857553-44-7Relevant academic research and scientific papers
An artificial oxygenase built from scratch: Substrate binding site identified using a docking approach
Esmieu, Charlene,Cherrier, Mickael V.,Amara, Patricia,Girgenti, Elodie,Marchi-Delapierre, Caroline,Oddon, Frederic,Iannello, Marina,Jorge-Robin, Adeline,Cavazza, Christine,Menage, Stephane
, p. 3922 - 3925 (2013)
The substrate for an artificial iron monooxygenase was selected by using docking calculations. The high catalytic efficiency of the reported enzyme for sulfide oxidation was directly correlated to the predicted substrate binding mode in the protein cavity, thus illustrating the synergetic effect of the substrate binding site, protein scaffold, and catalytic site.
A Selective Sulfide Oxidation Catalyzed by Heterogeneous Artificial Metalloenzymes Iron?NikA
Cavazza, Christine,Lopez, Sarah,Ménage, Stéphane,Marchi-Delapierre, Caroline
supporting information, p. 16633 - 16638 (2020/11/30)
Performing a heterogeneous catalysis with proteins is still a challenge. Herein, we demonstrate the importance of cross-linked crystals for sulfoxide oxidation by an artificial enzyme. The biohybrid consists of the insertion of an iron complex into a NikA protein crystal. The heterogeneous catalysts displays a better efficiency-with higher reaction kinetics, a better stability and expand the substrate scope compared to its solution counterpart. Designing crystalline artificial enzymes represents a good alternative to soluble or supported enzymes for the future of synthetic biology.
