Characterization of a Peroxodiiron(III) Intermediate in the T201S Variant of Toluene/o-Xylene Monooxygenase Hydroxylase from Pseudomonas sp. OX1
We report the observation of a novel intermediate in the reaction of a reduced toluene/o-xylene monooxygenase hydroxylase (ToMOH[subscript red]) T201S variant, in the presence of a regulatory protein (ToMOD), with dioxygen. This species is the first oxygenated intermediate with an optical band in an...
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| Format: | Article |
| Language: | en_US |
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American Chemical Society (ACS)
2013
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| Online Access: | http://hdl.handle.net/1721.1/82137 https://orcid.org/0000-0002-2693-4982 |
| _version_ | 1826189666085240832 |
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| author | Song, Woon Ju Behan, Rachel K. Naik, Sunil G. Huynh, Boi Hanh Lippard, Stephen J. |
| author2 | Massachusetts Institute of Technology. Department of Chemistry |
| author_facet | Massachusetts Institute of Technology. Department of Chemistry Song, Woon Ju Behan, Rachel K. Naik, Sunil G. Huynh, Boi Hanh Lippard, Stephen J. |
| author_sort | Song, Woon Ju |
| collection | MIT |
| description | We report the observation of a novel intermediate in the reaction of a reduced toluene/o-xylene monooxygenase hydroxylase (ToMOH[subscript red]) T201S variant, in the presence of a regulatory protein (ToMOD), with dioxygen. This species is the first oxygenated intermediate with an optical band in any toluene monooxygenase. The UV−vis and Mössbauer spectroscopic properties of the intermediate allow us to assign it as a peroxodiiron(III) species, T201S[subscript peroxo], similar to H[subscript peroxo] in methane monooxygenase. Although T201S generates T201S[subscript peroxo] in addition to optically transparent ToMOH[subscript peroxo], previously observed in wild-type ToMOH, this conservative variant is catalytically active in steady-state catalysis and single-turnover experiments and displays the same regiospecificity for toluene and slightly different regiospecificity for o-xylene oxidation. |
| first_indexed | 2024-09-23T08:19:12Z |
| format | Article |
| id | mit-1721.1/82137 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T08:19:12Z |
| publishDate | 2013 |
| publisher | American Chemical Society (ACS) |
| record_format | dspace |
| spelling | mit-1721.1/821372022-09-23T12:17:12Z Characterization of a Peroxodiiron(III) Intermediate in the T201S Variant of Toluene/o-Xylene Monooxygenase Hydroxylase from Pseudomonas sp. OX1 Song, Woon Ju Behan, Rachel K. Naik, Sunil G. Huynh, Boi Hanh Lippard, Stephen J. Massachusetts Institute of Technology. Department of Chemistry Song, Woon Ju Behan, Rachel K. Lippard, Stephen J. We report the observation of a novel intermediate in the reaction of a reduced toluene/o-xylene monooxygenase hydroxylase (ToMOH[subscript red]) T201S variant, in the presence of a regulatory protein (ToMOD), with dioxygen. This species is the first oxygenated intermediate with an optical band in any toluene monooxygenase. The UV−vis and Mössbauer spectroscopic properties of the intermediate allow us to assign it as a peroxodiiron(III) species, T201S[subscript peroxo], similar to H[subscript peroxo] in methane monooxygenase. Although T201S generates T201S[subscript peroxo] in addition to optically transparent ToMOH[subscript peroxo], previously observed in wild-type ToMOH, this conservative variant is catalytically active in steady-state catalysis and single-turnover experiments and displays the same regiospecificity for toluene and slightly different regiospecificity for o-xylene oxidation. National Institute of General Medical Sciences (U.S.) (Grant GM32134) National Institute of General Medical Sciences (U.S.) (Fellowship 1 F32 GM084564-01) 2013-11-15T18:50:02Z 2013-11-15T18:50:02Z 2009-04 2009-02 Article http://purl.org/eprint/type/JournalArticle 0002-7863 1520-5126 http://hdl.handle.net/1721.1/82137 Song, Woon Ju, Rachel K. Behan, Sunil G. Naik, Boi Hanh Huynh, and Stephen J. Lippard. “Characterization of a Peroxodiiron(III) Intermediate in the T201S Variant of Toluene/o-Xylene Monooxygenase Hydroxylase from Pseudomonas sp. OX1.” Journal of the American Chemical Society 131, no. 17 (May 6, 2009): 6074-6075. https://orcid.org/0000-0002-2693-4982 en_US http://dx.doi.org/10.1021/ja9011782 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 (ACS) PMC |
| spellingShingle | Song, Woon Ju Behan, Rachel K. Naik, Sunil G. Huynh, Boi Hanh Lippard, Stephen J. Characterization of a Peroxodiiron(III) Intermediate in the T201S Variant of Toluene/o-Xylene Monooxygenase Hydroxylase from Pseudomonas sp. OX1 |
| title | Characterization of a Peroxodiiron(III) Intermediate in the T201S Variant of Toluene/o-Xylene Monooxygenase Hydroxylase from Pseudomonas sp. OX1 |
| title_full | Characterization of a Peroxodiiron(III) Intermediate in the T201S Variant of Toluene/o-Xylene Monooxygenase Hydroxylase from Pseudomonas sp. OX1 |
| title_fullStr | Characterization of a Peroxodiiron(III) Intermediate in the T201S Variant of Toluene/o-Xylene Monooxygenase Hydroxylase from Pseudomonas sp. OX1 |
| title_full_unstemmed | Characterization of a Peroxodiiron(III) Intermediate in the T201S Variant of Toluene/o-Xylene Monooxygenase Hydroxylase from Pseudomonas sp. OX1 |
| title_short | Characterization of a Peroxodiiron(III) Intermediate in the T201S Variant of Toluene/o-Xylene Monooxygenase Hydroxylase from Pseudomonas sp. OX1 |
| title_sort | characterization of a peroxodiiron iii intermediate in the t201s variant of toluene o xylene monooxygenase hydroxylase from pseudomonas sp ox1 |
| url | http://hdl.handle.net/1721.1/82137 https://orcid.org/0000-0002-2693-4982 |
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