An artificial di-iron oxo-protein with phenol oxidase activity

Nat Chem Biol. 2009 Dec;5(12):882-4. doi: 10.1038/nchembio.257. Epub 2009 Nov 8.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Catalysis
  • Catalytic Domain
  • Computational Biology*
  • Iron-Binding Proteins / chemistry*
  • Iron-Binding Proteins / genetics
  • Models, Molecular*
  • Molecular Sequence Data
  • Monophenol Monooxygenase / chemistry*
  • Monophenol Monooxygenase / genetics
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Conformation
  • Protein Engineering*
  • Substrate Specificity

Substances

  • Iron-Binding Proteins
  • Monophenol Monooxygenase

Associated data

  • PubChem-Substance/85244552
  • PubChem-Substance/85244553
  • PubChem-Substance/85244554
  • PubChem-Substance/85244555
  • PubChem-Substance/85244556
  • PubChem-Substance/85244557
  • PubChem-Substance/85244558
  • PubChem-Substance/85244559
  • PubChem-Substance/85244560
  • PubChem-Substance/85244561