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

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...

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Autores principales: Radon, Christin, Mittelstädt, Gerd, Duffus, Benjamin R., Bürger, Jörg, Hartmann, Tobias, Mielke, Thorsten, Teutloff, Christian, Leimkühler, Silke, Wendler, Petra
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2020
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7171172/
https://www.ncbi.nlm.nih.gov/pubmed/32313256
http://dx.doi.org/10.1038/s41467-020-15614-0
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author Radon, Christin
Mittelstädt, Gerd
Duffus, Benjamin R.
Bürger, Jörg
Hartmann, Tobias
Mielke, Thorsten
Teutloff, Christian
Leimkühler, Silke
Wendler, Petra
author_facet Radon, Christin
Mittelstädt, Gerd
Duffus, Benjamin R.
Bürger, Jörg
Hartmann, Tobias
Mielke, Thorsten
Teutloff, Christian
Leimkühler, Silke
Wendler, Petra
author_sort Radon, Christin
collection PubMed
description 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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spelling pubmed-71711722020-04-23 Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase Radon, Christin Mittelstädt, Gerd Duffus, Benjamin R. Bürger, Jörg Hartmann, Tobias Mielke, Thorsten Teutloff, Christian Leimkühler, Silke Wendler, Petra Nat Commun Article 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. Nature Publishing Group UK 2020-04-20 /pmc/articles/PMC7171172/ /pubmed/32313256 http://dx.doi.org/10.1038/s41467-020-15614-0 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Radon, Christin
Mittelstädt, Gerd
Duffus, Benjamin R.
Bürger, Jörg
Hartmann, Tobias
Mielke, Thorsten
Teutloff, Christian
Leimkühler, Silke
Wendler, Petra
Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase
title 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_short 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
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7171172/
https://www.ncbi.nlm.nih.gov/pubmed/32313256
http://dx.doi.org/10.1038/s41467-020-15614-0
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