Effect of methanogenic substrates on coenzyme F420-dependent N5,N10-methylene-H4MPT dehydrogenase, N5,N10-methenyl-H4MPT cyclohydrolase and F420-reducing hydrogenase activities in Methanosarcina barkeri

Simple item page
dc.contributor.authorMukhopadhyay, Biswarupen
dc.contributor.authorPurwantini, Endangen
dc.contributor.authorDaniels, Lacyen
dc.date.accessioned2023-01-19T15:47:46Zen
dc.date.available2023-01-19T15:47:46Zen
dc.date.issued1993en
dc.date.updated2023-01-18T18:59:43Zen
dc.description.abstractWe measured F420-dependent N5,N10-methylenetetrahydro-methanopterin dehydrogenase, N5, N10-methenyltetrahydro-methanopterin cyclohydrolase, and F420-reducing hydrogenase levels in Methanosarcina barkeri grown on various substrates. Variation in dehydrogenase levels during growth on a specific substrate was usually <3-fold, and much less for cyclohydrolase. H2−CO2-, methanol-, and H2−CO2+ methanol-grown cells had roughly equivalent levels of dehydrogenase and cyclohydrolase. In acetate-grown cells cyclohydrolase level was lowered 2 to 3-fold and dehydrogenase 10 to 80-fold; this was not due to repression by acetate, since, if cultures growing on acetate were supplemented with methanol or H2−CO2, dehydrogenase levels increased 14 to 19-fold, and cyclohydrolase levels by 3 to 4-fold. Compared to H2−CO2- or methanol-grown cells, acetate-or H2−CO2 + methanol-grown cells had lower levels of and less growth phase-dependent variation in hydrogenase activity. Our data are consistent with the following hypotheses: 1. M. barkeri oxidizes methanol via a portion of the CO2-reduction pathway operated in the reverse direction. 2. When steps from CO2 to CH3-S-CoM in the CO2-reduction pathway (in either direction) are not used for methanogenesis, hydrogenase activity is lowered.en
dc.description.versionPublished versionen
dc.format.extentPages 141-146en
dc.format.mimetypeapplication/pdfen
dc.identifier.orcidMukhopadhyay, Biswarup [0000-0003-0736-0298]en
dc.identifier.orcidPurwantini, Endang [0000-0002-4113-9995]en
dc.identifier.urihttp://hdl.handle.net/10919/113257en
dc.identifier.volume159en
dc.language.isoenen
dc.rightsIn Copyrighten
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en
dc.subjectBiotechnology, Biomaterials, and Energyen
dc.titleEffect of methanogenic substrates on coenzyme F<sub>420</sub>-dependent N<sup>5</sup>,N<sup>10</sup>-methylene-H<sub>4</sub>MPT dehydrogenase, N<sup>5</sup>,N<sup>10</sup>-methenyl-H<sub>4</sub>MPT cyclohydrolase and F<sub>420</sub>-reducing hydrogenase activities in <i>Methanosarcina barkeri</i>en
dc.title.serialArchives of Microbiologyen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten
dc.type.otherArticleen
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/Internal Med-Subgroupen

Files

Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
Mbarkeri_Methanogenesis_1993.pdf
Size:
579.63 KB
Format:
Adobe Portable Document Format
Description:
Published version
Download

Collections

All Faculty Deposits
Scholarly Works, Biochemistry