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  Electronic structure of the unique [4Fe-3S] cluster in O2-tolerant hydrogenases characterized by 57Fe Mössbauer and EPR spectroscopy

Pandelia, M.-E., Bykov, D., Izsak, R., Infossi, P., Giudici-Orticoni, M.-T., Bill, E., et al. (2013). Electronic structure of the unique [4Fe-3S] cluster in O2-tolerant hydrogenases characterized by 57Fe Mössbauer and EPR spectroscopy. Proceedings of the National Academy of Sciences of the United States of America, 110(2), 483-488. doi:10.1073/pnas.1202575110.

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Pandelia, Maria-Eirini1, Author           
Bykov, Dmytro2, Author           
Izsak, Robert2, Author           
Infossi, Pascale3, Author
Giudici-Orticoni, Marie-Thérèse3, Author
Bill, Eckhard2, Author           
Neese, Frank2, Author           
Lubitz, Wolfgang1, Author           
Affiliations:
1Research Department Lubitz, Max Planck Institute for Chemical Energy Conversion, Max Planck Society, ou_3023873              
2Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society, ou_3023886              
3Laboratoire de Bioénergétique et Ingénierie des Protéines, Centre National de la Recherche Scientifique, Aix-Marseille University, 13402 Marseille Cedex 20, France, ou_persistent22              

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 Abstract: Iron–sulfur clusters are ubiquitous electron transfer cofactors in hydrogenases. Their types and redox properties are important for H2 catalysis, but, recently, their role in a protection mechanism against oxidative inactivation has also been recognized for a [4Fe-3S] cluster in O2-tolerant group 1 [NiFe] hydrogenases. This cluster, which is uniquely coordinated by six cysteines, is situated in the proximity of the catalytic [NiFe] site and exhibits unusual redox versatility. The [4Fe-3S] cluster in hydrogenase (Hase) I from Aquifex aeolicus performs two redox transitions within a very small potential range, forming a superoxidized state above +200 mV vs. standard hydrogen electrode (SHE). Crystallographic data has revealed that this state is stabilized by the coordination of one of the iron atoms to a backbone nitrogen. Thus, the proximal [4Fe-3S] cluster undergoes redox-dependent changes to serve multiple purposes beyond classical electron transfer. In this paper, we present field-dependent 57Fe-Mössbauer and EPR data for Hase I, which, in conjunction with spectroscopically calibrated density functional theory (DFT) calculations, reveal the distribution of Fe valences and spin-coupling schemes for the iron–sulfur clusters. The data demonstrate that the electronic structure of the [4Fe-3S] core in its three oxidation states closely resembles that of corresponding conventional [4Fe-4S] cubanes, albeit with distinct differences for some individual iron sites. The medial and distal iron–sulfur clusters have similar electronic properties as the corresponding cofactors in standard hydrogenases, although their redox potentials are higher.

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Language(s): eng - English
 Dates: 2013-01-08
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.1202575110
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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : PNAS
  Other : Proceedings of the National Academy of Sciences of the USA
  Abbreviation : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 110 (2) Sequence Number: - Start / End Page: 483 - 488 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230