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

Nature Chemical Biology volume 5, pages 882884 (2009) | Download Citation

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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.

  • Compound C6H7NO

    4-Amino-phenol

  • Compound C6H5NO

    Benzoquinone mono-imine

  • Compound C14H22O2

    3,5-Ditert-butyl-catechol

  • Compound C14H20O2

    3,5-Ditert-butyl-quinone

  • Compound C6H8N2

    para-Phenylenediamine

  • Compound C6H8N2

    ortho-Phenylenediamine

  • Compound C6H8N2

    meta-Phenylenediamine

  • Compound C12H11N3O

    Aminoindoaniline

  • Compound C6H7N

    Aniline

  • Compound C18H15ClN4

    Phenosafranine

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Acknowledgements

The authors thank M. Trifuoggi for metal content analysis. This work was supported by the Italian Ministry of University and Scientific Research (PRIN 2007KAWXCL), the European Commission (Marie Curie Fellowship HPMD-GH-01-00113-03 to R.T.M.R.), the US National Institutes of Health (GM54616) and the US National Science Foundation (grant from the Materials Research Science and Engineering Center to the Laboratory for Research on the Structure of Matter at the University of Pennsylvania).

Author information

Author notes

    • Rafael Torres Martin de Rosales
    •  & Ornella Maglio

    Present addresses: Division of Imaging Sciences, King's College London, St. Thomas Hospital, London, UK (R.T.M.R.) and Institute of Biostructure and Bioimaging, National Research Council (CNR), Napoli, Italy (O.M.).

Affiliations

  1. Department of Chemistry, University Federico II of Napoli, Complesso Universitario Monte S. Angelo, Napoli, Italy.

    • Marina Faiella
    • , Concetta Andreozzi
    • , Rafael Torres Martin de Rosales
    • , Vincenzo Pavone
    • , Ornella Maglio
    • , Flavia Nastri
    •  & Angela Lombardi
  2. Department of Biochemistry and Biophysics, University of Pennsylvania, School of Medicine, Philadelphia, Pennsylvania, USA.

    • William F DeGrado

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Contributions

F.N., O.M. and A.L. designed experiments and analyzed results. R.T.M.R., M.F. and C.A. synthesized the protein and performed UV-vis and chemical denaturation studies. O.M. and M.F. determined the solution structure. F.N. and C.A. performed kinetic experiments. A.L and V.P. performed molecular modeling. W.F.D. and A.L. wrote the manuscript in consultation with the remaining authors.

Corresponding authors

Correspondence to William F DeGrado or Angela Lombardi.

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DOI

https://doi.org/10.1038/nchembio.257

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