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Structure and mechanism of the alkane-oxidizing enzyme AlkB
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 ste...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10110569/ https://www.ncbi.nlm.nih.gov/pubmed/37069165 http://dx.doi.org/10.1038/s41467-023-37869-z |
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author | Guo, Xue Zhang, Jianxiu Han, Lei Lee, Juliet Williams, Shoshana C. Forsberg, Allison Xu, Yan Austin, Rachel Narehood Feng, Liang |
author_facet | Guo, Xue Zhang, Jianxiu Han, Lei Lee, Juliet Williams, Shoshana C. Forsberg, Allison Xu, Yan Austin, Rachel Narehood Feng, Liang |
author_sort | Guo, Xue |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-10110569 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-101105692023-04-19 Structure and mechanism of the alkane-oxidizing enzyme AlkB Guo, Xue Zhang, Jianxiu Han, Lei Lee, Juliet Williams, Shoshana C. Forsberg, Allison Xu, Yan Austin, Rachel Narehood Feng, Liang Nat Commun Article 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. Nature Publishing Group UK 2023-04-17 /pmc/articles/PMC10110569/ /pubmed/37069165 http://dx.doi.org/10.1038/s41467-023-37869-z Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Guo, Xue Zhang, Jianxiu Han, Lei Lee, Juliet Williams, Shoshana C. Forsberg, Allison Xu, Yan Austin, Rachel Narehood Feng, Liang Structure and mechanism of the alkane-oxidizing enzyme AlkB |
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 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10110569/ https://www.ncbi.nlm.nih.gov/pubmed/37069165 http://dx.doi.org/10.1038/s41467-023-37869-z |
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