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Characterization of a putative sensory [FeFe]-hydrogenase provides new insight into the role of the active site architecture
[FeFe]-hydrogenases are known for their high rates of hydrogen turnover, and are intensively studied in the context of biotechnological applications. Evolution has generated a plethora of different subclasses with widely different characteristics. The M2e subclass is phylogenetically distinct from p...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society of Chemistry
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8163306/ https://www.ncbi.nlm.nih.gov/pubmed/34094474 http://dx.doi.org/10.1039/d0sc03319g |
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author | Land, Henrik Sekretareva, Alina Huang, Ping Redman, Holly J. Németh, Brigitta Polidori, Nakia Mészáros, Lívia S. Senger, Moritz Stripp, Sven T. Berggren, Gustav |
author_facet | Land, Henrik Sekretareva, Alina Huang, Ping Redman, Holly J. Németh, Brigitta Polidori, Nakia Mészáros, Lívia S. Senger, Moritz Stripp, Sven T. Berggren, Gustav |
author_sort | Land, Henrik |
collection | PubMed |
description | [FeFe]-hydrogenases are known for their high rates of hydrogen turnover, and are intensively studied in the context of biotechnological applications. Evolution has generated a plethora of different subclasses with widely different characteristics. The M2e subclass is phylogenetically distinct from previously characterized members of this enzyme family and its biological role is unknown. It features significant differences in domain- and active site architecture, and is most closely related to the putative sensory [FeFe]-hydrogenases. Here we report the first comprehensive biochemical and spectroscopical characterization of an M2e enzyme, derived from Thermoanaerobacter mathranii. As compared to other [FeFe]-hydrogenases characterized to-date, this enzyme displays an increased H(2) affinity, higher activation enthalpies for H(+)/H(2) interconversion, and unusual reactivity towards known hydrogenase inhibitors. These properties are related to differences in active site architecture between the M2e [FeFe]-hydrogenase and “prototypical” [FeFe]-hydrogenases. Thus, this study provides new insight into the role of this subclass in hydrogen metabolism and the influence of the active site pocket on the chemistry of the H-cluster. |
format | Online Article Text |
id | pubmed-8163306 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | The Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-81633062021-06-04 Characterization of a putative sensory [FeFe]-hydrogenase provides new insight into the role of the active site architecture Land, Henrik Sekretareva, Alina Huang, Ping Redman, Holly J. Németh, Brigitta Polidori, Nakia Mészáros, Lívia S. Senger, Moritz Stripp, Sven T. Berggren, Gustav Chem Sci Chemistry [FeFe]-hydrogenases are known for their high rates of hydrogen turnover, and are intensively studied in the context of biotechnological applications. Evolution has generated a plethora of different subclasses with widely different characteristics. The M2e subclass is phylogenetically distinct from previously characterized members of this enzyme family and its biological role is unknown. It features significant differences in domain- and active site architecture, and is most closely related to the putative sensory [FeFe]-hydrogenases. Here we report the first comprehensive biochemical and spectroscopical characterization of an M2e enzyme, derived from Thermoanaerobacter mathranii. As compared to other [FeFe]-hydrogenases characterized to-date, this enzyme displays an increased H(2) affinity, higher activation enthalpies for H(+)/H(2) interconversion, and unusual reactivity towards known hydrogenase inhibitors. These properties are related to differences in active site architecture between the M2e [FeFe]-hydrogenase and “prototypical” [FeFe]-hydrogenases. Thus, this study provides new insight into the role of this subclass in hydrogen metabolism and the influence of the active site pocket on the chemistry of the H-cluster. The Royal Society of Chemistry 2020-09-21 /pmc/articles/PMC8163306/ /pubmed/34094474 http://dx.doi.org/10.1039/d0sc03319g Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/ |
spellingShingle | Chemistry Land, Henrik Sekretareva, Alina Huang, Ping Redman, Holly J. Németh, Brigitta Polidori, Nakia Mészáros, Lívia S. Senger, Moritz Stripp, Sven T. Berggren, Gustav Characterization of a putative sensory [FeFe]-hydrogenase provides new insight into the role of the active site architecture |
title | Characterization of a putative sensory [FeFe]-hydrogenase provides new insight into the role of the active site architecture |
title_full | Characterization of a putative sensory [FeFe]-hydrogenase provides new insight into the role of the active site architecture |
title_fullStr | Characterization of a putative sensory [FeFe]-hydrogenase provides new insight into the role of the active site architecture |
title_full_unstemmed | Characterization of a putative sensory [FeFe]-hydrogenase provides new insight into the role of the active site architecture |
title_short | Characterization of a putative sensory [FeFe]-hydrogenase provides new insight into the role of the active site architecture |
title_sort | characterization of a putative sensory [fefe]-hydrogenase provides new insight into the role of the active site architecture |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8163306/ https://www.ncbi.nlm.nih.gov/pubmed/34094474 http://dx.doi.org/10.1039/d0sc03319g |
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