The protonation state of the deazaflavin dependent nitroreductase (Ddn) enzyme bound cofactor F420 was investigated using UV-visible spectroscopy and computational simulations. The reduced cofactor F420H2 was determined to be present in its deprotonated state in the holoenzyme form. The mechanistic implications of these findings are discussed.
Mohamed, A. E., Ahmed, F. H., Arulmozhiraja, S., Lin, C. Y., Taylor, M. C., Krausz, E. R., … Coote, M. L. (2016). Protonation state of F420H2 in the prodrug-activating deazaflavin dependent nitroreductase (Ddn) from Mycobacterium tuberculosis. Molecular BioSystems, 12(4), 1110–1113. https://doi.org/10.1039/c6mb00033a