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Issue 4, 2016
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Protonation state of F420H2 in the prodrug-activating deazaflavin dependent nitroreductase (Ddn) from Mycobacterium tuberculosis

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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.

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

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Article information


Submitted
15 Jan 2016
Accepted
09 Feb 2016
First published
09 Feb 2016

This article is Open Access

Mol. BioSyst., 2016,12, 1110-1113
Article type
Communication

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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