Metal-binding promiscuity in artificial metalloenzyme design. (April 2015)

• Record Type: Journal Article
• Authors: Pordea, Anca
• Is Part Of: Current opinion in chemical biology. Volume 25(2015)
• Page Start: 124
• Page End: 132
• Publication Date: 2015-04
• Subjects: Bioorganic chemistry -- Periodicals; Biology -- Periodicals; Biochemistry -- Periodicals; Clinical biochemistry -- Periodicals; Biochemistry -- Periodicals; Chimie bio-organique -- Périodiques; Biologie -- Périodiques; 572.05
• DOI: 10.1016/j.cbpa.2014.12.035
• Languages: English
• ISSNs: 1367-5931

Abstract

Highlights: Metalloenzyme binding sites can accommodate a diverse range of metals. Metal substitution can lead to novel catalytic activity. Computational screening and rational design can identify promiscuous binding sites. Abstract : 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.