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

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 () and Chun-Chi Chen ()
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Lilan Zhang: Hubei University
Zhenzhen Xie: Hubei University
Ziwei Liu: Hubei University
Shuyu Zhou: Hubei University
Lixin Ma: Hubei University
Weidong Liu: Hubei University
Jian-Wen Huang: Hubei University
Tzu-Ping Ko: Institute of Biological Chemistry, Academia Sinica
Xiuqin Li: Hubei University
Yuechan Hu: Hubei University
Jian Min: Hubei University
Xuejing Yu: Hubei University
Rey-Ting Guo: Hubei University
Chun-Chi Chen: Hubei University

Nature Communications, 2020, vol. 11, issue 1, 1-6

Abstract: 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.

Date: 2020
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DOI: 10.1038/s41467-020-16500-5

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