Protonation State of F420H2 in the Prodrug-activating Deazaflavin Dependent Nitroreductase (Ddn) from Mycobacterium Tuberculosis

Overview

Journal Mol Biosyst

Publisher Royal Society of Chemistry

Specialties Biochemistry
Molecular Biology

Date 2016 Feb 16

PMID 26876228

Citations 8

Authors

A Elaaf Mohamed

F Hafna Ahmed

Sundaram Arulmozhiraja

Ching Y Lin

Matthew C Taylor

Elmars R Krausz

Colin J Jackson

Michelle L Coote

Affiliations

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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.

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