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dc.contributor.authorYacoby, Iftach
dc.contributor.authorPochekailov, Sergii
dc.contributor.authorZhang, Shuguang
dc.contributor.authorToporik, Hila
dc.contributor.authorGhirardi, Maria L.
dc.contributor.authorKing, Paul W.
dc.date.accessioned2012-02-02T20:06:35Z
dc.date.available2012-02-02T20:06:35Z
dc.date.issued2011-05
dc.date.submitted2011-03
dc.identifier.issn0027-8424
dc.identifier.issn1091-6490
dc.identifier.urihttp://hdl.handle.net/1721.1/69016
dc.description.abstractPhotosynthetic water splitting, coupled to hydrogenase-catalyzed hydrogen production, is considered a promising clean, renewable source of energy. It is widely accepted that the oxygen sensitivity of hydrogen production, combined with competition between hydrogenases and NADPH-dependent carbon dioxide fixation are the main limitations for its commercialization. Here we provide evidence that, under the anaerobic conditions that support hydrogen production, there is a significant loss of photosynthetic electrons toward NADPH production in vitro. To elucidate the basis for competition, we bioengineered a ferredoxin-hydrogenase fusion and characterized hydrogen production kinetics in the presence of Fd, ferredoxin:NADP+-oxidoreductase (FNR), and NADP+. Replacing the hydrogenase with a ferredoxin-hydrogenase fusion switched the bias of electron transfer from FNR to hydrogenase and resulted in an increased rate of hydrogen photoproduction. These results suggest a new direction for improvement of biohydrogen production and a means to further resolve the mechanisms that control partitioning of photosynthetic electron transport.en_US
dc.description.sponsorshipUnited States. Dept. of Energy. Fuel Cell Technologies Programen_US
dc.description.sponsorshipUnited States. Dept. of Energy. Office of Basic Energy Sciencesen_US
dc.description.sponsorshipUnited States. Dept. of Energy (Contract DE-AC36-08-GO28308)en_US
dc.description.sponsorshipThe Yang Trust Funden_US
dc.description.sponsorshipEuropean Molecular Biology Organizationen_US
dc.language.isoen_US
dc.publisherProceedings of the National Academy of Sciences (PNAS)en_US
dc.relation.isversionofhttp://dx.doi.org/10.1073/pnas.1103659108en_US
dc.rightsArticle is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.en_US
dc.sourcePNASen_US
dc.titlePhotosynthetic electron partitioning between [FeFe]-hydrogenase and ferredoxin:NADP+-oxidoreductase (FNR) enzymes in vitroen_US
dc.typeArticleen_US
dc.identifier.citationYacoby, I. et al. “Photosynthetic electron partitioning between [FeFe]-hydrogenase and ferredoxin:NADP+-oxidoreductase (FNR) enzymes in vitro.” Proceedings of the National Academy of Sciences 108.23 (2011): 9396-9401. Web. 2 Feb. 2012.en_US
dc.contributor.departmentMassachusetts Institute of Technology. Center for Biomedical Engineeringen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Chemical Engineeringen_US
dc.contributor.approverYacoby, Iftach
dc.contributor.mitauthorYacoby, Iftach
dc.contributor.mitauthorPochekailov, Sergii
dc.contributor.mitauthorZhang, Shuguang
dc.relation.journalProceedings of the National Academy of Sciencesen_US
dc.eprint.versionFinal published versionen_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsYacoby, I.; Pochekailov, S.; Toporik, H.; Ghirardi, M. L.; King, P. W.; Zhang, S.en
mit.licensePUBLISHER_POLICYen_US
mit.metadata.statusComplete


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