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.
Highlights
The protonation state of the deazaflavin dependent nitroreductase (Ddn) enzyme bound cofactor F420 was investigated using UV-visible spectroscopy and computational simulations
Bicyclic nitroimidazoles have recently been discovered to be activated by a class of F420 dependent oxidoreductases (FDORs) called FDORAs,[2,4,6] which are thought to have a physiological role in reducing oxidative stress against mycobacteria during infection.[7]
While the deazaflavin F420 is structurally analogous to riboflavin based cofactors such as flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), it is functionally closer to nicotinamide (e.g. NAD) cofactors by being involved in redox reactions as a hydride carrier involved in two electron transfer mechanisms.[12]
Summary
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.
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