Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase
Rhodobacter capsulatus NAD+ dependent formate dehydrogenase (RcFDH) is a molybdoenzyme that catalyses the reversible oxidation of formate to carbon dioxide, and is of interest for biotechnological applications. Here the authors present the cryo-EM structures of RcFDH as isolated from R. capsulatus a...
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2020-04-01
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Online Access: | https://doi.org/10.1038/s41467-020-15614-0 |
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doaj-ee6fb5dae1e445018b0579d6448937222021-05-11T08:12:00ZengNature Publishing GroupNature Communications2041-17232020-04-011111910.1038/s41467-020-15614-0Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenaseChristin Radon0Gerd Mittelstädt1Benjamin R. Duffus2Jörg Bürger3Tobias Hartmann4Thorsten Mielke5Christian Teutloff6Silke Leimkühler7Petra Wendler8Institute of Biochemistry and Biology, Department of Biochemistry, University of PotsdamInstitute of Biochemistry and Biology, Department of Molecular Enzymology, University of PotsdamInstitute of Biochemistry and Biology, Department of Molecular Enzymology, University of PotsdamMax-Planck Institute of Molecular GeneticsInstitute of Biochemistry and Biology, Department of Molecular Enzymology, University of PotsdamMax-Planck Institute of Molecular GeneticsDepartment of Physics, Freie Universität BerlinInstitute of Biochemistry and Biology, Department of Molecular Enzymology, University of PotsdamInstitute of Biochemistry and Biology, Department of Biochemistry, University of PotsdamRhodobacter capsulatus NAD+ dependent formate dehydrogenase (RcFDH) is a molybdoenzyme that catalyses the reversible oxidation of formate to carbon dioxide, and is of interest for biotechnological applications. Here the authors present the cryo-EM structures of RcFDH as isolated from R. capsulatus and in the reduced state with bound NADH, and discuss the enzyme mechanism.https://doi.org/10.1038/s41467-020-15614-0 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Christin Radon Gerd Mittelstädt Benjamin R. Duffus Jörg Bürger Tobias Hartmann Thorsten Mielke Christian Teutloff Silke Leimkühler Petra Wendler |
spellingShingle |
Christin Radon Gerd Mittelstädt Benjamin R. Duffus Jörg Bürger Tobias Hartmann Thorsten Mielke Christian Teutloff Silke Leimkühler Petra Wendler Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase Nature Communications |
author_facet |
Christin Radon Gerd Mittelstädt Benjamin R. Duffus Jörg Bürger Tobias Hartmann Thorsten Mielke Christian Teutloff Silke Leimkühler Petra Wendler |
author_sort |
Christin Radon |
title |
Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase |
title_short |
Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase |
title_full |
Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase |
title_fullStr |
Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase |
title_full_unstemmed |
Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase |
title_sort |
cryo-em structures reveal intricate fe-s cluster arrangement and charging in rhodobacter capsulatus formate dehydrogenase |
publisher |
Nature Publishing Group |
series |
Nature Communications |
issn |
2041-1723 |
publishDate |
2020-04-01 |
description |
Rhodobacter capsulatus NAD+ dependent formate dehydrogenase (RcFDH) is a molybdoenzyme that catalyses the reversible oxidation of formate to carbon dioxide, and is of interest for biotechnological applications. Here the authors present the cryo-EM structures of RcFDH as isolated from R. capsulatus and in the reduced state with bound NADH, and discuss the enzyme mechanism. |
url |
https://doi.org/10.1038/s41467-020-15614-0 |
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