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Metabolic Capacity of the Antarctic Cyanobacterium Phormidium pseudopriestleyi That Sustains Oxygenic Photosynthesis in the Presence of Hydrogen Sulfide
Sulfide inhibits oxygenic photosynthesis by blocking electron transfer between H(2)O and the oxygen-evolving complex in the D1 protein of Photosystem II. The ability of cyanobacteria to counter this effect has implications for understanding the productivity of benthic microbial mats in sulfidic envi...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8002359/ https://www.ncbi.nlm.nih.gov/pubmed/33809699 http://dx.doi.org/10.3390/genes12030426 |
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author | Lumian, Jessica E. Jungblut, Anne D. Dillion, Megan L. Hawes, Ian Doran, Peter T. Mackey, Tyler J. Dick, Gregory J. Grettenberger, Christen L. Sumner, Dawn Y. |
author_facet | Lumian, Jessica E. Jungblut, Anne D. Dillion, Megan L. Hawes, Ian Doran, Peter T. Mackey, Tyler J. Dick, Gregory J. Grettenberger, Christen L. Sumner, Dawn Y. |
author_sort | Lumian, Jessica E. |
collection | PubMed |
description | Sulfide inhibits oxygenic photosynthesis by blocking electron transfer between H(2)O and the oxygen-evolving complex in the D1 protein of Photosystem II. The ability of cyanobacteria to counter this effect has implications for understanding the productivity of benthic microbial mats in sulfidic environments throughout Earth history. In Lake Fryxell, Antarctica, the benthic, filamentous cyanobacterium Phormidium pseudopriestleyi creates a 1–2 mm thick layer of 50 µmol L(−1) O(2) in otherwise sulfidic water, demonstrating that it sustains oxygenic photosynthesis in the presence of sulfide. A metagenome-assembled genome of P. pseudopriestleyi indicates a genetic capacity for oxygenic photosynthesis, including multiple copies of psbA (encoding the D1 protein of Photosystem II), and anoxygenic photosynthesis with a copy of sqr (encoding the sulfide quinone reductase protein that oxidizes sulfide). The genomic content of P. pseudopriestleyi is consistent with sulfide tolerance mechanisms including increasing psbA expression or directly oxidizing sulfide with sulfide quinone reductase. However, the ability of the organism to reduce Photosystem I via sulfide quinone reductase while Photosystem II is sulfide-inhibited, thereby performing anoxygenic photosynthesis in the presence of sulfide, has yet to be demonstrated. |
format | Online Article Text |
id | pubmed-8002359 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-80023592021-03-28 Metabolic Capacity of the Antarctic Cyanobacterium Phormidium pseudopriestleyi That Sustains Oxygenic Photosynthesis in the Presence of Hydrogen Sulfide Lumian, Jessica E. Jungblut, Anne D. Dillion, Megan L. Hawes, Ian Doran, Peter T. Mackey, Tyler J. Dick, Gregory J. Grettenberger, Christen L. Sumner, Dawn Y. Genes (Basel) Article Sulfide inhibits oxygenic photosynthesis by blocking electron transfer between H(2)O and the oxygen-evolving complex in the D1 protein of Photosystem II. The ability of cyanobacteria to counter this effect has implications for understanding the productivity of benthic microbial mats in sulfidic environments throughout Earth history. In Lake Fryxell, Antarctica, the benthic, filamentous cyanobacterium Phormidium pseudopriestleyi creates a 1–2 mm thick layer of 50 µmol L(−1) O(2) in otherwise sulfidic water, demonstrating that it sustains oxygenic photosynthesis in the presence of sulfide. A metagenome-assembled genome of P. pseudopriestleyi indicates a genetic capacity for oxygenic photosynthesis, including multiple copies of psbA (encoding the D1 protein of Photosystem II), and anoxygenic photosynthesis with a copy of sqr (encoding the sulfide quinone reductase protein that oxidizes sulfide). The genomic content of P. pseudopriestleyi is consistent with sulfide tolerance mechanisms including increasing psbA expression or directly oxidizing sulfide with sulfide quinone reductase. However, the ability of the organism to reduce Photosystem I via sulfide quinone reductase while Photosystem II is sulfide-inhibited, thereby performing anoxygenic photosynthesis in the presence of sulfide, has yet to be demonstrated. MDPI 2021-03-16 /pmc/articles/PMC8002359/ /pubmed/33809699 http://dx.doi.org/10.3390/genes12030426 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ). |
spellingShingle | Article Lumian, Jessica E. Jungblut, Anne D. Dillion, Megan L. Hawes, Ian Doran, Peter T. Mackey, Tyler J. Dick, Gregory J. Grettenberger, Christen L. Sumner, Dawn Y. Metabolic Capacity of the Antarctic Cyanobacterium Phormidium pseudopriestleyi That Sustains Oxygenic Photosynthesis in the Presence of Hydrogen Sulfide |
title | Metabolic Capacity of the Antarctic Cyanobacterium Phormidium pseudopriestleyi That Sustains Oxygenic Photosynthesis in the Presence of Hydrogen Sulfide |
title_full | Metabolic Capacity of the Antarctic Cyanobacterium Phormidium pseudopriestleyi That Sustains Oxygenic Photosynthesis in the Presence of Hydrogen Sulfide |
title_fullStr | Metabolic Capacity of the Antarctic Cyanobacterium Phormidium pseudopriestleyi That Sustains Oxygenic Photosynthesis in the Presence of Hydrogen Sulfide |
title_full_unstemmed | Metabolic Capacity of the Antarctic Cyanobacterium Phormidium pseudopriestleyi That Sustains Oxygenic Photosynthesis in the Presence of Hydrogen Sulfide |
title_short | Metabolic Capacity of the Antarctic Cyanobacterium Phormidium pseudopriestleyi That Sustains Oxygenic Photosynthesis in the Presence of Hydrogen Sulfide |
title_sort | metabolic capacity of the antarctic cyanobacterium phormidium pseudopriestleyi that sustains oxygenic photosynthesis in the presence of hydrogen sulfide |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8002359/ https://www.ncbi.nlm.nih.gov/pubmed/33809699 http://dx.doi.org/10.3390/genes12030426 |
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