Datum
2022-05-31Autor
Burgstaller, HeinrichWang, YingyingCaliebe, JohannaHüren, VanessaAppel, JensBoehm, MarkoLeitzke, SinjeTheune, MariusKing, Paul W.Gutekunst, KirstinSchlagwort
570 Biowissenschaften, Biologie 580 Pflanzen (Botanik) SynechocystisCyanobakterienHydrogenasenDihydrolipoamid-DehydrogenasePhotosyntheseAtmungArgininMetadata
Zur Langanzeige
Aufsatz
Synechocystis sp. PCC 6803 Requires the Bidirectional Hydrogenase to Metabolize Glucose and Arginine Under Oxic Conditions
Zusammenfassung
The cyanobacterium Synechocystis sp.PCC 6803 possesses a bidirectional NiFe-hydrogenase, HoxEFUYH. It functions to produce hydrogen under dark, fermentative conditions and photoproduces hydrogen when dark-adapted cells are illuminated. Unexpectedly, we found that the deletion of the large subunit of the hydrogenase (HoxH) in Synechocystis leads to an inability to grow on arginine and glucose under continuous light in the presence of oxygen. This is surprising, as the hydrogenase is an oxygen-sensitive enzyme. In wild-type (WT) cells, thylakoid membranes largely disappeared, cyanophycin accumulated, and the plastoquinone (PQ) pool was highly reduced, whereas ΔhoxH cells entered a dormant-like state and neither consumed glucose nor arginine at comparable rates to the WT. Hydrogen production was not traceable in the WT under these conditions. We tested and could show that the hydrogenase does not work as an oxidase on arginine and glucose but has an impact on the redox states of photosynthetic complexes in the presence of oxygen. It acts as an electron valve as an immediate response to the supply of arginine and glucose but supports the input of electrons from arginine and glucose oxidation into the photosynthetic electron chain in the long run, possibly via the NDH-1 complex. Despite the data presented in this study, the latter scenario requires further proof. The exact role of the hydrogenase in the presence of arginine and glucose remains unresolved. In addition, a unique feature of the hydrogenase is its ability to shift electrons between NAD(H), NADP(H), ferredoxin, and flavodoxin, which was recently shown in vitro and might be required for fine-tuning. Taken together, our data show that Synechocystis depends on the hydrogenase to metabolize organic carbon and nitrogen in the presence of oxygen, which might be an explanation for its prevalence in aerobic cyanobacteria.
Zitierform
In: Frontiers in Microbiology Volume 13 (2022-05-31) eissn:1664-302XFörderhinweis
Gefördert durch den Publikationsfonds der Universität KasselZitieren
@article{doi:10.17170/kobra-202206146340,
author={Burgstaller, Heinrich and Wang, Yingying and Caliebe, Johanna and Hüren, Vanessa and Appel, Jens and Boehm, Marko and Leitzke, Sinje and Theune, Marius and King, Paul W. and Gutekunst, Kirstin},
title={Synechocystis sp. PCC 6803 Requires the Bidirectional Hydrogenase to Metabolize Glucose and Arginine Under Oxic Conditions},
journal={Frontiers in Microbiology},
year={2022}
}
0500 Oax 0501 Text $btxt$2rdacontent 0502 Computermedien $bc$2rdacarrier 1100 2022$n2022 1500 1/eng 2050 ##0##http://hdl.handle.net/123456789/13935 3000 Burgstaller, Heinrich 3010 Wang, Yingying 3010 Caliebe, Johanna 3010 Hüren, Vanessa 3010 Appel, Jens 3010 Boehm, Marko 3010 Leitzke, Sinje 3010 Theune, Marius 3010 King, Paul W. 3010 Gutekunst, Kirstin 4000 Synechocystis sp. PCC 6803 Requires the Bidirectional Hydrogenase to Metabolize Glucose and Arginine Under Oxic Conditions / Burgstaller, Heinrich 4030 4060 Online-Ressource 4085 ##0##=u http://nbn-resolving.de/http://hdl.handle.net/123456789/13935=x R 4204 \$dAufsatz 4170 5550 {{Synechocystis}} 5550 {{Cyanobakterien}} 5550 {{Hydrogenasen}} 5550 {{Dihydrolipoamid-Dehydrogenase}} 5550 {{Photosynthese}} 5550 {{Atmung}} 5550 {{Arginin}} 7136 ##0##http://hdl.handle.net/123456789/13935
2022-06-20T13:51:19Z 2022-06-20T13:51:19Z 2022-05-31 doi:10.17170/kobra-202206146340 http://hdl.handle.net/123456789/13935 Gefördert durch den Publikationsfonds der Universität Kassel eng Namensnennung 4.0 International http://creativecommons.org/licenses/by/4.0/ hydrogenase diaphorase photosynthetic complex I (NDH-1) photosynthesis respiration arginine photomixotrophy 570 580 Synechocystis sp. PCC 6803 Requires the Bidirectional Hydrogenase to Metabolize Glucose and Arginine Under Oxic Conditions Aufsatz The cyanobacterium Synechocystis sp.PCC 6803 possesses a bidirectional NiFe-hydrogenase, HoxEFUYH. It functions to produce hydrogen under dark, fermentative conditions and photoproduces hydrogen when dark-adapted cells are illuminated. Unexpectedly, we found that the deletion of the large subunit of the hydrogenase (HoxH) in Synechocystis leads to an inability to grow on arginine and glucose under continuous light in the presence of oxygen. This is surprising, as the hydrogenase is an oxygen-sensitive enzyme. In wild-type (WT) cells, thylakoid membranes largely disappeared, cyanophycin accumulated, and the plastoquinone (PQ) pool was highly reduced, whereas ΔhoxH cells entered a dormant-like state and neither consumed glucose nor arginine at comparable rates to the WT. Hydrogen production was not traceable in the WT under these conditions. We tested and could show that the hydrogenase does not work as an oxidase on arginine and glucose but has an impact on the redox states of photosynthetic complexes in the presence of oxygen. It acts as an electron valve as an immediate response to the supply of arginine and glucose but supports the input of electrons from arginine and glucose oxidation into the photosynthetic electron chain in the long run, possibly via the NDH-1 complex. Despite the data presented in this study, the latter scenario requires further proof. The exact role of the hydrogenase in the presence of arginine and glucose remains unresolved. In addition, a unique feature of the hydrogenase is its ability to shift electrons between NAD(H), NADP(H), ferredoxin, and flavodoxin, which was recently shown in vitro and might be required for fine-tuning. Taken together, our data show that Synechocystis depends on the hydrogenase to metabolize organic carbon and nitrogen in the presence of oxygen, which might be an explanation for its prevalence in aerobic cyanobacteria. open access Burgstaller, Heinrich Wang, Yingying Caliebe, Johanna Hüren, Vanessa Appel, Jens Boehm, Marko Leitzke, Sinje Theune, Marius King, Paul W. Gutekunst, Kirstin doi:10.3389/fmicb.2022.896190 Synechocystis Cyanobakterien Hydrogenasen Dihydrolipoamid-Dehydrogenase Photosynthese Atmung Arginin publishedVersion eissn:1664-302X Frontiers in Microbiology Volume 13 false 896190
Die folgenden Lizenzbestimmungen sind mit dieser Ressource verbunden: