Electronic factor in biological electron transfer systems. Role of aromatic side groups

1991 ◽  
Vol 40 (S18) ◽  
pp. 99-118 ◽  
Author(s):  
S. Larsson ◽  
M. Braga ◽  
A. Broo ◽  
B. k�llebring
1997 ◽  
Vol 12 (8) ◽  
pp. 721-727 ◽  
Author(s):  
Karl S. Ryder ◽  
David G. Morris ◽  
Jonathan M. Cooper

2021 ◽  
Vol 8 (1) ◽  
Author(s):  
Zhan Song ◽  
Cancan Wei ◽  
Chao Li ◽  
Xin Gao ◽  
Shuhong Mao ◽  
...  

AbstractFerredoxin (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


Author(s):  
Zhan Song ◽  
Cancan Wei ◽  
Chao Li ◽  
Xin Gao ◽  
Shuhong Mao ◽  
...  

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 NADPH reduction activity and 9OHAD production yield and proved the importance of [2Fe-2S] clusters of Fdx-containing oxidoreductase in transferring electrons in steroidal conversion. The truncated Fdx domain in all oxidoreductases, together with mutagenesis data, further 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 conversion rate have been significantly improved. A novel efficient electron transfer pathway of PRF+Fdx+KshA 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.


2016 ◽  
Vol 1857 ◽  
pp. e17
Author(s):  
A. William Rutherford ◽  
K. Brinkert ◽  
S. de Causmaecker ◽  
A. Krieger-Lizskay ◽  
A. Fantuzzi

Author(s):  
Lars Mohrhusen ◽  
Jessica Kräuter ◽  
Katharina Al-Shamery

The photochemical conversion of organic compounds on tailored transition metal oxide surfaces by (UV) irradiation has found wide applications ranging from the production of chemicals to the degradation of organic...


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