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

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 interactio...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2004-01, Vol.43 (6), p.724-727
Main Authors: Butterfield, Sara M., Goodman, Catherine M., Rotello, Vincent M., Waters, Marcey L.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Flavin Mononucleotide - chemistry
Flavin Mononucleotide - metabolism
flavins
Kinetics
molecular recognition
Oxidation-Reduction
Peptides - chemistry
Peptides - metabolism
peptidomimetics
Protein Binding
Protein Conformation
Protein Engineering
Protein Folding
protein models
redox chemistry
Water - chemistry
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Summary: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.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200352527