Nitrite reductase activity in F420-dependent sulphite reductase (Fsr) from Methanocaldococcus jannaschii

dc.contributor.authorHeryakusuma, Christianen
dc.contributor.authorJohnson, Eric F.en
dc.contributor.authorPurwantini, Endangen
dc.contributor.authorMukhopadhyay, Biswarupen
dc.date.accessioned2024-01-17T20:26:30Zen
dc.date.available2024-01-17T20:26:30Zen
dc.date.issued2023-04-20en
dc.description.abstract<i>Methanocaldococcus jannaschii</i> (<i>Mj</i>), a hyperthermophilic and evolutionarily deeply rooted methanogenic archaeon from a deep-sea hydrothermal vent, produces F<sub>420</sub>-dependent sulphite reductase (Fsr) in response to exposure to sulphite. This enzyme allows <i>Mj</i> to detoxify sulphite, a potent inhibitor of methyl coenzyme-M reductase (Mcr), by reducing it to sulphide with reduced coenzyme F<sub>420</sub> (F<sub>420</sub>H<sub>2</sub>) as an electron donor; Mcr is essential for energy production for a methanogen. Fsr allows <i>Mj</i> to utilize sulphite as a sulphur source. Nitrite is another potent inhibitor of Mcr and is toxic to methanogens. It is reduced by most sulphite reductases. In this study, we report that <i>Mj</i>Fsr reduced nitrite to ammonia with F<sub>420</sub>H<sub>2</sub> with physiologically relevant <i>K</i> <sub>m</sub> values (nitrite, 8.9 µM; F<sub>420</sub>H<sub>2</sub>, 9.7 µM). The enzyme also reduced hydroxylamine with a <i>K</i> <sub>m</sub> value of 112.4 µM, indicating that it was an intermediate in the reduction of nitrite to ammonia. These results open the possibility that <i>Mj</i> could use nitrite as a nitrogen source if it is provided at a low concentration of the type that occurs in its habitat.en
dc.description.versionPublished versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.doihttps://doi.org/10.1099/acmi.0.000482.v3en
dc.identifier.eissn2516-8290en
dc.identifier.issn2516-8290en
dc.identifier.issue4en
dc.identifier.orcidPurwantini, Endang [0000-0002-4113-9995]en
dc.identifier.orcidMukhopadhyay, Biswarup [0000-0003-0736-0298]en
dc.identifier.otherPMC10202398en
dc.identifier.other000482.v3 (PII)en
dc.identifier.pmid37223055en
dc.identifier.urihttps://hdl.handle.net/10919/117388en
dc.identifier.volume5en
dc.language.isoenen
dc.publisherMicrobiology Societyen
dc.relation.urihttps://www.ncbi.nlm.nih.gov/pubmed/37223055en
dc.rightsCreative Commons Attribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.subjectF420-dependent nitrite reductase (FNiR)en
dc.subjectF420-dependent sulphite reductase (Fsr)en
dc.subjectF420H2en
dc.subjectcoenzyme F420en
dc.subjectdeazaflavinen
dc.subjectmethanogenen
dc.titleNitrite reductase activity in F<sub>420</sub>-dependent sulphite reductase (Fsr) from <i>Methanocaldococcus jannaschii</i>en
dc.title.serialAccess Microbiologyen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten
dc.type.otherresearch-articleen
dc.type.otherJournal Articleen
dcterms.dateAccepted2023-01-25en
pubs.organisational-group/Virginia Techen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciencesen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciences/Biochemistryen
pubs.organisational-group/Virginia Tech/Faculty of Health Sciencesen
pubs.organisational-group/Virginia Tech/All T&R Facultyen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciences/CALS T&R Facultyen
pubs.organisational-group/Virginia Tech/VT Carilion School of Medicineen
pubs.organisational-group/Virginia Tech/VT Carilion School of Medicine/Internal Medicineen
pubs.organisational-group/Virginia Tech/VT Carilion School of Medicine/Internal Medicine/Secondary Appointment- Internal Medicineen
pubs.organisational-group/Virginia Tech/VT Carilion School of Medicine/Internal Medicine/Internal Med-Subgroupen

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