Literature DB >> 19915535

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

Marina Faiella1, Concetta Andreozzi, Rafael Torres Martin de Rosales, Vincenzo Pavone, Ornella Maglio, Flavia Nastri, William F DeGrado, Angela Lombardi.   

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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Year:  2009        PMID： 19915535      PMCID： PMC3808167          DOI： 10.1038/nchembio.257

Source DB:  PubMed          Journal:  Nat Chem Biol        ISSN： 1552-4450            Impact factor:   15.040


  22 in total

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Journal:  Nature       Date:  2008-03-19       Impact factor: 49.962

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6.  Retrostructural analysis of metalloproteins: application to the design of a minimal model for diiron proteins.

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7.  Spectroscopic definition of the biferrous and biferric sites in de novo designed four-helix bundle DFsc peptides: implications for O2 reactivity of binuclear non-heme iron enzymes.

Authors:  Caleb B Bell; Jennifer R Calhoun; Elena Bobyr; Pin-Pin Wei; Britt Hedman; Keith O Hodgson; William F Degrado; Edward I Solomon
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8.  Oxygen reactivity of the biferrous site in the de novo designed four helix bundle peptide DFsc: nature of the "intermediate" and reaction mechanism.

Authors:  Jennifer R Calhoun; Caleb B Bell; Thomas J Smith; Thomas J Thamann; William F DeGrado; Edward I Solomon
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  63 in total

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6.  Artificial Diiron Enzymes with a De Novo Designed Four-Helix Bundle Structure.

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Journal:  Eur J Inorg Chem       Date:  2015-07-06       Impact factor: 2.524

7.  Rapid Sampling of Hydrogen Bond Networks for Computational Protein Design.

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8.  Systematic Perturbations of Binuclear Non-heme Iron Sites: Structure and Dioxygen Reactivity of de Novo Due Ferri Proteins.

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9.  Covalent Anchor Positions Play an Important Role in Tuning Catalytic Properties of a Rationally Designed MnSalen-containing Metalloenzyme.

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10.  Proteins from an unevolved library of de novo designed sequences bind a range of small molecules.

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Journal:  ACS Synth Biol       Date:  2012-04-02       Impact factor: 5.110
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