Protonation state of F420H2 in the prodrug-activating deazaflavin dependent nitroreductase (Ddn) from Mycobacterium tuberculosis

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Abstract

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.

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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

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