flavin-adenine-dinucleotide and pinoresinol

The regio- and stereospecificity of bimolecular phenoxy radical coupling reactions, of especial importance in lignin and lignan biosynthesis, are clearly controlled in some manner in vivo; yet in vitro coupling by oxidases, such as laccases, only produce racemic products. In other words, laccases, peroxidases, and comparable oxidases are unable to control regio- or stereospecificity by themselves and thus some other agent must exist. A 78-kilodalton protein has been isolated that, in the presence of an oxidase or one electron oxidant, effects stereoselective bimolecular phenoxy radical coupling in vitro. Itself lacking a catalytically active (oxidative) center, its mechanism of action is presumed to involve capture of E-coniferyl alcohol-derived free-radical intermediates, with consequent stereoselective coupling to give (+)-pinoresinol.

Topics: Dimerization; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Free Radicals; Furans; Kinetics; Laccase; Lignans; Molecular Conformation; Oxidation-Reduction; Oxidoreductases; Phenols; Plant Proteins; Stereoisomerism