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

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.

journal_name

Nat Commun

journal_title

Nature communications

authors

Zhang L,Xie Z,Liu Z,Zhou S,Ma L,Liu W,Huang JW,Ko TP,Li X,Hu Y,Min J,Yu X,Guo RT,Chen CC

doi

10.1038/s41467-020-16500-5

subject

Has Abstract

pub_date

2020-05-29 00:00:00

pages

2676

issue

1

issn

2041-1723

pii

10.1038/s41467-020-16500-5

journal_volume

11

pub_type

杂志文章

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