Structure and mechanism of the alkane-oxidizing enzyme AlkB
Abstract Alkanes are the most energy-rich form of carbon and are widely dispersed in the environment. Their transformation by microbes represents a key step in the global carbon cycle. Alkane monooxygenase (AlkB), a membrane-spanning metalloenzyme, converts straight chain alkanes to alcohols in the...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2023-04-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-023-37869-z |
| _version_ | 1827961161774006272 |
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| author | Xue Guo Jianxiu Zhang Lei Han Juliet Lee Shoshana C. Williams Allison Forsberg Yan Xu Rachel Narehood Austin Liang Feng |
| author_facet | Xue Guo Jianxiu Zhang Lei Han Juliet Lee Shoshana C. Williams Allison Forsberg Yan Xu Rachel Narehood Austin Liang Feng |
| author_sort | Xue Guo |
| collection | DOAJ |
| description | Abstract Alkanes are the most energy-rich form of carbon and are widely dispersed in the environment. Their transformation by microbes represents a key step in the global carbon cycle. Alkane monooxygenase (AlkB), a membrane-spanning metalloenzyme, converts straight chain alkanes to alcohols in the first step of the microbially-mediated degradation of alkanes, thereby playing a critical role in the global cycling of carbon and the bioremediation of oil. AlkB biodiversity is attributed to its ability to oxidize alkanes of various chain lengths, while individual AlkBs target a relatively narrow range. Mechanisms of substrate selectivity and catalytic activity remain elusive. Here we report the cryo-EM structure of AlkB, which provides a distinct architecture for membrane enzymes. Our structure and functional studies reveal an unexpected diiron center configuration and identify molecular determinants for substrate selectivity. These findings provide insight into the catalytic mechanism of AlkB and shed light on its function in alkane-degrading microorganisms. |
| first_indexed | 2024-04-09T16:22:36Z |
| format | Article |
| id | doaj.art-3696eaeba632468db5511a8af1dc1cb1 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-04-09T16:22:36Z |
| publishDate | 2023-04-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-3696eaeba632468db5511a8af1dc1cb12023-04-23T11:22:36ZengNature PortfolioNature Communications2041-17232023-04-011411910.1038/s41467-023-37869-zStructure and mechanism of the alkane-oxidizing enzyme AlkBXue Guo0Jianxiu Zhang1Lei Han2Juliet Lee3Shoshana C. Williams4Allison Forsberg5Yan Xu6Rachel Narehood Austin7Liang Feng8Department of Molecular and Cellular Physiology, Stanford University School of MedicineDepartment of Molecular and Cellular Physiology, Stanford University School of MedicineDepartment of Molecular and Cellular Physiology, Stanford University School of MedicineDepartment of Chemistry, Barnard CollegeDepartment of Chemistry, Barnard CollegeDepartment of Chemistry, Barnard CollegeDepartment of Molecular and Cellular Physiology, Stanford University School of MedicineDepartment of Chemistry, Barnard CollegeDepartment of Molecular and Cellular Physiology, Stanford University School of MedicineAbstract Alkanes are the most energy-rich form of carbon and are widely dispersed in the environment. Their transformation by microbes represents a key step in the global carbon cycle. Alkane monooxygenase (AlkB), a membrane-spanning metalloenzyme, converts straight chain alkanes to alcohols in the first step of the microbially-mediated degradation of alkanes, thereby playing a critical role in the global cycling of carbon and the bioremediation of oil. AlkB biodiversity is attributed to its ability to oxidize alkanes of various chain lengths, while individual AlkBs target a relatively narrow range. Mechanisms of substrate selectivity and catalytic activity remain elusive. Here we report the cryo-EM structure of AlkB, which provides a distinct architecture for membrane enzymes. Our structure and functional studies reveal an unexpected diiron center configuration and identify molecular determinants for substrate selectivity. These findings provide insight into the catalytic mechanism of AlkB and shed light on its function in alkane-degrading microorganisms.https://doi.org/10.1038/s41467-023-37869-z |
| spellingShingle | Xue Guo Jianxiu Zhang Lei Han Juliet Lee Shoshana C. Williams Allison Forsberg Yan Xu Rachel Narehood Austin Liang Feng Structure and mechanism of the alkane-oxidizing enzyme AlkB Nature Communications |
| title | Structure and mechanism of the alkane-oxidizing enzyme AlkB |
| title_full | Structure and mechanism of the alkane-oxidizing enzyme AlkB |
| title_fullStr | Structure and mechanism of the alkane-oxidizing enzyme AlkB |
| title_full_unstemmed | Structure and mechanism of the alkane-oxidizing enzyme AlkB |
| title_short | Structure and mechanism of the alkane-oxidizing enzyme AlkB |
| title_sort | structure and mechanism of the alkane oxidizing enzyme alkb |
| url | https://doi.org/10.1038/s41467-023-37869-z |
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