“…The crystal structure of FMN, the product of the reaction, bound to V. harveyi luciferase has been reported, while the crystals of the luciferase/FMNH 2 complex degraded rapidly and were unsuitable for data collection [90]. In Q67, FMN may bind to the active site pocket formed by eight β-sheets (β1, β2, β3, β5, β8, β9, β10, and β13) in the α-subunit (Figure 5(a-3,a-4)), and there is a similar pocket in the β-subunit (Figure 5(a-3)), which may bind other small molecules to affect the activity of the whole enzyme, such as hermetic organic solvents [45]. However, no structural information on the spatial orientation of the luciferase with the substrate (FMNH 2 and the aldehyde) or intermediates of the reaction is available, preventing a more detailed interpretation of how the overall reaction is generated.…”