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  Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase

Radon, C., Mittelstädt, G., Duffus, B. R., Bürger, J., Hartmann, T., Mielke, T., et al. (2020). Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase. Nature Communications, 11: 1912. doi:10.1038/s41467-020-15614-0.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0006-4E44-7 Version Permalink: http://hdl.handle.net/21.11116/0000-0006-4E45-6
Genre: Journal Article

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 Creators:
Radon, Christin , Author
Mittelstädt, Gerd , Author
Duffus, Benjamin R. , Author
Bürger, Jörg1, 2, Author              
Hartmann, Tobias , Author
Mielke, Thorsten1, Author              
Teutloff, Christian , Author
Leimkühler, Silke, Author
Wendler, Petra, Author
Affiliations:
1Microscopy and Cryo-Electron Microscopy (Head: Thorsten Mielke), Scientific Service (Head: Christoph Krukenkamp), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479668              
2Charité, Institut für Medizinische Physik undBiophysik, Charitéplatz 1, 10117 Berlin, Germany, ou_persistent22              

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Free keywords: Biocatalysis, Enzyme mechanisms, Cryoelectron microscopy
 Abstract: Metal-containing formate dehydrogenases (FDH) catalyse the reversible oxidation of formate to carbon dioxide at their molybdenum or tungsten active site. They display a diverse subunit and cofactor composition, but structural information on these enzymes is limited. Here we report the cryo-electron microscopic structures of the soluble Rhodobacter capsulatus FDH (RcFDH) as isolated and in the presence of reduced nicotinamide adenine dinucleotide (NADH). RcFDH assembles into a 360 kDa dimer of heterotetramers revealing a putative interconnection of electron pathway chains. In the presence of NADH, the RcFDH structure shows charging of cofactors, indicative of an increased electron load.

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Language(s): eng - English
 Dates: 2020-03-192020-04-20
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: DOI: 10.1038/s41467-020-15614-0
 Degree: -

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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 11 Sequence Number: 1912 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723