An artificial di-iron oxo-protein with phenol oxidase activity
M Faiella, C Andreozzi, RTM De Rosales… - Nature chemical …, 2009 - nature.com
Nature chemical biology, 2009•nature.com
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.
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.
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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