Part:BBa_K4759006
Fdx_1499
This is a ferredoxin from Synechococcus elongate PCC7942
Usage and Biology
In Xiaodong Zhang’s research The three-component system using the Fdr_0978/Fdx_1499 as Cytochrome P450 CYP109B1’s redox partner showed the highest catalytic activity. The P450 enzymes are redox-dependent proteins that source electrons from reducing cofactors to drive their activities. In bacterial systems, the electrostatic interactions between the ferredoxin (Fdx), P450 heme, and the reductase domains, as well as the negatively and positively charged amino acids on the Fdx iron-sulfur cluster and P450 proximal site, mediate the conformational changes of the Fdx for electron transfer to P450s. In addition, the substrate binding to P450 induces P450 conformational change to increase its preference for Fdx through electrostatic and steric complementarity. Optimizing protein-to-protein interactions using different methods to improve the electron transfer efficiency of the P450 system, known as "redox chaperone engineering", is one of the important means of engineering P450s, and fruitful progress has been made. Several studies have confirmed that the combined expression of P450, an enzyme with different RPs can reconstruct and promote reactivity. This strategy has been widely used in the bacterial class I P450 system. Electron transport as a redox companion
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal SapI.rc site found at 94
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