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

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

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

23 Citations (Scopus)

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.

Original language	English
Pages (from-to)	1110-1113
Number of pages	4
Journal	Molecular BioSystems
Volume	12
Issue number	4
DOIs	https://doi.org/10.1039/c6mb00033a
Publication status	Published - 2016

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10.1039/c6mb00033a

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

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.",

author = "Mohamed, \{A. Elaaf\} and Ahmed, \{F. Hafna\} and Sundaram Arulmozhiraja and Lin, \{Ching Y.\} and Taylor, \{Matthew C.\} and Krausz, \{Elmars R.\} and Jackson, \{Colin J.\} and Coote, \{Michelle L.\}",

note = "Publisher Copyright: {\textcopyright} The Royal Society of Chemistry 2016.",

year = "2016",

doi = "10.1039/c6mb00033a",

language = "English",

volume = "12",

pages = "1110--1113",

journal = "Molecular BioSystems",

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T1 - Protonation state of F420H2 in the prodrug-activating deazaflavin dependent nitroreductase (Ddn) from Mycobacterium tuberculosis

AU - Mohamed, A. Elaaf

AU - Ahmed, F. Hafna

AU - Arulmozhiraja, Sundaram

AU - Lin, Ching Y.

AU - Taylor, Matthew C.

AU - Krausz, Elmars R.

AU - Jackson, Colin J.

AU - Coote, Michelle L.

PY - 2016

Y1 - 2016

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/84962045955

U2 - 10.1039/c6mb00033a

DO - 10.1039/c6mb00033a

M3 - Article

SN - 1742-206X

VL - 12

SP - 1110

EP - 1113

JO - Molecular BioSystems

JF - Molecular BioSystems

IS - 4

ER -

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

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