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

doi:10.1039/C6MB00033A

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

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

Author affiliations

* Corresponding authors

^a Research School of Chemistry, The Australian National University, Canberra, ACT 2601, Australia
E-mail: colin.jackson@anu.edu.au, michelle.coote@anu.edu.au

^b CSIRO Land and Water, Black Mountain Laboratories, Canberra, ACT 2601, Australia

^c ARC Centre of Excellence for Electromaterials Science,

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.

This article is part of the themed collection: Chemical Biology in Molecular BioSystems

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Article information

DOI: https://doi.org/10.1039/C6MB00033A
Article type: Communication
Submitted: 15 Janv. 2016
Accepted: 09 Febr. 2016
First published: 09 Febr. 2016
This article is Open Access

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Mol. BioSyst., 2016,12, 1110-1113

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

A. E. Mohamed, F. H. Ahmed, S. Arulmozhiraja, C. Y. Lin, M. C. Taylor, E. R. Krausz, C. J. Jackson and M. L. Coote, Mol. BioSyst., 2016, 12, 1110 DOI: 10.1039/C6MB00033A

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Molecular BioSystems