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

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dc.contributor.authorMohamed, Ahmed Elaaf
dc.contributor.authorAhmed, Fathimath
dc.contributor.authorArulmozhiraja, Sundaram
dc.contributor.authorLin, Ching Yeh
dc.contributor.authorTaylor, Matthew C.
dc.contributor.authorKrausz, Elmars
dc.contributor.authorJackson, Colin
dc.contributor.authorCoote, Michelle
dc.date.accessioned2021-10-29T04:10:55Z
dc.date.available2021-10-29T04:10:55Z
dc.date.issued2016
dc.description.abstractThe 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.en_AU
dc.description.sponsorshipMLC 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.en_AU
dc.format.mimetypeapplication/pdfen_AU
dc.identifier.issn1742-206Xen_AU
dc.identifier.urihttp://hdl.handle.net/1885/251302
dc.language.isoen_AUen_AU
dc.provenanceThis article is licensed under a Creative Commons Attribution 3.0 Unported Licence.en_AU
dc.publisherThe Royal Society of Chemistryen_AU
dc.relationhttp://purl.org/au-research/grants/arc/DP130102144en_AU
dc.rights© 2016 The Royal Society of Chemistryen_AU
dc.rights.licenseCreative Commons Attribution 3.0 Unported (CC BY 3.0)en_AU
dc.rights.urihttps://creativecommons.org/licenses/by/3.0/en_AU
dc.sourceMolecular BioSystemsen_AU
dc.titleProtonation state of F420H2 in the prodrug-activating deazaflavin dependent nitroreductase (Ddn) from Mycobacterium tuberculosisen_AU
dc.typeJournal articleen_AU
dcterms.accessRightsOpen Accessen_AU
dcterms.dateAccepted2016-02-09
local.bibliographicCitation.issue4en_AU
local.bibliographicCitation.lastpage1113en_AU
local.bibliographicCitation.startpage1110en_AU
local.contributor.affiliationMohamed, Elaaf, Research School of Chemistry, ANUen_AU
local.contributor.affiliationAhmed, Fathimath, Research School of Chemistry, ANUen_AU
local.contributor.affiliationArulmozhiraja, Sundaram, Research School of Chemistry, ANUen_AU
local.contributor.affiliationLin, Ching-Yeh, Research School of Chemistry, ANUen_AU
local.contributor.affiliationTaylor, Matthew C., Commonwealth Scientific and Industrial Research Organisation Land and Water Flagshipen_AU
local.contributor.affiliationKrausz, Elmars, Research School of Chemistry, ANUen_AU
local.contributor.affiliationJackson, Colin, Research School of Chemistry, ANUen_AU
local.contributor.affiliationCoote, Michelle, Research School of Chemistry, ANUen_AU
local.contributor.authoruidMohamed, Elaaf, u4477422en_AU
local.contributor.authoruidAhmed, Fathimath, u4463232en_AU
local.contributor.authoruidArulmozhiraja, Sundaram, u4633119en_AU
local.contributor.authoruidLin, Ching-Yeh, u4169280en_AU
local.contributor.authoruidKrausz, Elmars, u8102117en_AU
local.contributor.authoruidJackson, Colin, u4040768en_AU
local.contributor.authoruidCoote, Michelle, u4031074en_AU
local.description.notesAdded manually as didn't come across from ARIESen_AU
local.identifier.absfor320800en_AU
local.identifier.absfor340700en_AU
local.identifier.ariespublicationU3488905xPUB15682en_AU
local.identifier.citationvolume12en_AU
local.identifier.doi10.1039/c6mb00033aen_AU
local.publisher.urlhttps://pubs.rsc.org/en_AU
local.type.statusPublished Versionen_AU

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