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High-resolution cryo-EM structures of plant cytochrome b(6)f at work
Plants use solar energy to power cellular metabolism. The oxidation of plastoquinol and reduction of plastocyanin by cytochrome b(6)f (Cyt b(6)f) is known as one of the key steps of photosynthesis, but the catalytic mechanism in the plastoquinone oxidation site (Q(p)) remains elusive. Here, we descr...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Association for the Advancement of Science
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9839326/ https://www.ncbi.nlm.nih.gov/pubmed/36638176 http://dx.doi.org/10.1126/sciadv.add9688 |
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author | Sarewicz, Marcin Szwalec, Mateusz Pintscher, Sebastian Indyka, Paulina Rawski, Michał Pietras, Rafał Mielecki, Bohun Koziej, Łukasz Jaciuk, Marcin Glatt, Sebastian Osyczka, Artur |
author_facet | Sarewicz, Marcin Szwalec, Mateusz Pintscher, Sebastian Indyka, Paulina Rawski, Michał Pietras, Rafał Mielecki, Bohun Koziej, Łukasz Jaciuk, Marcin Glatt, Sebastian Osyczka, Artur |
author_sort | Sarewicz, Marcin |
collection | PubMed |
description | Plants use solar energy to power cellular metabolism. The oxidation of plastoquinol and reduction of plastocyanin by cytochrome b(6)f (Cyt b(6)f) is known as one of the key steps of photosynthesis, but the catalytic mechanism in the plastoquinone oxidation site (Q(p)) remains elusive. Here, we describe two high-resolution cryo-EM structures of the spinach Cyt b(6)f homodimer with endogenous plastoquinones and in complex with plastocyanin. Three plastoquinones are visible and line up one after another head to tail near Q(p) in both monomers, indicating the existence of a channel in each monomer. Therefore, quinones appear to flow through Cyt b(6)f in one direction, transiently exposing the redox-active ring of quinone during catalysis. Our work proposes an unprecedented one-way traffic model that explains efficient quinol oxidation during photosynthesis and respiration. |
format | Online Article Text |
id | pubmed-9839326 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | American Association for the Advancement of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-98393262023-01-24 High-resolution cryo-EM structures of plant cytochrome b(6)f at work Sarewicz, Marcin Szwalec, Mateusz Pintscher, Sebastian Indyka, Paulina Rawski, Michał Pietras, Rafał Mielecki, Bohun Koziej, Łukasz Jaciuk, Marcin Glatt, Sebastian Osyczka, Artur Sci Adv Biomedicine and Life Sciences Plants use solar energy to power cellular metabolism. The oxidation of plastoquinol and reduction of plastocyanin by cytochrome b(6)f (Cyt b(6)f) is known as one of the key steps of photosynthesis, but the catalytic mechanism in the plastoquinone oxidation site (Q(p)) remains elusive. Here, we describe two high-resolution cryo-EM structures of the spinach Cyt b(6)f homodimer with endogenous plastoquinones and in complex with plastocyanin. Three plastoquinones are visible and line up one after another head to tail near Q(p) in both monomers, indicating the existence of a channel in each monomer. Therefore, quinones appear to flow through Cyt b(6)f in one direction, transiently exposing the redox-active ring of quinone during catalysis. Our work proposes an unprecedented one-way traffic model that explains efficient quinol oxidation during photosynthesis and respiration. American Association for the Advancement of Science 2023-01-13 /pmc/articles/PMC9839326/ /pubmed/36638176 http://dx.doi.org/10.1126/sciadv.add9688 Text en Copyright © 2023 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 NonCommercial License 4.0 (CC BY-NC). https://creativecommons.org/licenses/by-nc/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license (https://creativecommons.org/licenses/by-nc/4.0/) , which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited. |
spellingShingle | Biomedicine and Life Sciences Sarewicz, Marcin Szwalec, Mateusz Pintscher, Sebastian Indyka, Paulina Rawski, Michał Pietras, Rafał Mielecki, Bohun Koziej, Łukasz Jaciuk, Marcin Glatt, Sebastian Osyczka, Artur High-resolution cryo-EM structures of plant cytochrome b(6)f at work |
title | High-resolution cryo-EM structures of plant cytochrome b(6)f at work |
title_full | High-resolution cryo-EM structures of plant cytochrome b(6)f at work |
title_fullStr | High-resolution cryo-EM structures of plant cytochrome b(6)f at work |
title_full_unstemmed | High-resolution cryo-EM structures of plant cytochrome b(6)f at work |
title_short | High-resolution cryo-EM structures of plant cytochrome b(6)f at work |
title_sort | high-resolution cryo-em structures of plant cytochrome b(6)f at work |
topic | Biomedicine and Life Sciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9839326/ https://www.ncbi.nlm.nih.gov/pubmed/36638176 http://dx.doi.org/10.1126/sciadv.add9688 |
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