Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase
| Autor: | Christophe Léger, Mériem Merrouch, Chie Ueda, Catherine L. Drennan, Vincent Fourmond, Sébastien Dementin, Laura Fradale, Elizabeth C. Wittenborn, Maria-Eirini Pandelia |
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| Přispěvatelé: | Berkeley California Institute for Quantitative Biosciences [Berkeley], University of California (UC), Bioénergétique et Ingénierie des Protéines (BIP ), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Brandeis University, Massachusetts Institute of Technology (MIT), ANR-17-CE11-0027,MeCO2Bio,Études mécanistiques de la réduction du CO2: exploration de la biodiversité des CO déshydrogénases(2017), ANR-15-CE05-0020,shields,Des films de polymères pour supporter et protéger des catalyseurs d'oxydation de l'hydrogène et de réduction du CO2(2015), University of California, Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU) |
| Rok vydání: | 2018 |
| Předmět: |
Iron-Sulfur Proteins
Models Molecular 0301 basic medicine Protein Conformation Structural Biology and Molecular Biophysics carbon fixation Crystallography X-Ray 01 natural sciences Nickel Biology (General) Desulfovibrio vulgaris chemistry.chemical_classification Carbon Monoxide biology Chemistry General Neuroscience Carbon fixation metallocluster General Medicine Aldehyde Oxidoreductases Medicine Oxidation-Reduction Carbon monoxide dehydrogenase QH301-705.5 Stereochemistry Science Iron carbon monoxide dehydrogenase Short Report desulfovibrio fructosovorans Redox General Biochemistry Genetics and Molecular Biology 03 medical and health sciences Bacterial Proteins Multienzyme Complexes Biochemistry and Chemical Biology Oxidoreductase [CHIM]Chemical Sciences X-ray crystallography Binding Sites General Immunology and Microbiology 010405 organic chemistry Mutagenesis biology.organism_classification CO-dehydrogenase 0104 chemical sciences desulfovibrio vulgaris 030104 developmental biology Structural biology 13. Climate action Mutation biology.protein Other Sulfur Cysteine |
| Zdroj: | eLife eLife, 2018, 7, ⟨10.7554/eLife.39451⟩ eLife, Vol 7 (2018) eLife, eLife Sciences Publication, 2018, 7, ⟨10.7554/eLife.39451⟩ |
| ISSN: | 2050-084X |
| DOI: | 10.7554/elife.39451 |
| Popis: | The C-cluster of the enzyme carbon monoxide dehydrogenase (CODH) is a structurally distinctive Ni-Fe-S cluster employed to catalyze the reduction of CO2 to CO as part of the Wood-Ljungdahl carbon fixation pathway. Using X-ray crystallography, we have observed unprecedented conformational dynamics in the C-cluster of the CODH from Desulfovibrio vulgaris, providing the first view of an oxidized state of the cluster. Combined with supporting spectroscopic data, our structures reveal that this novel, oxidized cluster arrangement plays a role in avoiding irreversible oxidative degradation at the C-cluster. Furthermore, mutagenesis of a conserved cysteine residue that binds the C-cluster in the oxidized state but not in the reduced state suggests that the oxidized conformation could be important for proper cluster assembly, in particular Ni incorporation. Together, these results lay a foundation for future investigations of C-cluster activation and assembly, and contribute to an emerging paradigm of metallocluster plasticity. eLife digest Life relies on countless chemical reactions, almost all of which need to be sped up by enzymes. About half of all enzymes carry metal ions that expand the range of the reactions that they can catalyze. In some enzymes these metal ions assemble with sulfur ions to form so-called metalloclusters. These structures can carry out many different types of reactions, including converting simple forms of elements like nitrogen and carbon into other forms that can be used to make more complicated biological molecules. One enzyme that contains metalloclusters is carbon monoxide dehydrogenase. Known as CODH for short, this enzyme uses a metallocluster called the “C-cluster” to interconvert two gases: the pollutant carbon monoxide and the greenhouse gas carbon dioxide. CODH enzymes are found inside certain bacteria, but they are also of interest for humans, who wish to use them to remove the harmful gases from the environment. But this is not as simple as it may at first seem: CODH enzymes usually become inactive when exposed to air because the metalloclusters fall apart in the presence of oxygen. One CODH enzyme from a widespread bacterium called Desulfovibrio vulgaris, however, is an attractive target for industrial use because it can tolerate oxygen better. Yet, it is still unclear why this enzyme does not get inactivated the way other CODHs do. Wittenborn et al. have now characterized the CODH enzyme from D. vulgaris in more depth via a technique called X-ray crystallography, which can reveal the location of individual atoms within a molecule. By a happy accident, the structures revealed that the C-cluster can adopt a dramatically different arrangement of metal and sulfur ions after being exposed to oxygen. This rearrangement is fully reversible; when oxygen is removed, the metal and sulfur ions move back to their normal positions. This ability to flip between different arrangements appears to protect the metallocluster from losing its metal ions when exposed to oxygen. By providing structural snapshots of how CODH responds to oxygen these results provide a more complete understanding of an enzyme that plays a key role in the global carbon cycle. This understanding could help scientists to develop bioremediation tools to remove carbon monoxide and carbon dioxide from the atmosphere and to engineer bacteria to capture carbon to make biofuels. |
| Databáze: | OpenAIRE |
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