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  Structural insights into the iron nitrogenase complex

Schmidt, F. V., Schulz, L., Zarzycki, J., Prinz, S., Oehlmann, N. N., Erb, T. J., et al. (2024). Structural insights into the iron nitrogenase complex. Nature Structural & Molecular Biology, 31(1), 150-158. doi:10.1038/s41594-023-01124-2.

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Item Permalink: https://hdl.handle.net/21.11116/0000-000E-04EE-2 Version Permalink: https://hdl.handle.net/21.11116/0000-000F-2059-9
Genre: Journal Article

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Locator:
https://doi.org/10.1038/s41594-023-01124-2 (Publisher version)
Description:
Verlagsversion
OA-Status:
Gold
Locator:
https://doi.org/10.1101/2023.05.02.539077 (Preprint)
Description:
Preprint
OA-Status:
Green

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 Creators:
Schmidt, Frederik Vincent1, Author           
Schulz, Luca2, Author           
Zarzycki, Jan2, Author           
Prinz, Simone3, Author
Oehlmann, Niels Nathan1, Author           
Erb, Tobias J.2, Author                 
Rebelein, Johannes G.1, Author                 
Affiliations:
1Emmy Noether research Group Microbial Metalloenzymes, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266294              
2Understanding and Building Metabolism, Department of Biochemistry and Synthetic Metabolism, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266303              
3external, ou_persistent22              

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 Abstract: Nitrogenases are best known for catalyzing the reduction of dinitrogen to ammonia at a complex metallic cofactor. Recently, nitrogenases were shown to reduce carbon dioxide (CO2) and carbon monoxide to hydrocarbons, offering a pathway to recycle carbon waste into hydrocarbon products. Among the three nitrogenase isozymes, the iron nitrogenase has the highest wild-type activity for the reduction of CO2, but the molecular architecture facilitating these activities has remained unknown. Here, we report a 2.35-Å cryogenic electron microscopy structure of the ADP·AlF3-stabilized iron nitrogenase complex from Rhodobacter capsulatus, revealing an [Fe8S9C-(R)-homocitrate] cluster in the active site. The enzyme complex suggests that the iron nitrogenase G subunit is involved in cluster stabilization and substrate channeling and confers specificity between nitrogenase reductase and catalytic component proteins. Moreover, the structure highlights a different interface between the two catalytic halves of the iron and the molybdenum nitrogenase, potentially influencing the intrasubunit ‘communication’ and thus the nitrogenase mechanism.

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Language(s): eng - English
 Dates: 2023-09-122023-12-072024
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: URI: https://doi.org/10.1038/s41594-023-01124-2
Other: Schmidt2023
DOI: 10.1038/s41594-023-01124-2
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Project name : -
Grant ID : 446841743
Funding program : -
Funding organization : Deutsche Forschungsgemeinschaft (DFG)
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Grant ID : -
Funding program : -
Funding organization : Max Planck Society
Project name : -
Grant ID : -
Funding program : Add-On Fellowship for Interdisciplinary Life Sciences
Funding organization : Joachim Herz Foundation
Project name : -
Grant ID : -
Funding program : Kekulé fellowship
Funding organization : Verband der Chemischen Industrie
Project name : Projekt DEAL
Grant ID : -
Funding program : -
Funding organization : Allianz der deutschen Wissenschaftsorganisationen

Source 1

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Title: Nature Structural & Molecular Biology
  Other : Nature Structural and Molecular Biology
  Abbreviation : Nat Struct Mol Biol
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: New York, NY : Nature Pub. Group
Pages: - Volume / Issue: 31 (1) Sequence Number: - Start / End Page: 150 - 158 Identifier: ISSN: 1545-9993
CoNE: https://pure.mpg.de/cone/journals/resource/954925603763