Model systems for flavoenzyme activity: interplay of hydrogen bonding and aromatic stacking in cofactor redox modulation.
[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.
Gray
Mark
M
Department of Chemistry, University of Massachusetts, Amherst 01003, USA.
Goodman
Allan J
AJ
Carroll
Joseph B
JB
Bardon
Kevin
K
Markey
Michael
M
Cooke
Graeme
G
Rotello
Vincent M
VM
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
D014966:Xanthenes; D005182:Flavin-Adenine Dinucleotide; D005486:Flavin Mononucleotide; D010088:Oxidoreductases