title: Metal-binding promiscuity in artificial metalloenzyme design.
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.
authors.affiliation: Department of Chemical and Environmental Engineering, University of Nottingham, University Park, Nottingham NG7 2RD, United Kingdom. Electronic address: anca.pordea@nottingham.ac.uk.
authors.forename: Anca
authors.initials: A
authors.lastname: Pordea
mesh_terms: D000596:Amino Acids / Q000378:metabolism; D004798:Enzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008667:Metalloproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008670:Metals / Q000378:metabolism*; D015202:Protein Engineering / Q000379:methods*; D013379:Substrate Specificity
chemical_list: D000596:Amino Acids; D004798:Enzymes; D008667:Metalloproteins; D008670:Metals