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嗜热细菌是新型 Rieske 非血红素铁加氧酶的潜在来源。

Thermophilic bacteria are potential sources of novel Rieske non-heme iron oxygenases.

作者信息

Chakraborty Joydeep, Suzuki-Minakuchi Chiho, Okada Kazunori, Nojiri Hideaki

机构信息

Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, Japan.

出版信息

AMB Express. 2017 Dec;7(1):17. doi: 10.1186/s13568-016-0318-5. Epub 2017 Jan 4.

Abstract

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.

摘要

Rieske非血红素铁加氧酶含有一个Rieske型[2Fe-2S]簇和一个非血红素催化铁中心,是氧化还原酶的一个重要家族,主要参与多种芳烃的区域和立体选择性转化。尽管Rieske非血红素铁加氧酶存在于生命的所有领域,但研究最广泛的是嗜温细菌中的此类酶。本研究探索了从嗜热菌中分离新型Rieske非血红素铁加氧酶的可能性。浏览整个细菌基因组数据库后,鉴定出了45个来自嗜热菌的同源物,它们主要分布在绿弯菌门、嗜热放线菌门和厚壁菌门中。根据脂肪族指数测定的热稳定性表明,某些同源物与其嗜温亲属相比具有更高的值。对底物偏好的预测表明,大多数已鉴定的加氧酶同源物可以转化多种芳烃。进一步鉴定编码功能性加氧酶系统组分的推定基因,为重建具有新特性的功能性嗜热Rieske非血红素铁加氧酶系统开辟了可能性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4c0d/5209329/778d529658d4/13568_2016_318_Fig1_HTML.jpg

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