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A catalytically active [Mn]-hydrogenase incorporating a non-native metal cofactor
Nature carefully selects specific metal ions for incorporation into the enzymes that catalyze the chemical reactions necessary for life. Hydrogenases, enzymes that activate molecular H(2), exclusively utilize Ni and Fe in [NiFe]-, [FeFe]-, and [Fe]-hydrogeanses. However, other transition metals are...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6591119/ https://www.ncbi.nlm.nih.gov/pubmed/31110253 http://dx.doi.org/10.1038/s41557-019-0266-1 |
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author | Pan, Hui-Jie Huang, Gangfeng Wodrich, Matthew D. Tirani, Farzaneh Fadaei Ataka, Kenichi Shima, Seigo Hu, Xile |
author_facet | Pan, Hui-Jie Huang, Gangfeng Wodrich, Matthew D. Tirani, Farzaneh Fadaei Ataka, Kenichi Shima, Seigo Hu, Xile |
author_sort | Pan, Hui-Jie |
collection | PubMed |
description | Nature carefully selects specific metal ions for incorporation into the enzymes that catalyze the chemical reactions necessary for life. Hydrogenases, enzymes that activate molecular H(2), exclusively utilize Ni and Fe in [NiFe]-, [FeFe]-, and [Fe]-hydrogeanses. However, other transition metals are known to activate or catalyze the production of hydrogen in synthetic systems. Here, we report the development of a biomimetic model complex of [Fe]-hydrogenase that incorporates a Mn, as opposed to a Fe, metal center. This Mn complex is able to heterolytically cleave H(2) as well as catalyze hydrogenation reactions. Incorporation of the model into an apoenzyme of [Fe]-hydrogenase results in a [Mn]-hydrogenase with enhanced occupancy-normalized activity over an analogous semi-synthetic [Fe]-hydrogenase. These findings represent the first instance of a non-native metal hydrogenase showing catalytic functionality and demonstrate that hydrogenases based on a manganese active site are viable. |
format | Online Article Text |
id | pubmed-6591119 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
record_format | MEDLINE/PubMed |
spelling | pubmed-65911192019-11-20 A catalytically active [Mn]-hydrogenase incorporating a non-native metal cofactor Pan, Hui-Jie Huang, Gangfeng Wodrich, Matthew D. Tirani, Farzaneh Fadaei Ataka, Kenichi Shima, Seigo Hu, Xile Nat Chem Article Nature carefully selects specific metal ions for incorporation into the enzymes that catalyze the chemical reactions necessary for life. Hydrogenases, enzymes that activate molecular H(2), exclusively utilize Ni and Fe in [NiFe]-, [FeFe]-, and [Fe]-hydrogeanses. However, other transition metals are known to activate or catalyze the production of hydrogen in synthetic systems. Here, we report the development of a biomimetic model complex of [Fe]-hydrogenase that incorporates a Mn, as opposed to a Fe, metal center. This Mn complex is able to heterolytically cleave H(2) as well as catalyze hydrogenation reactions. Incorporation of the model into an apoenzyme of [Fe]-hydrogenase results in a [Mn]-hydrogenase with enhanced occupancy-normalized activity over an analogous semi-synthetic [Fe]-hydrogenase. These findings represent the first instance of a non-native metal hydrogenase showing catalytic functionality and demonstrate that hydrogenases based on a manganese active site are viable. 2019-05-20 2019-07 /pmc/articles/PMC6591119/ /pubmed/31110253 http://dx.doi.org/10.1038/s41557-019-0266-1 Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Pan, Hui-Jie Huang, Gangfeng Wodrich, Matthew D. Tirani, Farzaneh Fadaei Ataka, Kenichi Shima, Seigo Hu, Xile A catalytically active [Mn]-hydrogenase incorporating a non-native metal cofactor |
title | A catalytically active [Mn]-hydrogenase incorporating a non-native metal cofactor |
title_full | A catalytically active [Mn]-hydrogenase incorporating a non-native metal cofactor |
title_fullStr | A catalytically active [Mn]-hydrogenase incorporating a non-native metal cofactor |
title_full_unstemmed | A catalytically active [Mn]-hydrogenase incorporating a non-native metal cofactor |
title_short | A catalytically active [Mn]-hydrogenase incorporating a non-native metal cofactor |
title_sort | catalytically active [mn]-hydrogenase incorporating a non-native metal cofactor |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6591119/ https://www.ncbi.nlm.nih.gov/pubmed/31110253 http://dx.doi.org/10.1038/s41557-019-0266-1 |
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