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  1H NMR Spectroscopy of [FeFe] Hydrogenase: Insight into the Electronic Structure of the Active Site

Rumpel, S., Ravera, E., Sommer, C., Reijerse, E., Farès, C., Luchinat, C., et al. (2018). 1H NMR Spectroscopy of [FeFe] Hydrogenase: Insight into the Electronic Structure of the Active Site. Journal of the American Chemical Society, 140(1), 131-134. doi:10.1021/jacs.7b11196.

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Rumpel, Sigrun1, Author
Ravera, Enrico2, Author
Sommer, Constanze1, Author
Reijerse, Edward1, Author
Farès, Christophe3, Author           
Luchinat, Claudio2, Author
Lubitz, Wolfgang1, Author
Affiliations:
1Max-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr, Germany, ou_persistent22              
2Department of Chemistry “Ugo Schiff” and Magnetic Resonance Center (CERM), University of Florence and Interuniversity Consortium for Magnetic Resonance of Metallo Proteins (CIRMMP), Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy, ou_persistent22              
3Service Department Farès (NMR), Max-Planck-Institut für Kohlenforschung, Max Planck Society, ou_1445623              

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 Abstract: The [FeFe] hydrogenase HydA1 from Chlamydomonas reinhardtii has been studied using 1H NMR spectroscopy identifying the paramagnetically shifted 1H resonances associated with both the [4Fe-4S]H and the [2Fe]H subclusters of the active site “H-cluster”. The signal pattern of the unmaturated HydA1 containing only [4Fe-4S]H is reminiscent of bacterial-type ferredoxins. The spectra of maturated HydA1, with a complete H-cluster in the active Hox and the CO-inhibited Hox–CO state, reveal additional upfield and downfield shifted 1H resonances originating from the four methylene protons of the azadithiolate ligand in the [2Fe]H subsite. The two axial protons are affected by positive spin density, while the two equatorial protons experience negative spin density. These protons can be used as important probes sensing the effects of ligand-binding to the catalytic site of the H-cluster.

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Language(s): eng - English
 Dates: 2017-10-272017-12-062018-01-10
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/jacs.7b11196
 Degree: -

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Title: Journal of the American Chemical Society
  Other : JACS
  Abbreviation : J. Am. Chem. Soc.
Source Genre: Journal
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Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 140 (1) Sequence Number: - Start / End Page: 131 - 134 Identifier: ISSN: 0002-7863
CoNE: https://pure.mpg.de/cone/journals/resource/954925376870