Structural insight into the electron transfer pathway of a self-sufficient P450 monooxygenase

Self-sufficient cytochrome P450 monooxygenases, which contain all redox partners in a single polypeptide chain, are of interest for biotechnological applications. Here, the authors present the crystal structure of full-length Thermobispora bispora CYP116B46 and discuss the potential electron transfe...

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Autores principales:	Lilan Zhang, Zhenzhen Xie, Ziwei Liu, Shuyu Zhou, Lixin Ma, Weidong Liu, Jian-Wen Huang, Tzu-Ping Ko, Xiuqin Li, Yuechan Hu, Jian Min, Xuejing Yu, Rey-Ting Guo, Chun-Chi Chen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/25583d0860a44241a350fa6add954485
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spelling	oai:doaj.org-article:25583d0860a44241a350fa6add9544852021-12-02T14:47:36ZStructural insight into the electron transfer pathway of a self-sufficient P450 monooxygenase10.1038/s41467-020-16500-52041-1723https://doaj.org/article/25583d0860a44241a350fa6add9544852020-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16500-5https://doaj.org/toc/2041-1723Self-sufficient cytochrome P450 monooxygenases, which contain all redox partners in a single polypeptide chain, are of interest for biotechnological applications. Here, the authors present the crystal structure of full-length Thermobispora bispora CYP116B46 and discuss the potential electron transfer pathway.Lilan ZhangZhenzhen XieZiwei LiuShuyu ZhouLixin MaWeidong LiuJian-Wen HuangTzu-Ping KoXiuqin LiYuechan HuJian MinXuejing YuRey-Ting GuoChun-Chi ChenNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-6 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Lilan Zhang Zhenzhen Xie Ziwei Liu Shuyu Zhou Lixin Ma Weidong Liu Jian-Wen Huang Tzu-Ping Ko Xiuqin Li Yuechan Hu Jian Min Xuejing Yu Rey-Ting Guo Chun-Chi Chen Structural insight into the electron transfer pathway of a self-sufficient P450 monooxygenase
description	Self-sufficient cytochrome P450 monooxygenases, which contain all redox partners in a single polypeptide chain, are of interest for biotechnological applications. Here, the authors present the crystal structure of full-length Thermobispora bispora CYP116B46 and discuss the potential electron transfer pathway.
format	article
author	Lilan Zhang Zhenzhen Xie Ziwei Liu Shuyu Zhou Lixin Ma Weidong Liu Jian-Wen Huang Tzu-Ping Ko Xiuqin Li Yuechan Hu Jian Min Xuejing Yu Rey-Ting Guo Chun-Chi Chen
author_facet	Lilan Zhang Zhenzhen Xie Ziwei Liu Shuyu Zhou Lixin Ma Weidong Liu Jian-Wen Huang Tzu-Ping Ko Xiuqin Li Yuechan Hu Jian Min Xuejing Yu Rey-Ting Guo Chun-Chi Chen
author_sort	Lilan Zhang
title	Structural insight into the electron transfer pathway of a self-sufficient P450 monooxygenase
title_short	Structural insight into the electron transfer pathway of a self-sufficient P450 monooxygenase
title_full	Structural insight into the electron transfer pathway of a self-sufficient P450 monooxygenase
title_fullStr	Structural insight into the electron transfer pathway of a self-sufficient P450 monooxygenase
title_full_unstemmed	Structural insight into the electron transfer pathway of a self-sufficient P450 monooxygenase
title_sort	structural insight into the electron transfer pathway of a self-sufficient p450 monooxygenase
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/25583d0860a44241a350fa6add954485
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Structural insight into the electron transfer pathway of a self-sufficient P450 monooxygenase

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