Difference between revisions of "Part:BBa K4759006"

Latest revision as of 07:50, 10 October 2023

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