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A Model of the [FeFe] Hydrogenase Active Site with a Biologically Relevant Azadithiolate Bridge: A Spectroscopic and Theoretical Investigation
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Photochemistry and Molecular Science.
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2011 (English)In: Angewandte Chemie International Edition, ISSN 1433-7851, E-ISSN 1521-3773, Vol. 50, no 6, 1439-1443 p.Article in journal (Refereed) Published
Abstract [en]

Convincing evidence for the presence of a nitrogen atom in the dithiolate bridge of the active site of native [FeFe] hydrogenases (B) is provided by a spectroscopic, electrochemical, and theoretical study of a well-characterized structural mimic of the [FeFe] hydrogenase subcluster (picture: 14N matched-HYSCORE spectrum of the model compound A). This result should help to understand the mechanism of dihydrogen conversion and production.

Place, publisher, year, edition, pages
2011. Vol. 50, no 6, 1439-1443 p.
Keyword [en]
density functional calculations, ENDOR spectroscopy, enzyme models, EPR spectroscopy, hydrogenases
National Category
Chemical Sciences
URN: urn:nbn:se:uu:diva-149081DOI: 10.1002/anie.201006244ISI: 000287161600043PubMedID: 21290530OAI: oai:DiVA.org:uu-149081DiVA: diva2:404008
Available from: 2011-03-15 Created: 2011-03-15 Last updated: 2012-10-01

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Ott, Sascha
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