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Solution structure and biochemical characterization of a spare part protein that restores activity to an oxygen-damaged glycyl radical enzyme.

J. Biol. Inorg. Chem.. 2019; 
BowmanSarah E J,BackmanLindsey R F,BjorkRebekah E,AndorferMary C,YoriSantiago,CarusoAlessio,StultzCollin M,DrennanCatheri
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Molecular Biology Reagents To prepare the cPFL:YfiD co-expression plasmid used in the SDS-PAGE experiment, the yfid gene was inser ted into the second MCS of pCOLA-Duet using NdeI and XhoI cut sites, and a hexahistadine-TEVcleavage site was added at the 5′ end of this gene (Genscript). Get A Quote

摘要

Glycyl radical enzymes (GREs) utilize a glycyl radical cofactor to carry out a diverse array of chemically challenging enzymatic reactions in anaerobic bacteria. Although the glycyl radical is a powerful catalyst, it is also oxygen sensitive such that oxygen exposure causes cleavage of the GRE at the site of the radical. This oxygen sensitivity presents a challenge to facultative anaerobes dwelling in areas prone to oxygen exposure. Once GREs are irreversibly oxygen damaged, cells either need to make new GREs or somehow repair the damaged one. One particular GRE, pyruvate formate lyase (PFL), can be repaired through the binding of a 14.3?kDa protein, termed YfiD, which is constitutively expressed in... More

关键词

Circular dichroism,Cofactor repair,Glycyl radical enzyme,Nuclear magnetic resonance,Radical chemi