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dc.contributor.authorPaengnakorn, P.
dc.contributor.authorAsh, P. A.
dc.contributor.authorShaw, S.
dc.contributor.authorDanyal, K.
dc.contributor.authorChen, T.
dc.contributor.authorDean, Dennis R.
dc.contributor.authorSeefeldt, Lance C.
dc.contributor.authorVincent, K. A.
dc.date.accessioned2017-05-01T06:42:16Z
dc.date.available2017-05-01T06:42:16Z
dc.date.issued2016-10-27
dc.identifierc6sc02860h.pdf
dc.identifierc6sc02860h1.pdf
dc.identifier.issn2041-6520
dc.identifier.urihttp://hdl.handle.net/10919/77546
dc.description.abstractWe demonstrate electrochemical control of the nitrogenase MoFe protein, in the absence of Fe protein or ATP, using europium(III/II) polyaminocarboxylate complexes as electron transfer mediators. This allows the potential dependence of proton reduction and inhibitor (CO) binding to the active site FeMo-cofactor to be established. Reduction of protons to H2 is catalyzed by the wild type MoFe protein and β-98Tyr→His and β-99Phe→His variants of the MoFe protein at potentials more negative than −800 mV (vs. SHE), with greater electrocatalytic proton reduction rates observed for the variants compared to the wild type protein. Electrocatalytic proton reduction is strongly attenuated by carbon monoxide (CO), and the potential-dependence of CO binding to the FeMo-cofactor is determined by in situ infrared (IR) spectroelectrochemistry. The vibrational wavenumbers for CO coordinated to the FeMo-cofactor are consistent with earlier IR studies on the MoFe protein with Fe protein/ATP as reductant showing that electrochemically generated states of the protein are closely related to states generated with the native Fe protein as electron donor.
dc.format.extent1500-1505
dc.format.mimetypeapplication/pdf
dc.language.isoen_US
dc.publisherRoyal Society of Chemistry
dc.relation.ispartofRoyal Society of Chemistry Gold Open Access - 2016
dc.rightsCreative Commons Attribution 3.0 Unporteden
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/en
dc.titleInfrared spectroscopy of the nitrogenase MoFe protein under electrochemical control: potential-triggered CO binding
dc.typeArticle - Refereed
dc.rights.holderPaengnakorn, P.en
dc.rights.holderAsh, P. A.en
dc.rights.holderShaw, S.en
dc.rights.holderDanyal, K.en
dc.rights.holderChen, T.en
dc.rights.holderDean, D. R.en
dc.rights.holderSeefeldt, L. C.en
dc.rights.holderVincent, K. A.en
dc.contributor.departmentVirginia Tech. Department of Biochemistry
dc.contributor.departmentVirginia Tech. Fralin Life Science Institute
dc.contributor.departmentBiochemistryen_US
dc.title.serialChemical Science
dc.identifier.doihttps://doi.org/10.1039/c6sc02860h
dc.identifier.volume8
dc.identifier.issue2
dc.type.dcmitypeText
dc.type.dcmitypeDataset
dc.identifier.eissn2041-6539


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Creative Commons Attribution 3.0 Unported
License: Creative Commons Attribution 3.0 Unported