Identity and function of an essential nitrogen ligand of the nitrogenase cofactor biosynthesis protein NifB
NifB is a radical SAM enzyme involved in the biosynthesis of the Mo-nitrogenase cofactor, which is responsible for the ambient conversion of N2 to NH3. Here, the authors identify and uncover the function of a His43 residue as an essential nitrogen ligand of NifB in cofactor biosynthesis.
Main Authors: | , , , , , , , |
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Format: | Article |
Language: | English |
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Nature Portfolio
2020-04-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-020-15627-9 |
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author | Lee A. Rettberg Jarett Wilcoxen Andrew J. Jasniewski Chi Chung Lee Kazuki Tanifuji Yilin Hu R. David Britt Markus W. Ribbe |
author_facet | Lee A. Rettberg Jarett Wilcoxen Andrew J. Jasniewski Chi Chung Lee Kazuki Tanifuji Yilin Hu R. David Britt Markus W. Ribbe |
author_sort | Lee A. Rettberg |
collection | DOAJ |
description | NifB is a radical SAM enzyme involved in the biosynthesis of the Mo-nitrogenase cofactor, which is responsible for the ambient conversion of N2 to NH3. Here, the authors identify and uncover the function of a His43 residue as an essential nitrogen ligand of NifB in cofactor biosynthesis. |
first_indexed | 2024-12-18T04:22:47Z |
format | Article |
id | doaj.art-90274eff35004d1e96f2484f0db98a92 |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-12-18T04:22:47Z |
publishDate | 2020-04-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
spelling | doaj.art-90274eff35004d1e96f2484f0db98a922022-12-21T21:21:12ZengNature PortfolioNature Communications2041-17232020-04-011111810.1038/s41467-020-15627-9Identity and function of an essential nitrogen ligand of the nitrogenase cofactor biosynthesis protein NifBLee A. Rettberg0Jarett Wilcoxen1Andrew J. Jasniewski2Chi Chung Lee3Kazuki Tanifuji4Yilin Hu5R. David Britt6Markus W. Ribbe7Department of Molecular Biology and Biochemistry, University of CaliforniaDepartment of Chemistry, University of CaliforniaDepartment of Molecular Biology and Biochemistry, University of CaliforniaDepartment of Molecular Biology and Biochemistry, University of CaliforniaDepartment of Molecular Biology and Biochemistry, University of CaliforniaDepartment of Molecular Biology and Biochemistry, University of CaliforniaDepartment of Chemistry, University of CaliforniaDepartment of Molecular Biology and Biochemistry, University of CaliforniaNifB is a radical SAM enzyme involved in the biosynthesis of the Mo-nitrogenase cofactor, which is responsible for the ambient conversion of N2 to NH3. Here, the authors identify and uncover the function of a His43 residue as an essential nitrogen ligand of NifB in cofactor biosynthesis.https://doi.org/10.1038/s41467-020-15627-9 |
spellingShingle | Lee A. Rettberg Jarett Wilcoxen Andrew J. Jasniewski Chi Chung Lee Kazuki Tanifuji Yilin Hu R. David Britt Markus W. Ribbe Identity and function of an essential nitrogen ligand of the nitrogenase cofactor biosynthesis protein NifB Nature Communications |
title | Identity and function of an essential nitrogen ligand of the nitrogenase cofactor biosynthesis protein NifB |
title_full | Identity and function of an essential nitrogen ligand of the nitrogenase cofactor biosynthesis protein NifB |
title_fullStr | Identity and function of an essential nitrogen ligand of the nitrogenase cofactor biosynthesis protein NifB |
title_full_unstemmed | Identity and function of an essential nitrogen ligand of the nitrogenase cofactor biosynthesis protein NifB |
title_short | Identity and function of an essential nitrogen ligand of the nitrogenase cofactor biosynthesis protein NifB |
title_sort | identity and function of an essential nitrogen ligand of the nitrogenase cofactor biosynthesis protein nifb |
url | https://doi.org/10.1038/s41467-020-15627-9 |
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