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Introduction of an Artificial Cu Binding Site at the Surface of CA II: Pitfalls of Rational Design Finally Scooped by Serendipity

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The aim of this study was the introduction of an artificial copper center at the surface of carbonic anhydrase II (CA II) which subsequently might be used by azide and alkyne building blocks to catalyze triazole formation following 2+3 dipolar cycloaddition. Several mutants were produced to introduce favorable copper coordinating residues taking model copper-proteins from nature as reference templates. Unfortunately, the embarked rational design strategy remained unsuccessful which underlines that our still rather limited understanding of amino acid exchanges on the architecture of proteins might provoke unpredictable effects while tampering with complex biological systems such as a highly functionalized proteins. Finally, more by serendipity than design the formation of an artificial Cu center at the surface of CA II could be achieved. The metal ion is coordinated by two histidines and a serine residue in square planar coordination geometry.

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Keywords: Artificial Cu; Cambridge Structural Database; Carbonic anhydrase II; Cloning; Design of Mutants; Healthcare; Huisgen reaction; Lysis; Protein Purification; Pseudomonas aeruginosa; Rational Design; Stedium Biotech; Structural Investigation of CA II; X-ray crystallography; Zn2+ ion; active site; amino acids; anaerobic conditions; artificial Cu2+; artificial metal; axial position; binding pocket; binding site; biohybrid materials; carbon dioxide; carbonyl groups; catalytic reaction; catalyzes; copper-ion; crystallographic study; cysteine; cysteine residue; density; disulfide bond; disulfide bridge; enzyme; equilibrium rate; glutathione-S-transferase; helix-helix interactions; high flexibility; high-affinity metal; histidines; hydration; hypothesis; inhibitor cocktail tablet; isothermal titration calorimetry; linear coordination site; melting temperature; metal chelation; metal-center; mutagenesis; novel residues; p-chloromercuribenzoic acid; protein crystallography; protein monomers; protons; site-directed mutagenesis; stoichiometry; target protein; thiole group; triazole; trigonal planar geometry; trigonal-planar coordination; wild-type structures; zinc metalloenzyme

Document Type: Research Article

Publication date: January 1, 2011

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  • Current Chemical Biology aims to publish full-length and mini reviews on exciting new developments at the chemistry-biology interface, covering topics relating to Chemical Synthesis, Science at Chemistry-Biology Interface and Chemical Mechanisms of Biological Systems.

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