1. Structural insight into the electron transfer pathway of a self-sufficient P450 monooxygenase.
- Author
-
Zhang, Lilan, Xie, Zhenzhen, Liu, Ziwei, Zhou, Shuyu, Ma, Lixin, Liu, Weidong, Huang, Jian-Wen, Ko, Tzu-Ping, Li, Xiuqin, Hu, Yuechan, Min, Jian, Yu, Xuejing, Guo, Rey-Ting, and Chen, Chun-Chi
- Subjects
CHARGE exchange ,MONOOXYGENASES ,HEME ,CRYSTAL structure ,ENZYMES - Abstract
Cytochrome P450 monooxygenases are versatile heme-thiolate enzymes that catalyze a wide range of reactions. Self-sufficient cytochrome P450 enzymes contain the redox partners in a single polypeptide chain. Here, we present the crystal structure of full-length CYP116B46, a self-sufficient P450. The continuous polypeptide chain comprises three functional domains, which align well with the direction of electrons traveling from FMN to the heme through the [2Fe-2S] cluster. FMN and the [2Fe-2S] cluster are positioned closely, which facilitates efficient electron shuttling. The edge-to-edge straight-line distance between the [2Fe-2S] cluster and heme is approx. 25.3 Å. The role of several residues located between the [2Fe-2S] cluster and heme in the catalytic reaction is probed in mutagenesis experiments. These findings not only provide insights into the intramolecular electron transfer of self-sufficient P450s, but are also of interest for biotechnological applications of self-sufficient P450s. 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. [ABSTRACT FROM AUTHOR]
- Published
- 2020
- Full Text
- View/download PDF