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
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oai:doaj.org-article:ee6fb5dae1e445018b0579d6448937222021-12-02T14:42:48ZCryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase10.1038/s41467-020-15614-02041-1723https://doaj.org/article/ee6fb5dae1e445018b0579d6448937222020-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-15614-0https://doaj.org/toc/2041-1723Rhodobacter 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.Christin RadonGerd MittelstädtBenjamin R. DuffusJörg BürgerTobias HartmannThorsten MielkeChristian TeutloffSilke LeimkühlerPetra WendlerNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-9 (2020) |
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Science Q 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 |
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. |
format |
article |
author |
Christin Radon Gerd Mittelstädt Benjamin R. Duffus Jörg Bürger Tobias Hartmann Thorsten Mielke Christian Teutloff Silke Leimkühler Petra Wendler |
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 Portfolio |
publishDate |
2020 |
url |
https://doaj.org/article/ee6fb5dae1e445018b0579d644893722 |
work_keys_str_mv |
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