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dc.contributor.authorFriedle, Simone
dc.contributor.authorReisner, Erwin
dc.contributor.authorLippard, Stephen J.
dc.date.accessioned2011-07-07T15:14:22Z
dc.date.available2011-07-07T15:14:22Z
dc.date.issued2010-05
dc.date.submitted2010-02
dc.identifier.issn1460-4744
dc.identifier.issn0306-0012
dc.identifier.urihttp://hdl.handle.net/1721.1/64760
dc.description.abstractThis tutorial review describes recent progress in modeling the active sites of carboxylate-rich non-heme diiron enzymes that activate dioxygen to carry out several key reactions in Nature. The chemistry of soluble methane monooxygenase, which catalyzes the selective oxidation of methane to methanol, is of particular interest for (bio)technological applications. Novel synthetic diiron complexes that mimic structural, and, to a lesser extent, functional features of these diiron enzymes are discussed. The chemistry of the enzymes is also briefly summarized. A particular focus of this review is on models that mimic characteristics of the diiron systems that were previously not emphasized, including systems that contain (i) aqua ligands, (ii) different substrates tethered to the ligand framework, (iii) dendrimers attached to carboxylates to mimic the protein environment, (iv) two N-donors in a syn-orientation with respect to the iron–iron vector, and (v) a N-rich ligand environment capable of accessing oxygenated high-valent diiron intermediates.en_US
dc.description.sponsorshipNational Institute of General Medical Sciences (U.S.) (grant GM032134)en_US
dc.description.sponsorshipEngineering and Physical Sciences Research Council (EP/H00338X/1)en_US
dc.language.isoen_US
dc.publisherRoyal Society of Chemistryen_US
dc.relation.isversionofhttp://dx.doi.org/10.1039/C003079Cen_US
dc.rightsCreative Commons Attribution-Noncommercial-Share Alike 3.0en_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/en_US
dc.sourceProf. Lippard via Erja Kajosaloen_US
dc.titleCurrent Challenges for Modeling Enzyme Active Sites by Biomimetic Synthetic Diiron Complexesen_US
dc.title.alternativeCurrent challenges of modeling diiron enzyme active sites for dioxygen activation by biomimetic synthetic complexesen_US
dc.typeArticleen_US
dc.identifier.citationFriedle, Simone, Erwin Reisner, and Stephen J. Lippard. “Current Challenges of Modeling Diiron Enzyme Active Sites for Dioxygen Activation by Biomimetic Synthetic Complexes.” Chem. Soc. Rev. 39.8 (2010) : 2768-2779.en_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Chemistryen_US
dc.contributor.approverLippard, Stephen J.
dc.contributor.mitauthorLippard, Stephen J.
dc.contributor.mitauthorFriedle, Simone
dc.contributor.mitauthorReisner, Erwin
dc.relation.journalChemical Society Reviewsen_US
dc.eprint.versionAuthor's final manuscripten_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsFriedle, Simone; Reisner, Erwin; Lippard, Stephen J.en
dc.identifier.orcidhttps://orcid.org/0000-0002-2693-4982
mit.licenseOPEN_ACCESS_POLICYen_US
mit.metadata.statusComplete


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