dc.contributor.author | Yacoby, Iftach | |
dc.contributor.author | Pochekailov, Sergii | |
dc.contributor.author | Zhang, Shuguang | |
dc.contributor.author | Toporik, Hila | |
dc.contributor.author | Ghirardi, Maria L. | |
dc.contributor.author | King, Paul W. | |
dc.date.accessioned | 2012-02-02T20:06:35Z | |
dc.date.available | 2012-02-02T20:06:35Z | |
dc.date.issued | 2011-05 | |
dc.date.submitted | 2011-03 | |
dc.identifier.issn | 0027-8424 | |
dc.identifier.issn | 1091-6490 | |
dc.identifier.uri | http://hdl.handle.net/1721.1/69016 | |
dc.description.abstract | Photosynthetic 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.sponsorship | United States. Dept. of Energy. Fuel Cell Technologies Program | en_US |
dc.description.sponsorship | United States. Dept. of Energy. Office of Basic Energy Sciences | en_US |
dc.description.sponsorship | United States. Dept. of Energy (Contract DE-AC36-08-GO28308) | en_US |
dc.description.sponsorship | The Yang Trust Fund | en_US |
dc.description.sponsorship | European Molecular Biology Organization | en_US |
dc.language.iso | en_US | |
dc.publisher | Proceedings of the National Academy of Sciences (PNAS) | en_US |
dc.relation.isversionof | http://dx.doi.org/10.1073/pnas.1103659108 | en_US |
dc.rights | Article 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.source | PNAS | en_US |
dc.title | Photosynthetic electron partitioning between [FeFe]-hydrogenase and ferredoxin:NADP+-oxidoreductase (FNR) enzymes in vitro | en_US |
dc.type | Article | en_US |
dc.identifier.citation | Yacoby, 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.department | Massachusetts Institute of Technology. Center for Biomedical Engineering | en_US |
dc.contributor.department | Massachusetts Institute of Technology. Department of Chemical Engineering | en_US |
dc.contributor.approver | Yacoby, Iftach | |
dc.contributor.mitauthor | Yacoby, Iftach | |
dc.contributor.mitauthor | Pochekailov, Sergii | |
dc.contributor.mitauthor | Zhang, Shuguang | |
dc.relation.journal | Proceedings of the National Academy of Sciences | en_US |
dc.eprint.version | Final published version | en_US |
dc.type.uri | http://purl.org/eprint/type/JournalArticle | en_US |
eprint.status | http://purl.org/eprint/status/PeerReviewed | en_US |
dspace.orderedauthors | Yacoby, I.; Pochekailov, S.; Toporik, H.; Ghirardi, M. L.; King, P. W.; Zhang, S. | en |
mit.license | PUBLISHER_POLICY | en_US |
mit.metadata.status | Complete | |