Ultrafast fluorescence dynamics of FMN binding protein (FBP) from
Desulfobivrio vulgaris, strain MiyaxakiF, were compared in solution and crystal phases. Fluorescence lifetimes of FBP were 167 fs (96%) and1.5 ps (4%) in solution (
av = 220 fs), and 730 fs (60%) and longer than 10 ps (40%) in crystals (
av =4.44 ps). The quenching of the fluorescence of flavin in the protein was considered to be due to photoinducedelectron transfer (ET) from Trp or Tyr to the excited isoalloxazine (Iso) nearby. The average lifetime was20 times longer in crystal vs in solution. Averaged distances between Iso and nearby Trp-32, Tyr-35, andTrp-106 were 8.42, 7.36, and 8.15 Å in solution, respectively (obtained by NMR spectroscopy), and 7.05,7.72, and 8.49 Å in crystal, respectively (obtained by X-ray crystallography). The prolonged lifetime in crystalcannot be elucidated by the change in the distances between the states. It was suggested that the longerlifetime in crystal was ascribed to the absence of water molecules around FBP with rapid motional freedom,which may be the driving force for the ET in flavoproteins.