Advanced Electron Paramagnetic Resonance and Density Functional Theory Study of a (2Fe3S) Cluster Mimicking the Active Site of [FeFe] Hydrogenase.
Despite extensive investigations of the active site of the [FeFe] hydrogenases, many details concerning the properties of the "hydrogen converting cluster" are not yet fully understood. The complexity of the so-called H-cluster is one of the main difficulties in studying the properties of its compon...
| Publicado en: | Journal of the American Chemical Society Vol. 132; no. 49; pp. 17578 - 17588 |
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| Autores principales: | , , , |
| Formato: | Artículo |
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American Chemical Society
12/15/2010
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| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=hlh&AN=56659051&site=ehost-live header: @attributes: shortDbName: hlh uiTerm: 56659051 longDbName: Humanities International Complete uiTag: AN controlInfo: bkinfo: jinfo: jid: 00027863 ACS jtl: Journal of the American Chemical Society issn: 00027863 maglogo: N pubinfo: dt: 12/15/2010 vid: 132 iid: 49 pid: 997 pub: American Chemical Society artinfo: ui: 56659051 10.1021/ja107793e ppf: 17578 ppct: 10 formats: tig: atl: Advanced Electron Paramagnetic Resonance and Density Functional Theory Study of a (2Fe3S) Cluster Mimicking the Active Site of [FeFe] Hydrogenase. aug: au: Silakov, Alexey Shaw, Jennifer L. Reijerse, Eduard J. Lubitz, Wolfgang affil: Max-Planck-Institut für Bioanorganische Chemie, Suftstrasse 34-36, Mülheim an der Ruhr, 45470, Germany su: Hydrogenase Electron paramagnetic resonance Density functionals Oxidation-reduction reaction Nuclear isomers Particles (Nuclear physics) sug: subj: Hydrogenase Electron paramagnetic resonance Density functionals Oxidation-reduction reaction Nuclear isomers Particles (Nuclear physics) ab: Despite extensive investigations of the active site of the [FeFe] hydrogenases, many details concerning the properties of the "hydrogen converting cluster" are not yet fully understood. The complexity of the so-called H-cluster is one of the main difficulties in studying the properties of its components. The present study is aimed at the mixed-valence EPA active [Fe(μ-CO)(CO)(CN)(MeSCHC(Me)(CHS))] that is structurally closely related to the redox active binuclear part of the H-cluster in its CO-inhibited oxidized state. In this work, we present a characterization of this compound by advanced pulse EPR methods. The accurate determination of the Fe, ¹H, ²H, N, and N electron nuclear hyperfine interactions provided a very detailed picture of the electronic structure of this complex. A theoretical study using density functional theory (DFT) calculations identified possible isomers of the compound and further refined the knowledge about its properties. It was found that upon one electron oxidation of the parent Fe(I)-Fe(I) complex, the dominant mixed-valence Fe(I)-Fe(II) species is the one in which the CN ligand of the iron center that is distal to the thioether moves from the basal to the apical position. The unpaired spin distribution of the model complex is found to be clearly different from that of the native H-cluster. These differences are discussed and provide new insight into the functional features of the [FeFe] hydrogenase active site. pubtype: Academic Journal doctype: Article src: R language: English refInfo: copyright: @attributes: flag: Y dt: @attributes: year: 2010 holdings: @attributes: islocal: N |
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