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Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
Published on: October 3, 2018
An artificial di-iron oxo-protein with phenol oxidase activity
Marina Faiella1, Concetta Andreozzi, Rafael Torres Martin de Rosales
1Department of Chemistry, University Federico II of Napoli, Complesso Universitario Monte S. Angelo, Italy.
Abstract:
Here we report the de novo design and NMR structure of a four-helical bundle di-iron protein with phenol oxidase activity. The introduction of the cofactor-binding and phenol-binding sites required the incorporation of residues that were detrimental to the free energy of folding of the protein. Sufficient stability was, however, obtained by optimizing the sequence of a loop distant from the active site.
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