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Structure and electron transfer pathways of an electron-bifurcating NiFe-hydrogenase
Electron bifurcation enables thermodynamically unfavorable biochemical reactions. Four groups of bifurcating flavoenzyme are known and three use FAD to bifurcate. FeFe-HydABC hydrogenase represents the fourth group, but its bifurcation site is unknown. We report cryo-EM structures of the related NiF...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Association for the Advancement of Science
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8880783/ https://www.ncbi.nlm.nih.gov/pubmed/35213221 http://dx.doi.org/10.1126/sciadv.abm7546 |
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author | Feng, Xiang Schut, Gerrit J. Haja, Dominik K. Adams, Michael W. W. Li, Huilin |
author_facet | Feng, Xiang Schut, Gerrit J. Haja, Dominik K. Adams, Michael W. W. Li, Huilin |
author_sort | Feng, Xiang |
collection | PubMed |
description | Electron bifurcation enables thermodynamically unfavorable biochemical reactions. Four groups of bifurcating flavoenzyme are known and three use FAD to bifurcate. FeFe-HydABC hydrogenase represents the fourth group, but its bifurcation site is unknown. We report cryo-EM structures of the related NiFe-HydABCSL hydrogenase that reversibly oxidizes H(2) and couples endergonic reduction of ferredoxin with exergonic reduction of NAD. FMN surrounded by a unique arrangement of iron sulfur clusters forms the bifurcating center. NAD binds to FMN in HydB, and electrons from H(2) via HydA to a HydB [4Fe-4S] cluster enable the FMN to reduce NAD. Low-potential electron transfer from FMN to the HydC [2Fe-2S] cluster and subsequent reduction of a uniquely penta-coordinated HydB [2Fe-2S] cluster require conformational changes, leading to ferredoxin binding and reduction by a [4Fe-4S] cluster in HydB. This work clarifies the electron transfer pathways for a large group of hydrogenases underlying many essential functions in anaerobic microorganisms. |
format | Online Article Text |
id | pubmed-8880783 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Association for the Advancement of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-88807832022-03-10 Structure and electron transfer pathways of an electron-bifurcating NiFe-hydrogenase Feng, Xiang Schut, Gerrit J. Haja, Dominik K. Adams, Michael W. W. Li, Huilin Sci Adv Physical and Materials Sciences Electron bifurcation enables thermodynamically unfavorable biochemical reactions. Four groups of bifurcating flavoenzyme are known and three use FAD to bifurcate. FeFe-HydABC hydrogenase represents the fourth group, but its bifurcation site is unknown. We report cryo-EM structures of the related NiFe-HydABCSL hydrogenase that reversibly oxidizes H(2) and couples endergonic reduction of ferredoxin with exergonic reduction of NAD. FMN surrounded by a unique arrangement of iron sulfur clusters forms the bifurcating center. NAD binds to FMN in HydB, and electrons from H(2) via HydA to a HydB [4Fe-4S] cluster enable the FMN to reduce NAD. Low-potential electron transfer from FMN to the HydC [2Fe-2S] cluster and subsequent reduction of a uniquely penta-coordinated HydB [2Fe-2S] cluster require conformational changes, leading to ferredoxin binding and reduction by a [4Fe-4S] cluster in HydB. This work clarifies the electron transfer pathways for a large group of hydrogenases underlying many essential functions in anaerobic microorganisms. American Association for the Advancement of Science 2022-02-25 /pmc/articles/PMC8880783/ /pubmed/35213221 http://dx.doi.org/10.1126/sciadv.abm7546 Text en Copyright © 2022 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution License 4.0 (CC BY). https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution license (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Physical and Materials Sciences Feng, Xiang Schut, Gerrit J. Haja, Dominik K. Adams, Michael W. W. Li, Huilin Structure and electron transfer pathways of an electron-bifurcating NiFe-hydrogenase |
title | Structure and electron transfer pathways of an electron-bifurcating NiFe-hydrogenase |
title_full | Structure and electron transfer pathways of an electron-bifurcating NiFe-hydrogenase |
title_fullStr | Structure and electron transfer pathways of an electron-bifurcating NiFe-hydrogenase |
title_full_unstemmed | Structure and electron transfer pathways of an electron-bifurcating NiFe-hydrogenase |
title_short | Structure and electron transfer pathways of an electron-bifurcating NiFe-hydrogenase |
title_sort | structure and electron transfer pathways of an electron-bifurcating nife-hydrogenase |
topic | Physical and Materials Sciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8880783/ https://www.ncbi.nlm.nih.gov/pubmed/35213221 http://dx.doi.org/10.1126/sciadv.abm7546 |
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