins are equipped with charged polar substituents and combined with cyclodextrins5<\/sup> for the development of water soluble hemoprotein models.6<\/sup><\/span><\/p>\n

Aside from providing several efficient mimics of cytochrome c oxidase using iron-copper complexes of the ligands represented in Figure 1 (center and right),7<\/sup> the phenanthroline strapped zinc-porphyrin has exhibited peculiar binding features that led to the development of self-assembled porphyrin wires.8<\/sup><\/span><\/p>\n

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  1. \u00ab\u00a0Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8\u00a0\u00bb A\u00a0 by Yoshikawa\u00a0<\/a>et al. Science<\/cite>, 269, 1069-1074.<\/span><\/li>\n
  2. Electrocatalytic reduction of oxygen with phenanthroline-trapped porphyrins J. Porph. Phthalocyanines<\/em> (2007), 11, 212-221.<\/a><\/span><\/li>\n
  3. Toward Generic Models of Hemoproteins Org. Lett.<\/em> (2009), 11, 2487-2490.<\/a><\/span><\/li>\n
  4. A highly rigid capped porphyrin J. Org. Chem.<\/em> (1992), 57, 1015-18.<\/a><\/span><\/li>\n
  5. Hydrogen bond directed molecular recognition in water in a strapped-porphyrin-cyclodextrin assembly J. Porph. Phthalocyanines<\/em> (2019), 23, (4\/5), 569-574<\/a><\/span><\/li>\n
  6. A water-soluble supramolecular complex that mimics the heme\/copper hetero-binuclear site of cytochrome c oxidase Chem. Sci.<\/em> (2018), 9, (7), 1989-1995;<\/a> Modelling haemoproteins: porphyrins and cyclodextrins as sources of inspiration Chem. Commun.<\/em> (Feature Article) (2019), 55, (97), 14558-14565.<\/a><\/span><\/li>\n
  7. Comparative studies in series of cytochrome c oxidase models\u00a0 J. Inorg. Biochem.<\/em> 2012, 108, 196\u2013202<\/a>; A question of flexibility in cytochrome c oxidase models Inorg. Chim. Acta<\/em> (2017), 468, 232-238. <\/a><\/span><\/li>\n
  8. From Models of Hemoproteins to Self-Assembled Molecular Wires ChemPlusChem<\/em> (2017), 82, 584-594.<\/span><\/a><\/li>\n<\/ol>\n","protected":false},"excerpt":{"rendered":"

    This is a long lasting research axis which started prior to the resolution of the X-ray structure of cytochrome c Oxidase in 1995. Fig. 1. (left) Cytochrome c oxidase (CcO)… Read More<\/a><\/span><\/p>\n","protected":false},"author":1,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-449","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/clic.chimie.unistra.fr\/index.php?rest_route=\/wp\/v2\/pages\/449","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/clic.chimie.unistra.fr\/index.php?rest_route=\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/clic.chimie.unistra.fr\/index.php?rest_route=\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/clic.chimie.unistra.fr\/index.php?rest_route=\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/clic.chimie.unistra.fr\/index.php?rest_route=%2Fwp%2Fv2%2Fcomments&post=449"}],"version-history":[{"count":6,"href":"https:\/\/clic.chimie.unistra.fr\/index.php?rest_route=\/wp\/v2\/pages\/449\/revisions"}],"predecessor-version":[{"id":490,"href":"https:\/\/clic.chimie.unistra.fr\/index.php?rest_route=\/wp\/v2\/pages\/449\/revisions\/490"}],"wp:attachment":[{"href":"https:\/\/clic.chimie.unistra.fr\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=449"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}