Depletion and replacement of protein metal ligands.
Recently, site-directed mutagenesis has been applied to protein-derived metal ligands in a way that permits the replacement in trans of protein ligands. The chemical diversity of ligands available using this method far exceeds that attainable using standard mutagenesis. Non-conservative ligand replacement can yield novel metalloproteins with altered ligand-binding, enzymatic activities, and spectroscopic properties. Conservative ligand substitution, or 'ligand detachment', allows the structural and functional effects of the covalent linkage between the ligand and the protein to be evaluated; this linkage is often proposed to play a critical role in modulating the structure and reactivity of the metal center. Furthermore, this method can be exploited to study the details of molecular recognition at the structural, thermodynamic, and dynamic levels.
Barrick
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University of Oregon, Eugene, USA.
D001400:Azurin / Q000737:chemistry; D003574:Cytochrome c Group / Q000737:chemistry; D003578:Cytochrome-c Peroxidase / Q000737:chemistry; D045304:Cytochromes c; D006419:Heme Oxygenase (Decyclizing) / Q000737:chemistry; D006420:Hemeproteins / Q000737:chemistry*; D008024:Ligands; D008667:Metalloproteins / Q000737:chemistry* / Q000378:metabolism; D008670:Metals / Q000378:metabolism*; D009211:Myoglobin / Q000737:chemistry; D015202:Protein Engineering / Q000379:methods*; D029701:Saccharomyces cerevisiae Proteins; D016335:Zinc Fingers
C014059:CYC1 protein, S cerevisiae; D003574:Cytochrome c Group; D006420:Hemeproteins; D008024:Ligands; D008667:Metalloproteins; D008670:Metals; D009211:Myoglobin; D029701:Saccharomyces cerevisiae Proteins; D001400:Azurin; D045304:Cytochromes c; D003578:Cytochrome-c Peroxidase; D006419:Heme Oxygenase (Decyclizing)