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

A. Elaaf Mohamed, F. Hafna Ahmed, Sundaram Arulmozhiraja, Ching Y. Lin, Matthew C. Taylor, Elmars R. Krausz, Colin J. Jackson, Michelle L. Coote

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)1110-1113
Number of pages4
JournalMolecular BioSystems
Volume12
Issue number4
DOIs
Publication statusPublished - 2016
Externally publishedYes

Keywords

  • protonation
  • deazaflavin
  • nitroreductase
  • enzyme
  • spectroscopy
  • holoenzyme

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