6- Fluoro 5-enol-pyruvylshikimate 3-phosphate

Binding of fully oxidized FMN to enzyme was considerably enhanced in the presence of substrate, while a smaller enhancement was observed with product, leading the authors to suggest that a ternary enzyme-FMN-(substrate/product) complex is formed. Reduction of FMN in the presence of enzyme resulted in the formation of fully reduced, enzyme-bound, flavin. When FMN was reduced in the presence of both enzyme and the substrate analogue (6R)-6-fluoro-5-enol-pyruvylshikimate-3-phosphate a neutral flavin radical was formed. The radical was also formed to a lesser extent in the presence of 5-enolpyruvylshikimate-3-phosphate (40%) and chorismate (14%). 

EPR showed that the radical had g = 2.0039 and a linewidth of 2.1 mT which decreased to 1.5 mT in deuterated buffer, consistent with a neutral flavin radical. The linewidth was independent of whether chorismate or (6R)-6-fluoro-5-enol-pyruvylshikimate-3-phosphate was present. 

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See also in sourсe #XX -- [ , ]

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