Mohamed, Ahmed ElaafAhmed, FathimathArulmozhiraja, SundaramLin, Ching YehTaylor, Matthew C.Krausz, ElmarsJackson, ColinCoote, Michelle2021-10-292021-10-291742-206Xhttp://hdl.handle.net/1885/251302The 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.MLC and CJJ gratefully acknowledge funding from the Australian Research Council in the form of Discovery Project funding (DP130102144) and ARC Future Fellowships. MLC also acknowledges generous allocations of supercomputing time on the National Facility of the Australian National Computational Infrastructure.application/pdfen-AU© 2016 The Royal Society of Chemistryhttps://creativecommons.org/licenses/by/3.0/201610.1039/c6mb00033aCreative Commons Attribution 3.0 Unported (CC BY 3.0)