Nitrogenase Fe Protein: A Multi-Tasking Player in Substrate Reduction and Metallocluster Assembly

The Fe protein of nitrogenase plays multiple roles in substrate reduction and metallocluster assembly. Best known for its function to transfer electrons to its catalytic partner during nitrogenase catalysis, the Fe protein is also a key player in the biosynthesis of the complex metalloclusters of ni...

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Autores principales: Ribbe, Markus W., Górecki, Kamil, Grosch, Mario, Solomon, Joseph B., Quechol, Robert, Liu, Yiling A., Lee, Chi Chung, Hu, Yilin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9571451/
https://www.ncbi.nlm.nih.gov/pubmed/36235278
http://dx.doi.org/10.3390/molecules27196743
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author Ribbe, Markus W.
Górecki, Kamil
Grosch, Mario
Solomon, Joseph B.
Quechol, Robert
Liu, Yiling A.
Lee, Chi Chung
Hu, Yilin
author_facet Ribbe, Markus W.
Górecki, Kamil
Grosch, Mario
Solomon, Joseph B.
Quechol, Robert
Liu, Yiling A.
Lee, Chi Chung
Hu, Yilin
author_sort Ribbe, Markus W.
collection PubMed
description The Fe protein of nitrogenase plays multiple roles in substrate reduction and metallocluster assembly. Best known for its function to transfer electrons to its catalytic partner during nitrogenase catalysis, the Fe protein is also a key player in the biosynthesis of the complex metalloclusters of nitrogenase. In addition, it can function as a reductase on its own and affect the ambient reduction of CO(2) or CO to hydrocarbons. This review will provide an overview of the properties and functions of the Fe protein, highlighting the relevance of this unique FeS enzyme to areas related to the catalysis, biosynthesis, and applications of the fascinating nitrogenase system.
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spelling pubmed-95714512022-10-17 Nitrogenase Fe Protein: A Multi-Tasking Player in Substrate Reduction and Metallocluster Assembly Ribbe, Markus W. Górecki, Kamil Grosch, Mario Solomon, Joseph B. Quechol, Robert Liu, Yiling A. Lee, Chi Chung Hu, Yilin Molecules Review The Fe protein of nitrogenase plays multiple roles in substrate reduction and metallocluster assembly. Best known for its function to transfer electrons to its catalytic partner during nitrogenase catalysis, the Fe protein is also a key player in the biosynthesis of the complex metalloclusters of nitrogenase. In addition, it can function as a reductase on its own and affect the ambient reduction of CO(2) or CO to hydrocarbons. This review will provide an overview of the properties and functions of the Fe protein, highlighting the relevance of this unique FeS enzyme to areas related to the catalysis, biosynthesis, and applications of the fascinating nitrogenase system. MDPI 2022-10-10 /pmc/articles/PMC9571451/ /pubmed/36235278 http://dx.doi.org/10.3390/molecules27196743 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Ribbe, Markus W.
Górecki, Kamil
Grosch, Mario
Solomon, Joseph B.
Quechol, Robert
Liu, Yiling A.
Lee, Chi Chung
Hu, Yilin
Nitrogenase Fe Protein: A Multi-Tasking Player in Substrate Reduction and Metallocluster Assembly
title Nitrogenase Fe Protein: A Multi-Tasking Player in Substrate Reduction and Metallocluster Assembly
title_full Nitrogenase Fe Protein: A Multi-Tasking Player in Substrate Reduction and Metallocluster Assembly
title_fullStr Nitrogenase Fe Protein: A Multi-Tasking Player in Substrate Reduction and Metallocluster Assembly
title_full_unstemmed Nitrogenase Fe Protein: A Multi-Tasking Player in Substrate Reduction and Metallocluster Assembly
title_short Nitrogenase Fe Protein: A Multi-Tasking Player in Substrate Reduction and Metallocluster Assembly
title_sort nitrogenase fe protein: a multi-tasking player in substrate reduction and metallocluster assembly
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9571451/
https://www.ncbi.nlm.nih.gov/pubmed/36235278
http://dx.doi.org/10.3390/molecules27196743
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