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Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle
Besides its role in biological nitrogen fixation, vanadium-containing nitrogenase also reduces carbon monoxide (CO) to hydrocarbons, in analogy to the industrial Fischer-Tropsch process. The protein yields 93% of ethylene (C(2)H(4)), implying a C–C coupling step that mandates the simultaneous bindin...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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American Association for the Advancement of Science
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8163085/ https://www.ncbi.nlm.nih.gov/pubmed/34049880 http://dx.doi.org/10.1126/sciadv.abg4474 |
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author | Rohde, Michael Laun, Konstantin Zebger, Ingo Stripp, Sven T. Einsle, Oliver |
author_facet | Rohde, Michael Laun, Konstantin Zebger, Ingo Stripp, Sven T. Einsle, Oliver |
author_sort | Rohde, Michael |
collection | PubMed |
description | Besides its role in biological nitrogen fixation, vanadium-containing nitrogenase also reduces carbon monoxide (CO) to hydrocarbons, in analogy to the industrial Fischer-Tropsch process. The protein yields 93% of ethylene (C(2)H(4)), implying a C–C coupling step that mandates the simultaneous binding of two CO at the active site FeV cofactor. Spectroscopic data indicated multiple CO binding events, but structural analyses of Mo and V nitrogenase only confirmed a single site. Here, we report the structure of a two CO-bound state of V nitrogenase at 1.05 Å resolution, with one μ-bridging and one terminal CO molecule. This additional, specific ligand binding site suggests a mechanistic route for CO reduction and hydrocarbon formation, as well as a second access pathway for protons required during the reaction. Moreover, carbonyls are strong-field ligands that are chemically similar to mechanistically relevant hydrides that may be formed and used in a fully analogous fashion. |
format | Online Article Text |
id | pubmed-8163085 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Association for the Advancement of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-81630852021-06-07 Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle Rohde, Michael Laun, Konstantin Zebger, Ingo Stripp, Sven T. Einsle, Oliver Sci Adv Research Articles Besides its role in biological nitrogen fixation, vanadium-containing nitrogenase also reduces carbon monoxide (CO) to hydrocarbons, in analogy to the industrial Fischer-Tropsch process. The protein yields 93% of ethylene (C(2)H(4)), implying a C–C coupling step that mandates the simultaneous binding of two CO at the active site FeV cofactor. Spectroscopic data indicated multiple CO binding events, but structural analyses of Mo and V nitrogenase only confirmed a single site. Here, we report the structure of a two CO-bound state of V nitrogenase at 1.05 Å resolution, with one μ-bridging and one terminal CO molecule. This additional, specific ligand binding site suggests a mechanistic route for CO reduction and hydrocarbon formation, as well as a second access pathway for protons required during the reaction. Moreover, carbonyls are strong-field ligands that are chemically similar to mechanistically relevant hydrides that may be formed and used in a fully analogous fashion. American Association for the Advancement of Science 2021-05-28 /pmc/articles/PMC8163085/ /pubmed/34049880 http://dx.doi.org/10.1126/sciadv.abg4474 Text en Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC). https://creativecommons.org/licenses/by-nc/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license (https://creativecommons.org/licenses/by-nc/4.0/) , which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited. |
spellingShingle | Research Articles Rohde, Michael Laun, Konstantin Zebger, Ingo Stripp, Sven T. Einsle, Oliver Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle |
title | Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle |
title_full | Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle |
title_fullStr | Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle |
title_full_unstemmed | Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle |
title_short | Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle |
title_sort | two ligand-binding sites in co-reducing v nitrogenase reveal a general mechanistic principle |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8163085/ https://www.ncbi.nlm.nih.gov/pubmed/34049880 http://dx.doi.org/10.1126/sciadv.abg4474 |
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