| Literature DB >> 26876228 |
A Elaaf Mohamed1, F Hafna Ahmed, Sundaram Arulmozhiraja, Ching Y Lin, Matthew C Taylor, Elmars R Krausz, Colin J Jackson, Michelle L Coote.
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.Entities:
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Year: 2016 PMID: 26876228 DOI: 10.1039/c6mb00033a
Source DB: PubMed Journal: Mol Biosyst ISSN: 1742-2051