Customized exogenous ferredoxin functions as an efficient electron carrier

Ferredoxin (Fdx) is regarded as the main electron carrier in biological electron transfer and acts as an electron donor in metabolic pathways of many organisms. Here, we screened a self-sufficient P450-derived reductase PRF with promising production yield of 9OHAD (9α-hydroxy4-androstene-3,17-dione)...

Full description

Saved in:
Bibliographic Details
Published in:Bioresources and bioprocessing 2021-11, Vol.8 (1), p.109-109, Article 109
Main Authors: Song, Zhan, Wei, Cancan, Li, Chao, Gao, Xin, Mao, Shuhong, Lu, Fuping, Qin, Hui-Min
Format: Article
Language:English
Subjects:
4-Androstene-3,17-dione
[2Fe–2S] clusters
Biochemical Engineering
Chemistry
Chemistry and Materials Science
Clusters
Complex systems
Conversion
Electron bifurcation
Electron transfer
Electrons
Environmental Engineering/Biotechnology
Ferredoxin
Hydroxylase
Industrial and Production Engineering
Metabolic pathways
Metabolism
Mutagenesis
Oxidoreductase
Oxygenase
Protein interaction
Proteins
Redox potential
Reductases
Self sufficiency
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Ferredoxin (Fdx) is regarded as the main electron carrier in biological electron transfer and acts as an electron donor in metabolic pathways of many organisms. Here, we screened a self-sufficient P450-derived reductase PRF with promising production yield of 9OHAD (9α-hydroxy4-androstene-3,17-dione) from AD, and further proved the importance of [2Fe–2S] clusters of ferredoxin-oxidoreductase in transferring electrons in steroidal conversion. The results of truncated Fdx domain in all oxidoreductases and mutagenesis data elucidated the indispensable role of [2Fe–2S] clusters in the electron transfer process. By adding the independent plant-type Fdx to the reaction system, the AD (4-androstene-3,17-dione) conversion rate have been significantly improved. A novel efficient electron transfer pathway of PRF + Fdx + KshA (KshA, Rieske-type oxygenase of 3-ketosteroid-9-hydroxylase) in the reaction system rather than KshAB complex system was proposed based on analysis of protein–protein interactions and redox potential measurement. Adding free Fdx created a new conduit for electrons to travel from reductase to oxygenase. This electron transfer pathway provides new insight for the development of efficient exogenous Fdx as an electron carrier. Graphical Abstract
ISSN:2197-4365
2197-4365
DOI:10.1186/s40643-021-00464-5