ArticleDalton transactions (Cambridge, England : 2003)2010
The iron-site structure of [Fe]-hydrogenase and model systems: an X-ray absorption near edge spectroscopy study.
Article in Dalton transactions (Cambridge, England : 2003), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Bioinspired Framework Catalysts: From Enzyme Immobilization to Biomimetic Catalysis.Chemical reviews · 2023Review
- Radical S-adenosyl-L-methionine chemistry in the synthesis of hydrogenase and nitrogenase metal cofactors.The Journal of biological chemistry · 2015Review
- EPR/ENDOR, Mössbauer, and quantum-chemical investigations of diiron complexes mimicking the active oxidized state of [FeFe]hydrogenase.Inorganic chemistry · 2012Article
- O2 reactions at the six-iron active site (H-cluster) in [FeFe]-hydrogenase.The Journal of biological chemistry · 2011Article
- Iron acyl thiolato carbonyls: structural models for the active site of the [Fe]-hydrogenase (Hmd).Journal of the American Chemical Society · 2010Article
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Abstract
The [Fe]-hydrogenase is an ideal system for studying the electronic properties of the low spin iron site that is common to the catalytic centres of all hydrogenases. Because they have no auxiliary iron-sulfur clusters and possess a cofactor containing a single iron centre, the [Fe]-hydrogenases are well suited for spectroscopic analysis of those factors required for the activation of molecular hydrogen. Specifically, in this study we shed light on the electronic and molecular structure of the iron centre by XAS analysis of [Fe]-hydrogenase from Methanocaldococcus jannashii and five model complexes (Fe(ethanedithiolate)(CO)(2)(PMe(3))(2), [K(18-crown-6)](2)[Fe(CN)(2)(CO)(3)], K[Fe(CN)(CO)(4)], K(3)[Fe(III)(CN)(6)], K(4)[Fe(II)(CN)(6)]). The different electron donors have a strong influence on the iron absorption K-edge energy position, which is frequently used to determine the metal oxidation state. Our results demonstrate that the K-edges of Fe(II) complexes, achieved with low-spin ferrous thiolates, are consistent with a ferrous centre in the [Fe]-hydrogenase from Methanocaldococcus jannashii. The metal geometry also strongly influences the XANES and thus the electronic structure. Using in silico simulation, we were able to reproduce the main features of the XANES spectra and describe the effects of individual donor contributions on the spectra. Thereby, we reveal the essential role of an unusual carbon donor coming from an acyl group of the cofactor in the determination of the electronic structure required for the activity of the enzyme.
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