Customized exogenous ferredoxin functions as an efficient electron carrier
Abstract 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,...
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2021
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oai:doaj.org-article:4dee6a3bdfb04af085471a6add510d592021-11-07T12:03:46ZCustomized exogenous ferredoxin functions as an efficient electron carrier10.1186/s40643-021-00464-52197-4365https://doaj.org/article/4dee6a3bdfb04af085471a6add510d592021-11-01T00:00:00Zhttps://doi.org/10.1186/s40643-021-00464-5https://doaj.org/toc/2197-4365Abstract 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 AbstractZhan SongCancan WeiChao LiXin GaoShuhong MaoFuping LuHui-Min QinSpringerOpenarticleFerredoxinElectron transferElectron bifurcation[2Fe–2S] clustersTechnologyTChemical technologyTP1-1185BiotechnologyTP248.13-248.65ENBioresources and Bioprocessing, Vol 8, Iss 1, Pp 1-13 (2021) |
| institution |
DOAJ |
| collection |
DOAJ |
| language |
EN |
| topic |
Ferredoxin Electron transfer Electron bifurcation [2Fe–2S] clusters Technology T Chemical technology TP1-1185 Biotechnology TP248.13-248.65 |
| spellingShingle |
Ferredoxin Electron transfer Electron bifurcation [2Fe–2S] clusters Technology T Chemical technology TP1-1185 Biotechnology TP248.13-248.65 Zhan Song Cancan Wei Chao Li Xin Gao Shuhong Mao Fuping Lu Hui-Min Qin Customized exogenous ferredoxin functions as an efficient electron carrier |
| description |
Abstract 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 |
| format |
article |
| author |
Zhan Song Cancan Wei Chao Li Xin Gao Shuhong Mao Fuping Lu Hui-Min Qin |
| author_facet |
Zhan Song Cancan Wei Chao Li Xin Gao Shuhong Mao Fuping Lu Hui-Min Qin |
| author_sort |
Zhan Song |
| title |
Customized exogenous ferredoxin functions as an efficient electron carrier |
| title_short |
Customized exogenous ferredoxin functions as an efficient electron carrier |
| title_full |
Customized exogenous ferredoxin functions as an efficient electron carrier |
| title_fullStr |
Customized exogenous ferredoxin functions as an efficient electron carrier |
| title_full_unstemmed |
Customized exogenous ferredoxin functions as an efficient electron carrier |
| title_sort |
customized exogenous ferredoxin functions as an efficient electron carrier |
| publisher |
SpringerOpen |
| publishDate |
2021 |
| url |
https://doaj.org/article/4dee6a3bdfb04af085471a6add510d59 |
| work_keys_str_mv |
AT zhansong customizedexogenousferredoxinfunctionsasanefficientelectroncarrier AT cancanwei customizedexogenousferredoxinfunctionsasanefficientelectroncarrier AT chaoli customizedexogenousferredoxinfunctionsasanefficientelectroncarrier AT xingao customizedexogenousferredoxinfunctionsasanefficientelectroncarrier AT shuhongmao customizedexogenousferredoxinfunctionsasanefficientelectroncarrier AT fupinglu customizedexogenousferredoxinfunctionsasanefficientelectroncarrier AT huiminqin customizedexogenousferredoxinfunctionsasanefficientelectroncarrier |
| _version_ |
1718443545003556864 |