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dc.contributor.authorMilton, Ross D.
dc.contributor.authorCai, Rong
dc.contributor.authorSahin, Selmihan
dc.contributor.authorAbdellaoui, Sofiene
dc.contributor.authorAlkotaini, Bassam
dc.contributor.authorLeech, Dónal
dc.contributor.authorMinteer, Shelley D.
dc.identifier.citationMilton, Ross D., Cai, Rong, Sahin, Selmihan, Abdellaoui, Sofiene, Alkotaini, Bassam, Leech, Dónal, & Minteer, Shelley D. (2017). The In Vivo Potential-Regulated Protective Protein of Nitrogenase in Azotobacter vinelandii Supports Aerobic Bioelectrochemical Dinitrogen Reduction In Vitro. Journal of the American Chemical Society, 139(26), 9044-9052. doi: 10.1021/jacs.7b04893en_IE
dc.description.abstractNitrogenase, the only enzyme known to be able to reduce dinitrogen (N-2) to ammonia (NH3), is irreversibly damaged upon exposure to molecular oxygen (O-2). Several microbes, however, are able to grow aerobically and diazotrophically (fixing N-2 to grow) while containing functional nitrogenase. The obligate aerobic diazotroph, Azotobacter vinelandii, employs a multitude of protective mechanisms to preserve nitrogenase activity, including a "conformational switch" protein (FeSII, or "Shethna") that reversibly locks nitrogenase into a multicomponent protective complex upon exposure to low concentrations of O-2. We demonstrate in vitro that nitrogenase can be oxidatively damaged under anoxic conditions and that the aforementioned conformational switch can protect nitrogenase from such damage, confirming that the conformational change in the protecting protein can be achieved solely by regulating the potential of its [2Fe-2S] cluster. We further demonstrate that this protective complex preserves nitrogenase activity upon exposure to air. Finally, this protective FeSII protein was incorporated into an O-2-tolerant bioelectrosynthetic cell whereby NH3 was produced using air as a substrate, marking a significant step forward in overcoming the crippling limitation of nitrogenase's sensitivity toward O-2.en_IE
dc.description.sponsorshipWe acknowledge Peter Flynn, Sarah Soss and Dennis Edwards of the D.M. Grant NMR Center (University of Utah) for assistance with NMR spectroscopy. This work is supported by a Marie Curie-Skłodowska Individual Fellowship (Global) under the European Commission’s Horizon 2020 Framework (project 654836, “Bioelectroammonia”: R.D.M., D.L. and S.D.M.) and the Army Research Office MURI. S.S. would like to thank TUBITAK (The Scientific and Technological Research Council of Turkey) for their support. We thank the research group of Vahe Bandarian for valuable advice on FeSII expression.en_IE
dc.publisherAmerican Chemical Societyen_IE
dc.relation.ispartofJournal Of The American Chemical Societyen
dc.subjectFESII PROTEINen_IE
dc.subjectOXYGEN DAMAGEen_IE
dc.subjectBIOFUEL CELLSen_IE
dc.titleThe in vivo potential-regulated protective protein of nitrogenase in azotobacter vinelandii supports aerobic bioelectrochemical dinitrogen reduction in vitroen_IE
dc.contributor.funderHorizon 2020en_IE
dc.contributor.funderH2020 Marie Skłodowska-Curie Actionsen_IE
dc.local.contactDonal Leech, School Of Chemistry, Room C228 Arts/Science Building, University Road, Nui Galway. 5349 Email:
dcterms.projectinfo:eu-repo/grantAgreement/EC/H2020::MSCA-IF-GF/654836/EU/Bioelectroreduction of nitrogen to ammonia: the incorporation of nitrogenase within enzymatic biological fuel cells for simultaneous production of electrical energy and ammonia./Bioelectroammoniaen_IE

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