Carboxylate as the Protonation Site in (Peroxo)diiron(III) Model Complexes of Soluble Methane Monooxygenase and Related Diiron Proteins
Dioxygen activation by carboxylate-bridged diiron enzymes is involved in essential biological processes ranging from DNA synthesis and hydrocarbon metabolism to cell proliferation.1-3 The carboxylate-bridged diiron superfamily of proteins includes ribonucleotide reductase (RNR),4 Δ9 desaturase,5...
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| Format: | Article |
| Language: | en_US |
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American Chemical Society
2011
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| Online Access: | http://hdl.handle.net/1721.1/64759 https://orcid.org/0000-0002-2693-4982 |
| _version_ | 1826210187795496960 |
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| author | Do, Loi Hung Hayashi, Takahiro Moenne-Loccoz, Pierre Lippard, Stephen J. |
| author2 | Massachusetts Institute of Technology. Department of Chemistry |
| author_facet | Massachusetts Institute of Technology. Department of Chemistry Do, Loi Hung Hayashi, Takahiro Moenne-Loccoz, Pierre Lippard, Stephen J. |
| author_sort | Do, Loi Hung |
| collection | MIT |
| description | Dioxygen activation by carboxylate-bridged diiron enzymes
is involved in essential biological processes ranging from DNA
synthesis and hydrocarbon metabolism to cell proliferation.1-3
The carboxylate-bridged diiron superfamily of proteins includes
ribonucleotide reductase (RNR),4 Δ9 desaturase,5 bacterial
multicomponent monooxygenases (BMMs),6,7 and most recently
human deoxyhypusine hydroxylase (hDOHH).3 In all of these
systems, the O2 reduction step proceeds through a (peroxo)-
diiron(III) intermediate in which the resulting peroxo ligand is
proposed to bridge two iron atoms in a μ-1,2 or μ-η2η2
coordination mode.8-10 Extensive studies of soluble methane
monooxygenase (sMMO), a BMM family member that oxidizes
methane to methanol, reveal that the generation and activation
of Fe2O2 units requires protons.11,12 Given the complexity of
protein environments, identifying the sites involved in such
proton translocation processes and their effect on O2 activation
is not a trivial undertaking. |
| first_indexed | 2024-09-23T14:45:18Z |
| format | Article |
| id | mit-1721.1/64759 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T14:45:18Z |
| publishDate | 2011 |
| publisher | American Chemical Society |
| record_format | dspace |
| spelling | mit-1721.1/647592022-09-29T10:21:20Z Carboxylate as the Protonation Site in (Peroxo)diiron(III) Model Complexes of Soluble Methane Monooxygenase and Related Diiron Proteins Do, Loi Hung Hayashi, Takahiro Moenne-Loccoz, Pierre Lippard, Stephen J. Massachusetts Institute of Technology. Department of Chemistry Lippard, Stephen J. Do, Loi Hung Lippard, Stephen J. Dioxygen activation by carboxylate-bridged diiron enzymes is involved in essential biological processes ranging from DNA synthesis and hydrocarbon metabolism to cell proliferation.1-3 The carboxylate-bridged diiron superfamily of proteins includes ribonucleotide reductase (RNR),4 Δ9 desaturase,5 bacterial multicomponent monooxygenases (BMMs),6,7 and most recently human deoxyhypusine hydroxylase (hDOHH).3 In all of these systems, the O2 reduction step proceeds through a (peroxo)- diiron(III) intermediate in which the resulting peroxo ligand is proposed to bridge two iron atoms in a μ-1,2 or μ-η2η2 coordination mode.8-10 Extensive studies of soluble methane monooxygenase (sMMO), a BMM family member that oxidizes methane to methanol, reveal that the generation and activation of Fe2O2 units requires protons.11,12 Given the complexity of protein environments, identifying the sites involved in such proton translocation processes and their effect on O2 activation is not a trivial undertaking. National Institute of General Medical Sciences (U.S.) (grant GM032134) National Institute of General Medical Sciences (U.S.) (grant GM74785) 2011-07-07T15:01:15Z 2011-07-07T15:01:15Z 2010-01 2009-11 Article http://purl.org/eprint/type/JournalArticle 0002-7863 1520-5126 http://hdl.handle.net/1721.1/64759 Do, Loi H. et al. “Carboxylate as the Protonation Site in (Peroxo)diiron(III) Model Complexes of Soluble Methane Monooxygenase and Related Diiron Proteins.” Journal of the American Chemical Society 132.4 (2010) : 1273-1275. https://orcid.org/0000-0002-2693-4982 en_US http://dx.doi.org/10.1021/ja909718f Journal of the American Chemical Society Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. application/pdf American Chemical Society Prof. Lippard via Erja Kajosalo |
| spellingShingle | Do, Loi Hung Hayashi, Takahiro Moenne-Loccoz, Pierre Lippard, Stephen J. Carboxylate as the Protonation Site in (Peroxo)diiron(III) Model Complexes of Soluble Methane Monooxygenase and Related Diiron Proteins |
| title | Carboxylate as the Protonation Site in (Peroxo)diiron(III) Model Complexes of Soluble Methane Monooxygenase and Related Diiron Proteins |
| title_full | Carboxylate as the Protonation Site in (Peroxo)diiron(III) Model Complexes of Soluble Methane Monooxygenase and Related Diiron Proteins |
| title_fullStr | Carboxylate as the Protonation Site in (Peroxo)diiron(III) Model Complexes of Soluble Methane Monooxygenase and Related Diiron Proteins |
| title_full_unstemmed | Carboxylate as the Protonation Site in (Peroxo)diiron(III) Model Complexes of Soluble Methane Monooxygenase and Related Diiron Proteins |
| title_short | Carboxylate as the Protonation Site in (Peroxo)diiron(III) Model Complexes of Soluble Methane Monooxygenase and Related Diiron Proteins |
| title_sort | carboxylate as the protonation site in peroxo diiron iii model complexes of soluble methane monooxygenase and related diiron proteins |
| url | http://hdl.handle.net/1721.1/64759 https://orcid.org/0000-0002-2693-4982 |
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