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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Main Authors: Christin Radon, Gerd Mittelstädt, Benjamin R. Duffus, Jörg Bürger, Tobias Hartmann, Thorsten Mielke, Christian Teutloff, Silke Leimkühler, Petra Wendler
Format: Article
Language:English
Published: Nature Publishing Group 2020-04-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-020-15614-0
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spelling 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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