1 publication

1 publication

Metal-Binding Promiscuity in Artificial Metalloenzyme Design

Review

Pordea, A.

Curr. Opin. Chem. Biol. 2015, 25, 124-132, 10.1016/j.cbpa.2014.12.035

This review presents recent examples of metal-binding promiscuity in protein scaffolds and highlights the effect of metal variation on catalytic functionality. Naturally evolved binding sites, as well as unnatural amino acids and cofactors can bind a diverse range of metals, including non-biological transition elements. Computational screening and rational design have been successfully used to create promiscuous binding-sites. Incorporation of non-native metals into proteins expands the catalytic range of transformations catalysed by enzymes and enhances their potential for application in chemicals synthesis.


Notes: ---