title: Model systems for flavoenzyme activity: relationships between cofactor structure, binding and redox properties.
abstract: A series of flavins were synthesized bearing electron-withdrawing and -donating substituents. The electrochemical properties of these flavins in a nonpolar solvent were determined. The recognition of these flavins by a diamidopyridine (DAP) receptor and the effect this receptor has on flavin redox potential was also quantified. It was found that the DAP-flavin binding affinity and the reduction potentials (E(1/2)) for both the DAP-bound and unbound flavins correlated well with functions derived from linear free energy relationships (LFERs). These results provide insight and predictive capability for the interplay of electronics and redox state-specific interactions for both abiotic and enzymatic systems.
authors.affiliation: Department of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003, USA.
authors.forename: Yves-Marie
authors.initials: YM
authors.lastname: Legrand
authors.forename: Mark
authors.initials: M
authors.lastname: Gray
authors.forename: Graeme
authors.initials: G
authors.lastname: Cooke
authors.forename: Vincent M
authors.initials: VM
authors.lastname: Rotello
mesh_terms: D004563:Electrochemistry / Q000379:methods; D005415:Flavins / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D007700:Kinetics; D010084:Oxidation-Reduction; D011725:Pyridines / Q000737:chemistry / Q000378:metabolism; D013816:Thermodynamics
chemical_list: D005415:Flavins; D011725:Pyridines