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Thermophilic bacteria are potential sources of novel Rieske non-heme iron oxygenases
Rieske non-heme iron oxygenases, which have a Rieske-type [2Fe–2S] cluster and a non-heme catalytic iron center, are an important family of oxidoreductases involved mainly in regio- and stereoselective transformation of a wide array of aromatic hydrocarbons. Though present in all domains of life, th...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5209329/ https://www.ncbi.nlm.nih.gov/pubmed/28050858 http://dx.doi.org/10.1186/s13568-016-0318-5 |
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author | Chakraborty, Joydeep Suzuki-Minakuchi, Chiho Okada, Kazunori Nojiri, Hideaki |
author_facet | Chakraborty, Joydeep Suzuki-Minakuchi, Chiho Okada, Kazunori Nojiri, Hideaki |
author_sort | Chakraborty, Joydeep |
collection | PubMed |
description | Rieske non-heme iron oxygenases, which have a Rieske-type [2Fe–2S] cluster and a non-heme catalytic iron center, are an important family of oxidoreductases involved mainly in regio- and stereoselective transformation of a wide array of aromatic hydrocarbons. Though present in all domains of life, the most widely studied Rieske non-heme iron oxygenases are found in mesophilic bacteria. The present study explores the potential for isolating novel Rieske non-heme iron oxygenases from thermophilic sources. Browsing the entire bacterial genome database led to the identification of 45 homologs from thermophilic bacteria distributed mainly among Chloroflexi, Deinococcus–Thermus and Firmicutes. Thermostability, measured according to the aliphatic index, showed higher values for certain homologs compared with their mesophilic relatives. Prediction of substrate preferences indicated that a wide array of aromatic hydrocarbons could be transformed by most of the identified oxygenase homologs. Further identification of putative genes encoding components of a functional oxygenase system opens up the possibility of reconstituting functional thermophilic Rieske non-heme iron oxygenase systems with novel properties. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13568-016-0318-5) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-5209329 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-52093292017-01-18 Thermophilic bacteria are potential sources of novel Rieske non-heme iron oxygenases Chakraborty, Joydeep Suzuki-Minakuchi, Chiho Okada, Kazunori Nojiri, Hideaki AMB Express Original Article Rieske non-heme iron oxygenases, which have a Rieske-type [2Fe–2S] cluster and a non-heme catalytic iron center, are an important family of oxidoreductases involved mainly in regio- and stereoselective transformation of a wide array of aromatic hydrocarbons. Though present in all domains of life, the most widely studied Rieske non-heme iron oxygenases are found in mesophilic bacteria. The present study explores the potential for isolating novel Rieske non-heme iron oxygenases from thermophilic sources. Browsing the entire bacterial genome database led to the identification of 45 homologs from thermophilic bacteria distributed mainly among Chloroflexi, Deinococcus–Thermus and Firmicutes. Thermostability, measured according to the aliphatic index, showed higher values for certain homologs compared with their mesophilic relatives. Prediction of substrate preferences indicated that a wide array of aromatic hydrocarbons could be transformed by most of the identified oxygenase homologs. Further identification of putative genes encoding components of a functional oxygenase system opens up the possibility of reconstituting functional thermophilic Rieske non-heme iron oxygenase systems with novel properties. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13568-016-0318-5) contains supplementary material, which is available to authorized users. Springer Berlin Heidelberg 2017-01-04 /pmc/articles/PMC5209329/ /pubmed/28050858 http://dx.doi.org/10.1186/s13568-016-0318-5 Text en © The Author(s) 2017 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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. |
spellingShingle | Original Article Chakraborty, Joydeep Suzuki-Minakuchi, Chiho Okada, Kazunori Nojiri, Hideaki Thermophilic bacteria are potential sources of novel Rieske non-heme iron oxygenases |
title | Thermophilic bacteria are potential sources of novel Rieske non-heme iron oxygenases |
title_full | Thermophilic bacteria are potential sources of novel Rieske non-heme iron oxygenases |
title_fullStr | Thermophilic bacteria are potential sources of novel Rieske non-heme iron oxygenases |
title_full_unstemmed | Thermophilic bacteria are potential sources of novel Rieske non-heme iron oxygenases |
title_short | Thermophilic bacteria are potential sources of novel Rieske non-heme iron oxygenases |
title_sort | thermophilic bacteria are potential sources of novel rieske non-heme iron oxygenases |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5209329/ https://www.ncbi.nlm.nih.gov/pubmed/28050858 http://dx.doi.org/10.1186/s13568-016-0318-5 |
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