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.
Original language | English |
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Pages (from-to) | 882-884 |
Number of pages | 3 |
Journal | Nature Chemical Biology |
Volume | 5 |
Issue number | 12 |
DOIs | |
Publication status | Published - Dec 2009 |