The electronic structure of FeV-cofactor in vanadium-dependent nitrogenase

Simple item page
dc.contributor.authorYang, Zhi-Yongen
dc.contributor.authorJimenez-Vicente, Emilioen
dc.contributor.authorKallas, Haydenen
dc.contributor.authorLukoyanov, Dmitriy A.en
dc.contributor.authorYang, Haoen
dc.contributor.authorDel Campo, Julia S. Martinen
dc.contributor.authorDean, Dennis R.en
dc.contributor.authorHoffman, Brian M.en
dc.contributor.authorSeefeldt, Lance C.en
dc.contributor.departmentBiochemistryen
dc.date.accessioned2021-08-18T18:57:14Zen
dc.date.available2021-08-18T18:57:14Zen
dc.date.issued2021-03-29en
dc.date.updated2021-08-18T18:57:12Zen
dc.description.abstractThe electronic structure of the active-site metal cofactor (FeV-cofactor) of resting-state V-dependent nitrogenase has been an open question, with earlier studies indicating that it exhibits a broad S = 3/2 EPR signal (Kramers state) having g values of ∼4.3 and 3.8, along with suggestions that it contains metal-ions with valencies [1V3+, 3Fe3+, 4Fe2+]. In the present work, genetic, biochemical, and spectroscopic approaches were combined to reveal that the EPR signals previously assigned to FeV-cofactor do not correlate with active VFe-protein, and thus cannot arise from the resting-state of catalytically relevant FeV-cofactor. It, instead, appears resting-state FeV-cofactor is either diamagnetic, S = 0, or non-Kramers, integer-spin (S = 1, 2 etc.). When VFe-protein is freeze-trapped during high-flux turnover with its natural electron-donating partner Fe protein, conditions which populate reduced states of the FeV-cofactor, a new rhombic S = 1/2 EPR signal from such a reduced state is observed, with g = [2.18, 2.12, 2.09] and showing well-defined 51V (I = 7/2) hyperfine splitting, aiso = 110 MHz. These findings indicate a different assignment for the electronic structure of the resting state of FeV-cofactor: S = 0 (or integer-spin non-Kramers state) with metal-ion valencies, [1V3+, 4Fe3+, 3Fe2+]. Our findings suggest that the V3+ does not change valency throughout the catalytic cycle.en
dc.description.versionPublished versionen
dc.format.extentPages 6913-6922en
dc.format.extent10 page(s)en
dc.format.mimetypeapplication/pdfen
dc.identifier.doihttps://doi.org/10.1039/d0sc06561gen
dc.identifier.eissn2041-6539en
dc.identifier.issn2041-6520en
dc.identifier.issue20en
dc.identifier.orcidDean, Dennis [0000-0001-8960-6196]en
dc.identifier.otherd0sc06561g (PII)en
dc.identifier.pmid34123320 (pubmed)en
dc.identifier.urihttp://hdl.handle.net/10919/104671en
dc.identifier.volume12en
dc.language.isoenen
dc.publisherRoyal Society of Chemistryen
dc.relation.urihttp://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000641868400001&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=930d57c9ac61a043676db62af60056c1en
dc.rightsCreative Commons Attribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.subjectPhysical Sciencesen
dc.subjectChemistry, Multidisciplinaryen
dc.subjectChemistryen
dc.subject03 Chemical Sciencesen
dc.titleThe electronic structure of FeV-cofactor in vanadium-dependent nitrogenaseen
dc.title.serialChemical Scienceen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten
dc.type.otherArticleen
dc.type.otherJournalen
pubs.organisational-group/Virginia Techen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciencesen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciences/Biochemistryen
pubs.organisational-group/Virginia Tech/University Distinguished Professorsen
pubs.organisational-group/Virginia Tech/University Research Institutesen
pubs.organisational-group/Virginia Tech/University Research Institutes/Fralin Life Sciencesen
pubs.organisational-group/Virginia Tech/Faculty of Health Sciencesen
pubs.organisational-group/Virginia Tech/All T&R Facultyen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciences/CALS T&R Facultyen
pubs.organisational-group/Virginia Tech/University Research Institutes/Fralin Life Sciences/Durelle Scotten

Files

Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
The electronic structure of FeV-cofactor in vanadium-dependent nitrogenase.pdf
Size:
1.04 MB
Format:
Adobe Portable Document Format
Description:
Published version
Download

Collections

All Faculty Deposits
Scholarly Works, Biochemistry