Electron Transfer Control in Soluble Methane Monooxygenase
The hydroxylation or epoxidation of hydrocarbons by bacterial multicomponent monooxygenases (BMMs) requires the interplay of three or four protein components. How component protein interactions control catalysis, however, is not well understood. In particular, the binding sites of the reductase comp...
| Main Authors: | , , , , |
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| Other Authors: | |
| Format: | Article |
| Language: | en_US |
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American Chemical Society (ACS)
2015
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| Online Access: | http://hdl.handle.net/1721.1/97492 https://orcid.org/0000-0002-2693-4982 |
| _version_ | 1811090182944849920 |
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| author | Wang, Weixue Iacob, Roxana E. Luoh, Rebecca P. Engen, John R. Lippard, Stephen J. |
| author2 | Massachusetts Institute of Technology. Department of Biological Engineering |
| author_facet | Massachusetts Institute of Technology. Department of Biological Engineering Wang, Weixue Iacob, Roxana E. Luoh, Rebecca P. Engen, John R. Lippard, Stephen J. |
| author_sort | Wang, Weixue |
| collection | MIT |
| description | The hydroxylation or epoxidation of hydrocarbons by bacterial multicomponent monooxygenases (BMMs) requires the interplay of three or four protein components. How component protein interactions control catalysis, however, is not well understood. In particular, the binding sites of the reductase components on the surface of their cognate hydroxylases and the role(s) that the regulatory proteins play during intermolecular electron transfer leading to the hydroxylase reduction have been enigmatic. Here we determine the reductase binding site on the hydroxylase of a BMM enzyme, soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath). We present evidence that the ferredoxin domain of the reductase binds to the canyon region of the hydroxylase, previously determined to be the regulatory protein binding site as well. The latter thus inhibits reductase binding to the hydroxylase and, consequently, intermolecular electron transfer from the reductase to the hydroxylase diiron active site. The binding competition between the regulatory protein and the reductase may serve as a control mechanism for regulating electron transfer, and other BMM enzymes are likely to adopt the same mechanism. |
| first_indexed | 2024-09-23T14:36:54Z |
| format | Article |
| id | mit-1721.1/97492 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T14:36:54Z |
| publishDate | 2015 |
| publisher | American Chemical Society (ACS) |
| record_format | dspace |
| spelling | mit-1721.1/974922022-09-29T09:56:10Z Electron Transfer Control in Soluble Methane Monooxygenase Wang, Weixue Iacob, Roxana E. Luoh, Rebecca P. Engen, John R. Lippard, Stephen J. Massachusetts Institute of Technology. Department of Biological Engineering Massachusetts Institute of Technology. Department of Chemistry Wang, Weixue Luoh, Rebecca P. Lippard, Stephen J. The hydroxylation or epoxidation of hydrocarbons by bacterial multicomponent monooxygenases (BMMs) requires the interplay of three or four protein components. How component protein interactions control catalysis, however, is not well understood. In particular, the binding sites of the reductase components on the surface of their cognate hydroxylases and the role(s) that the regulatory proteins play during intermolecular electron transfer leading to the hydroxylase reduction have been enigmatic. Here we determine the reductase binding site on the hydroxylase of a BMM enzyme, soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath). We present evidence that the ferredoxin domain of the reductase binds to the canyon region of the hydroxylase, previously determined to be the regulatory protein binding site as well. The latter thus inhibits reductase binding to the hydroxylase and, consequently, intermolecular electron transfer from the reductase to the hydroxylase diiron active site. The binding competition between the regulatory protein and the reductase may serve as a control mechanism for regulating electron transfer, and other BMM enzymes are likely to adopt the same mechanism. National Institutes of Health (U.S.) (Grant GM032134) Waters Corporation 2015-06-22T14:10:58Z 2015-06-22T14:10:58Z 2014-06 2014-05 Article http://purl.org/eprint/type/JournalArticle 0002-7863 1520-5126 http://hdl.handle.net/1721.1/97492 Wang, Weixue, Roxana E. Iacob, Rebecca P. Luoh, John R. Engen, and Stephen J. Lippard. “Electron Transfer Control in Soluble Methane Monooxygenase.” Journal of the American Chemical Society 136, no. 27 (July 9, 2014): 9754–62. © 2014 American Chemical Society https://orcid.org/0000-0002-2693-4982 en_US http://dx.doi.org/10.1021/ja504688z 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) American Chemical Society |
| spellingShingle | Wang, Weixue Iacob, Roxana E. Luoh, Rebecca P. Engen, John R. Lippard, Stephen J. Electron Transfer Control in Soluble Methane Monooxygenase |
| title | Electron Transfer Control in Soluble Methane Monooxygenase |
| title_full | Electron Transfer Control in Soluble Methane Monooxygenase |
| title_fullStr | Electron Transfer Control in Soluble Methane Monooxygenase |
| title_full_unstemmed | Electron Transfer Control in Soluble Methane Monooxygenase |
| title_short | Electron Transfer Control in Soluble Methane Monooxygenase |
| title_sort | electron transfer control in soluble methane monooxygenase |
| url | http://hdl.handle.net/1721.1/97492 https://orcid.org/0000-0002-2693-4982 |
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