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Synechocystis sp. PCC 6803 Requires the Bidirectional Hydrogenase to Metabolize Glucose and Arginine Under Oxic Conditions

dc.date.accessioned2022-06-20T13:51:19Z
dc.date.available2022-06-20T13:51:19Z
dc.date.issued2022-05-31
dc.identifierdoi:10.17170/kobra-202206146340
dc.identifier.urihttp://hdl.handle.net/123456789/13935
dc.description.sponsorshipGefördert durch den Publikationsfonds der Universität Kasselger
dc.language.isoengeng
dc.rightsNamensnennung 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjecthydrogenaseeng
dc.subjectdiaphoraseeng
dc.subjectphotosynthetic complex I (NDH-1)eng
dc.subjectphotosynthesiseng
dc.subjectrespirationeng
dc.subjectarginineeng
dc.subjectphotomixotrophyeng
dc.subject.ddc570
dc.subject.ddc580
dc.titleSynechocystis sp. PCC 6803 Requires the Bidirectional Hydrogenase to Metabolize Glucose and Arginine Under Oxic Conditionseng
dc.typeAufsatz
dcterms.abstractThe 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.eng
dcterms.accessRightsopen access
dcterms.creatorBurgstaller, Heinrich
dcterms.creatorWang, Yingying
dcterms.creatorCaliebe, Johanna
dcterms.creatorHüren, Vanessa
dcterms.creatorAppel, Jens
dcterms.creatorBoehm, Marko
dcterms.creatorLeitzke, Sinje
dcterms.creatorTheune, Marius
dcterms.creatorKing, Paul W.
dcterms.creatorGutekunst, Kirstin
dc.relation.doidoi:10.3389/fmicb.2022.896190
dc.subject.swdSynechocystisger
dc.subject.swdCyanobakterienger
dc.subject.swdHydrogenasenger
dc.subject.swdDihydrolipoamid-Dehydrogenaseger
dc.subject.swdPhotosyntheseger
dc.subject.swdAtmungger
dc.subject.swdArgininger
dc.type.versionpublishedVersion
dcterms.source.identifiereissn:1664-302X
dcterms.source.journalFrontiers in Microbiologyeng
dcterms.source.volumeVolume 13
kup.iskupfalse
dcterms.source.articlenumber896190


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