FMN

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flavin mononucleotide

Facts (generated by robot; please edit if you find it inaccurate)

  • Studies with flavin analogs provide evidence that a protonated reduced FMN is the substrate-induced transient intermediate in the reaction of Escherichia coli chorismate synthase.
  • FMN is covalently attached to a threonine residue in the NqrB and NqrC subunits of Na(+)-translocating NADH-quinone reductase from Vibrio alginolyticus.
  • Each subunit is colored differently; FMN is shown as magenta spheres, metal sites as red spheres for Fe atoms and yellow spheres for S atoms.
  • Efficient and effective, FMN is profitabl 192 e and growing organically.
  • Until FMN is rebound, these apoflavodoxin molecules behave as described in Chapter 4.

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