Infrared spectroscopy of the nitrogenase MoFe protein under electrochemical control: potential-triggered CO binding

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dc.contributor.authorPaengnakorn, P.en
dc.contributor.authorAsh, P. A.en
dc.contributor.authorShaw, S.en
dc.contributor.authorDanyal, K.en
dc.contributor.authorChen, T.en
dc.contributor.authorDean, Dennis R.en
dc.contributor.authorSeefeldt, Lance C.en
dc.contributor.authorVincent, K. A.en
dc.contributor.departmentBiochemistryen
dc.contributor.departmentVirginia Tech. Fralin Life Sciences Instituteen
dc.contributor.departmentBiochemistryen
dc.date.accessioned2017-05-01T06:42:16Zen
dc.date.available2017-05-01T06:42:16Zen
dc.date.issued2016-10-27en
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.en
dc.format.extent1500-1505en
dc.format.mimetypeapplication/pdfen
dc.identifierc6sc02860h.pdfen
dc.identifierc6sc02860h1.pdfen
dc.identifier.doihttps://doi.org/10.1039/c6sc02860hen
dc.identifier.eissn2041-6539en
dc.identifier.issn2041-6520en
dc.identifier.issue2en
dc.identifier.urihttp://hdl.handle.net/10919/77546en
dc.identifier.volume8en
dc.language.isoenen
dc.publisherRoyal Society of Chemistryen
dc.relation.ispartofRoyal Society of Chemistry Gold Open Access - 2016en
dc.rightsCreative Commons Attribution 3.0 Unporteden
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.rights.urihttp://creativecommons.org/licenses/by/3.0/en
dc.titleInfrared spectroscopy of the nitrogenase MoFe protein under electrochemical control: potential-triggered CO bindingen
dc.title.serialChemical Scienceen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten
dc.type.dcmitypeDataseten

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