Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase
| Autor: | Silke Leimkühler, Petra Wendler, Benjamin R. Duffus, Jörg Bürger, Thorsten Mielke, Tobias Hartmann, Christian Teutloff, Christin Radon, Gerd Mittelstädt |
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| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Models
Molecular 0301 basic medicine Stereochemistry Dimer Science General Physics and Astronomy macromolecular substances 010402 general chemistry Formate dehydrogenase 01 natural sciences environment and public health Article Catalysis Rhodobacter capsulatus Tungsten General Biochemistry Genetics and Molecular Biology Cofactor 03 medical and health sciences chemistry.chemical_compound Cryoelectron microscopy Catalytic Domain Formate lcsh:Science Molybdenum Multidisciplinary Rhodobacter biology 500 Naturwissenschaften und Mathematik::530 Physik::539 Moderne Physik Active site General Chemistry Carbon Dioxide NAD biology.organism_classification Formate Dehydrogenases 0104 chemical sciences 030104 developmental biology chemistry Biocatalysis Enzyme mechanisms biology.protein bacteria lcsh:Q NAD+ kinase 500 Naturwissenschaften und Mathematik::570 Biowissenschaften Biologie::572 Biochemie Oxidation-Reduction |
| Zdroj: | Nature Communications Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020) |
| Popis: | 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. 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. |
| Databáze: | OpenAIRE |
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