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

Mol Biosyst. 2016 Apr;12(4):1110-3. doi: 10.1039/c6mb00033a. Epub 2016 Feb 15.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Hydrogen-Ion Concentration
  • Models, Molecular
  • Molecular Conformation
  • Molecular Structure
  • Mycobacterium tuberculosis / enzymology*
  • Nitroreductases / chemistry*
  • Nitroreductases / metabolism
  • Prodrugs / chemistry*
  • Prodrugs / metabolism
  • Protons*
  • Quinone Reductases / chemistry*

Substances

  • Prodrugs
  • Protons
  • coenzyme F420H2 - 2,3-dimethyl-1,4-naphthoquinone oxidoreductase
  • Quinone Reductases
  • Nitroreductases