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.
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Communication
A Peptide Flavoprotein Mimic: Flavin Recognition and Redox Potential Modulation in Water by a Designed β Hairpin†
Article first published online: 27 JAN 2004
DOI: 10.1002/anie.200352527
Copyright © 2004 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Butterfield, S. M., Goodman, C. M., Rotello, V. M. and Waters, M. L. (2004), A Peptide Flavoprotein Mimic: Flavin Recognition and Redox Potential Modulation in Water by a Designed β Hairpin. Angewandte Chemie International Edition, 43: 724–727. doi: 10.1002/anie.200352527
- †
Publication History
- Issue published online: 27 JAN 2004
- Article first published online: 27 JAN 2004
- Manuscript Revised: 27 OCT 2003
- Manuscript Received: 31 JUL 2003
Keywords:
- flavins;
- molecular recognition;
- peptidomimetics;
- protein models;
- redox chemistry
Graphical Abstract
Pinning down flavoproteins: A designed β-hairpin peptide binds flavin mononucleotide (FMN) in water through noncovalent interactions involving Trp and Lys residues on one face of the β hairpin (see model). Reduction of FMN is disfavored in the complex as a result of favorable π–π stacking interactions between Trp side chains and the oxidized flavin ring. This system mimicks the function of naturally occurring flavoproteins.