A Peptide Flavoprotein Mimic: Flavin Recognition and Redox Potential Modulation in Water by a Designed β Hairpin

Authors

  • Sara M. Butterfield,

    1. Department of Chemistry, CB 3290, University of North Carolina, Chapel Hill, NC 27599, USA, Fax: (+1) 919-962-2388
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  • Catherine M. Goodman,

    1. Department of Chemistry, Department of Polymer Science and Engineering, Program in Molecular and Cell Biology, University of Massachusetts, Amherst, MA 01003, USA
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  • Vincent M. Rotello Prof.,

    1. Department of Chemistry, Department of Polymer Science and Engineering, Program in Molecular and Cell Biology, University of Massachusetts, Amherst, MA 01003, USA
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  • Marcey L. Waters Prof.

    1. Department of Chemistry, CB 3290, University of North Carolina, Chapel Hill, NC 27599, USA, Fax: (+1) 919-962-2388
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  • We gratefully acknowledge the University of North Carolina College of Arts and Sciences for startup funds. This work was supported in part by a National Science Foundation Career Award (CHE-0094068, to M.W.) and the National Institutes of Health (GM GM59249, to V.R.). We thank W. John Cooper and Robert M. Hughes for the molecular modeling studies.

Abstract

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Ein künstliches β-Haarnadelpeptid bindet Flavinmononucleotid (FMN) in Wasser durch nichtkovalente Wechselwirkungen mit Trp- und Lys-Resten auf einer Seite der β-Haarnadel (siehe Modell). Die Reduktion von FMN im Komplex ist wegen der π-π-Stapelung zwischen Trp und dem oxidierten Flavinring gehemmt. Dieses System imitiert die Funktion natürlicher Flavoproteine.

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