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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 Krausz,Colin J. Jackson,Michelle L. Coote

MOLECULAR BIOSYSTEMS（2016）

Cited 19|Views8
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Abstract
The protonation state of the deazaflavin dependent nitroreductase (Ddn) enzyme bound cofactor F-420 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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Key words
dependent nitroreductase,tuberculosis,deazaflavin,ddn,prodrug-activating
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