Current Challenges for Modeling Enzyme Active Sites by Biomimetic Synthetic Diiron Complexes
This 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,...
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| Format: | Article |
| Language: | en_US |
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Royal Society of Chemistry
2011
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| Online Access: | http://hdl.handle.net/1721.1/64760 https://orcid.org/0000-0002-2693-4982 |
| _version_ | 1826191493428150272 |
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| author | Friedle, Simone Reisner, Erwin Lippard, Stephen J. |
| author2 | Massachusetts Institute of Technology. Department of Chemistry |
| author_facet | Massachusetts Institute of Technology. Department of Chemistry Friedle, Simone Reisner, Erwin Lippard, Stephen J. |
| author_sort | Friedle, Simone |
| collection | MIT |
| description | This 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. |
| first_indexed | 2024-09-23T08:56:44Z |
| format | Article |
| id | mit-1721.1/64760 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T08:56:44Z |
| publishDate | 2011 |
| publisher | Royal Society of Chemistry |
| record_format | dspace |
| spelling | mit-1721.1/647602022-09-26T09:22:58Z Current Challenges for Modeling Enzyme Active Sites by Biomimetic Synthetic Diiron Complexes Current challenges of modeling diiron enzyme active sites for dioxygen activation by biomimetic synthetic complexes Friedle, Simone Reisner, Erwin Lippard, Stephen J. Massachusetts Institute of Technology. Department of Chemistry Lippard, Stephen J. Lippard, Stephen J. Friedle, Simone Reisner, Erwin This 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. National Institute of General Medical Sciences (U.S.) (grant GM032134) Engineering and Physical Sciences Research Council (EP/H00338X/1) 2011-07-07T15:14:22Z 2011-07-07T15:14:22Z 2010-05 2010-02 Article http://purl.org/eprint/type/JournalArticle 1460-4744 0306-0012 http://hdl.handle.net/1721.1/64760 Friedle, 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. https://orcid.org/0000-0002-2693-4982 en_US http://dx.doi.org/10.1039/C003079C Chemical Society Reviews Creative Commons Attribution-Noncommercial-Share Alike 3.0 http://creativecommons.org/licenses/by-nc-sa/3.0/ application/pdf Royal Society of Chemistry Prof. Lippard via Erja Kajosalo |
| spellingShingle | Friedle, Simone Reisner, Erwin Lippard, Stephen J. Current Challenges for Modeling Enzyme Active Sites by Biomimetic Synthetic Diiron Complexes |
| title | Current Challenges for Modeling Enzyme Active Sites by Biomimetic Synthetic Diiron Complexes |
| title_full | Current Challenges for Modeling Enzyme Active Sites by Biomimetic Synthetic Diiron Complexes |
| title_fullStr | Current Challenges for Modeling Enzyme Active Sites by Biomimetic Synthetic Diiron Complexes |
| title_full_unstemmed | Current Challenges for Modeling Enzyme Active Sites by Biomimetic Synthetic Diiron Complexes |
| title_short | Current Challenges for Modeling Enzyme Active Sites by Biomimetic Synthetic Diiron Complexes |
| title_sort | current challenges for modeling enzyme active sites by biomimetic synthetic diiron complexes |
| url | http://hdl.handle.net/1721.1/64760 https://orcid.org/0000-0002-2693-4982 |
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