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

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Date

2016

Authors

Mohamed, Ahmed Elaaf
Ahmed, Fathimath
Arulmozhiraja, Sundaram
Lin, Ching Yeh
Taylor, Matthew C.
Krausz, Elmars
Jackson, Colin
Coote, Michelle

Journal Title

Journal ISSN

Volume Title

Publisher

The Royal Society of Chemistry

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.

Description

Keywords

Citation

URI

http://hdl.handle.net/1885/251302

Collections

ANU Research Publications

Source

Molecular BioSystems

Type

Journal article

Book Title

Entity type

Access Statement

Open Access

License Rights

Creative Commons Attribution 3.0 Unported (CC BY 3.0)

DOI

10.1039/c6mb00033a

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