title: Model systems for flavoenzyme activity: interplay of hydrogen bonding and aromatic stacking in cofactor redox modulation.
abstract: [structure: see text] A model system has been developed to study the synergy between aromatic stacking and hydrogen bonding in the binding of a flavin derivative. The results show that the identity of both the hydrogen bonding and pi-stacking units strongly determine the overall receptor affinity for flavin in both the oxidized and radical anion forms.
authors.affiliation: Department of Chemistry, University of Massachusetts, Amherst 01003, USA.
authors.forename: Mark
authors.initials: M
authors.lastname: Gray
authors.forename: Allan J
authors.initials: AJ
authors.lastname: Goodman
authors.forename: Joseph B
authors.initials: JB
authors.lastname: Carroll
authors.forename: Kevin
authors.initials: K
authors.lastname: Bardon
authors.forename: Michael
authors.initials: M
authors.lastname: Markey
authors.forename: Graeme
authors.initials: G
authors.lastname: Cooke
authors.forename: Vincent M
authors.initials: VM
authors.lastname: Rotello
mesh_terms: D005486:Flavin Mononucleotide / Q000737:chemistry / Q000378:metabolism*; D005182:Flavin-Adenine Dinucleotide / Q000737:chemistry / Q000378:metabolism*; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry* / Q000378:metabolism*; D014966:Xanthenes / Q000737:chemistry / Q000378:metabolism
chemical_list: D014966:Xanthenes; D005182:Flavin-Adenine Dinucleotide; D005486:Flavin Mononucleotide; D010088:Oxidoreductases