Show simple item record

dc.contributor.authorCollins, Johnen
dc.contributor.authorZhang, Tingen
dc.contributor.authorHuston, Scotten
dc.contributor.authorSun, Fangfangen
dc.contributor.authorZhang, Y. H. Percivalen
dc.contributor.authorFu, Jinglinen
dc.date.accessioned2017-01-18T03:08:11Zen
dc.date.available2017-01-18T03:08:11Zen
dc.date.issued2016-05-04en
dc.identifier.issn1932-6203en
dc.identifier.urihttp://hdl.handle.net/10919/74378en
dc.description.abstractBackground Redox cofactors of NADH/NADPH participate in many cellular metabolic pathways for facilitating the electron transfer from one molecule to another in redox reactions. Transhydrogenase plays an important role in linking catabolism and anabolism, regulating the ratio of NADH/NADPH in cells. The cytoplasmic transhydrogenases could be useful to engineer synthetic biochemical pathways for the production of high-value chemicals and biofuels. Methodology/Principal Findings A transhydrogenase activity was discovered for a FMN-bound diaphorase (DI) from Geobacillus stearothermophilus under anaerobic conditions. The DI-catalyzed hydride exchange were monitored and characterized between a NAD(P)H and a thio-modified NAD+ analogue. This new function of DI was demonstrated to transfer a hydride from NADPH to NAD+ that was consumed by NAD-specific lactate dehydrogenase and malic dehydrogenase. Conclusions/Significance We discover a novel transhydrogenase activity of a FMN-DI by stabilizing the reduced state of FMNH2 under anaerobic conditions. FMN-DI was demonstrated to catalyze the hydride transfer between NADPH and NAD+. In the future, it may be possible to incorporate this FMN-DI into synthetic enzymatic pathways for balancing NADH generation and NADPH consumption for anaerobic production of biofuels and biochemicals.en
dc.format.extent? - ? (9) page(s)en
dc.languageEnglishen
dc.publisherPLOSen
dc.relation.urihttp://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000375676400087&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=930d57c9ac61a043676db62af60056c1en
dc.rightsCreative Commons Attribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.subjectMultidisciplinary Sciencesen
dc.subjectScience & Technology - Other Topicsen
dc.subjectPROTON-TRANSLOCATING TRANSHYDROGENASEen
dc.subjectESCHERICHIA-COLIen
dc.subjectNUCLEOTIDE TRANSHYDROGENASEen
dc.subjectENZYMATIC PATHWAYen
dc.subjectNADH OXIDASEen
dc.subjectPURIFICATIONen
dc.subjectMECHANISMen
dc.titleA Hidden Transhydrogen Activity of a FMN-Bound Diaphorase under Anaerobic Conditionsen
dc.typeArticle - Refereeden
dc.description.versionPublished (Publication status)en
dc.contributor.departmentBiological Systems Engineeringen
dc.title.serialPLOS ONEen
dc.identifier.doihttps://doi.org/10.1371/journal.pone.0154865en
dc.identifier.volume11en
dc.identifier.issue5en
pubs.organisational-group/Virginia Techen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciencesen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciences/Biological Systems Engineeringen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciences/CALS T&R Facultyen
pubs.organisational-group/Virginia Tech/All T&R Facultyen
pubs.organisational-group/Virginia Tech/Faculty of Health Sciencesen


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record

Creative Commons Attribution 4.0 International
License: Creative Commons Attribution 4.0 International