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Structure of the membrane-bound formate hydrogenlyase complex from Escherichia coli
The prototypical hydrogen-producing enzyme, the membrane-bound formate hydrogenlyase (FHL) complex from Escherichia coli, links formate oxidation at a molybdopterin-containing formate dehydrogenase to proton reduction at a [NiFe] hydrogenase. It is of intense interest due to its ability to efficient...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9474812/ https://www.ncbi.nlm.nih.gov/pubmed/36104349 http://dx.doi.org/10.1038/s41467-022-32831-x |
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author | Steinhilper, Ralf Höff, Gabriele Heider, Johann Murphy, Bonnie J. |
author_facet | Steinhilper, Ralf Höff, Gabriele Heider, Johann Murphy, Bonnie J. |
author_sort | Steinhilper, Ralf |
collection | PubMed |
description | The prototypical hydrogen-producing enzyme, the membrane-bound formate hydrogenlyase (FHL) complex from Escherichia coli, links formate oxidation at a molybdopterin-containing formate dehydrogenase to proton reduction at a [NiFe] hydrogenase. It is of intense interest due to its ability to efficiently produce H(2) during fermentation, its reversibility, allowing H(2)-dependent CO(2) reduction, and its evolutionary link to respiratory complex I. FHL has been studied for over a century, but its atomic structure remains unknown. Here we report cryo-EM structures of FHL in its aerobically and anaerobically isolated forms at resolutions reaching 2.6 Å. This includes well-resolved density for conserved loops linking the soluble and membrane arms believed to be essential in coupling enzymatic turnover to ion translocation across the membrane in the complex I superfamily. We evaluate possible structural determinants of the bias toward hydrogen production over its oxidation and describe an unpredicted metal-binding site near the interface of FdhF and HycF subunits that may play a role in redox-dependent regulation of FdhF interaction with the complex. |
format | Online Article Text |
id | pubmed-9474812 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-94748122022-09-16 Structure of the membrane-bound formate hydrogenlyase complex from Escherichia coli Steinhilper, Ralf Höff, Gabriele Heider, Johann Murphy, Bonnie J. Nat Commun Article The prototypical hydrogen-producing enzyme, the membrane-bound formate hydrogenlyase (FHL) complex from Escherichia coli, links formate oxidation at a molybdopterin-containing formate dehydrogenase to proton reduction at a [NiFe] hydrogenase. It is of intense interest due to its ability to efficiently produce H(2) during fermentation, its reversibility, allowing H(2)-dependent CO(2) reduction, and its evolutionary link to respiratory complex I. FHL has been studied for over a century, but its atomic structure remains unknown. Here we report cryo-EM structures of FHL in its aerobically and anaerobically isolated forms at resolutions reaching 2.6 Å. This includes well-resolved density for conserved loops linking the soluble and membrane arms believed to be essential in coupling enzymatic turnover to ion translocation across the membrane in the complex I superfamily. We evaluate possible structural determinants of the bias toward hydrogen production over its oxidation and describe an unpredicted metal-binding site near the interface of FdhF and HycF subunits that may play a role in redox-dependent regulation of FdhF interaction with the complex. Nature Publishing Group UK 2022-09-14 /pmc/articles/PMC9474812/ /pubmed/36104349 http://dx.doi.org/10.1038/s41467-022-32831-x Text en © The Author(s) 2022, corrected publication 2022 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Steinhilper, Ralf Höff, Gabriele Heider, Johann Murphy, Bonnie J. Structure of the membrane-bound formate hydrogenlyase complex from Escherichia coli |
title | Structure of the membrane-bound formate hydrogenlyase complex from Escherichia coli |
title_full | Structure of the membrane-bound formate hydrogenlyase complex from Escherichia coli |
title_fullStr | Structure of the membrane-bound formate hydrogenlyase complex from Escherichia coli |
title_full_unstemmed | Structure of the membrane-bound formate hydrogenlyase complex from Escherichia coli |
title_short | Structure of the membrane-bound formate hydrogenlyase complex from Escherichia coli |
title_sort | structure of the membrane-bound formate hydrogenlyase complex from escherichia coli |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9474812/ https://www.ncbi.nlm.nih.gov/pubmed/36104349 http://dx.doi.org/10.1038/s41467-022-32831-x |
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