Structural highlights
Publication Abstract from PubMed
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.
An artificial di-iron oxo-protein with phenol oxidase activity.,Faiella M, Andreozzi C, de Rosales RT, Pavone V, Maglio O, Nastri F, DeGrado WF, Lombardi A Nat Chem Biol. 2009 Dec;5(12):882-4. doi: 10.1038/nchembio.257. Epub 2009 Nov 8. PMID:19915535[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Faiella M, Andreozzi C, de Rosales RT, Pavone V, Maglio O, Nastri F, DeGrado WF, Lombardi A. An artificial di-iron oxo-protein with phenol oxidase activity. Nat Chem Biol. 2009 Dec;5(12):882-4. PMID:19915535 doi:10.1038/nchembio.257
