Advanced electron paramagnetic resonance and density functional theory study of a {2Fe3S} cluster mimicking the active site of [FeFe] hydrogenase

Alexey Silakov, Jennifer L. Shaw, Eduard J. Reijerse, Wolfgang Lubitz

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

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 EPR active [Fe2(μ-CO)(CO)3(CN)2{MeSCH 2C(Me)(CH2S)2}]1- 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 57Fe, 1H, 2H, 14N, and 15N 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.

Original languageEnglish (US)
Pages (from-to)17578-17587
Number of pages10
JournalJournal of the American Chemical Society
Volume132
Issue number49
DOIs
StatePublished - Dec 15 2010

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Hydrogenase
Electron Spin Resonance Spectroscopy
Carbon Monoxide
Density functional theory
Paramagnetic resonance
Catalytic Domain
Electrons
Isomers
Electronic structure
Ligands
Sulfides
Iron
Oxidation
Hydrogen
Oxidation-Reduction
Theoretical Models

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

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title = "Advanced electron paramagnetic resonance and density functional theory study of a {2Fe3S} cluster mimicking the active site of [FeFe] hydrogenase",
abstract = "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 EPR active [Fe2(μ-CO)(CO)3(CN)2{MeSCH 2C(Me)(CH2S)2}]1- 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 57Fe, 1H, 2H, 14N, and 15N 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.",
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Advanced electron paramagnetic resonance and density functional theory study of a {2Fe3S} cluster mimicking the active site of [FeFe] hydrogenase. / Silakov, Alexey; Shaw, Jennifer L.; Reijerse, Eduard J.; Lubitz, Wolfgang.

In: Journal of the American Chemical Society, Vol. 132, No. 49, 15.12.2010, p. 17578-17587.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Advanced electron paramagnetic resonance and density functional theory study of a {2Fe3S} cluster mimicking the active site of [FeFe] hydrogenase

AU - Silakov, Alexey

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AU - Lubitz, Wolfgang

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