title: Protonation state of F420H2 in the prodrug-activating deazaflavin dependent nitroreductase (Ddn) from Mycobacterium tuberculosis.
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.
authors.affiliation: Research School of Chemistry, The Australian National University, Canberra, ACT 2601, Australia. colin.jackson@anu.edu.au michelle.coote@anu.edu.au.
authors.forename: A Elaaf
authors.initials: AE
authors.lastname: Mohamed
authors.forename: F Hafna
authors.initials: FH
authors.lastname: Ahmed
authors.forename: Sundaram
authors.initials: S
authors.lastname: Arulmozhiraja
authors.forename: Ching Y
authors.initials: CY
authors.lastname: Lin
authors.forename: Matthew C
authors.initials: MC
authors.lastname: Taylor
authors.forename: Elmars R
authors.initials: ER
authors.lastname: Krausz
authors.forename: Colin J
authors.initials: CJ
authors.lastname: Jackson
authors.forename: Michelle L
authors.initials: ML
authors.lastname: Coote
mesh_terms: D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D008968:Molecular Conformation; D015394:Molecular Structure; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D009601:Nitroreductases / Q000737:chemistry* / Q000378:metabolism; D011355:Prodrugs / Q000737:chemistry* / Q000378:metabolism; D011522:Protons; D011808:Quinone Reductases / Q000737:chemistry*
chemical_list: D011355:Prodrugs; D011522:Protons; C088764:coenzyme F420H2 - 2,3-dimethyl-1,4-naphthoquinone oxidoreductase; D011808:Quinone Reductases; D009601:Nitroreductases