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Wiring of photosystem II to hydrogenase for photoelectrochemical water splitting
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Mersch, Dirk, Lee, Chong-Yong, Zhang, Jenny Zhenqi, Brinkert, Katharina, Fontecilla-Camps, Juan C., Rutherford, A. William and Reisner, Erwin (2015) Wiring of photosystem II to hydrogenase for photoelectrochemical water splitting. Journal of the American Chemical Society, 137 (26). pp. 8541-8549. doi:10.1021/jacs.5b03737 ISSN 0002-7863.
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WRAP-wiring-photosystem-II-hydrogenase-photoelectrochemical-water-splitting-Brinkert-2019.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution 4.0. Download (3800Kb) | Preview |
Official URL: http://dx.doi.org/10.1021/jacs.5b03737
Abstract
In natural photosynthesis, light is used for the production of chemical energy carriers to fuel biological activity. The re-engineering of natural photosynthetic pathways can provide inspiration for sustainable fuel production and insights for understanding the process itself. Here, we employ a semiartificial approach to study photobiological water splitting via a pathway unavailable to nature: the direct coupling of the water oxidation enzyme, photosystem II, to the H2 evolving enzyme, hydrogenase. Essential to this approach is the integration of the isolated enzymes into the artificial circuit of a photoelectrochemical cell. We therefore developed a tailor-made hierarchically structured indium–tin oxide electrode that gives rise to the excellent integration of both photosystem II and hydrogenase for performing the anodic and cathodic half-reactions, respectively. When connected together with the aid of an applied bias, the semiartificial cell demonstrated quantitative electron flow from photosystem II to the hydrogenase with the production of H2 and O2 being in the expected two-to-one ratio and a light-to-hydrogen conversion efficiency of 5.4% under low-intensity red-light irradiation. We thereby demonstrate efficient light-driven water splitting using a pathway inaccessible to biology and report on a widely applicable in vitro platform for the controlled coupling of enzymatic redox processes to meaningfully study photocatalytic reactions.
Item Type: | Journal Article | ||||||||||||||||||||||||||||||
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Subjects: | Q Science > QK Botany | ||||||||||||||||||||||||||||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||||||||||||||||||||||||||||
Library of Congress Subject Headings (LCSH): | Photosynthesis, Hydrogenase | ||||||||||||||||||||||||||||||
Journal or Publication Title: | Journal of the American Chemical Society | ||||||||||||||||||||||||||||||
Publisher: | American Chemical Society | ||||||||||||||||||||||||||||||
ISSN: | 0002-7863 | ||||||||||||||||||||||||||||||
Official Date: | 2015 | ||||||||||||||||||||||||||||||
Dates: |
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Volume: | 137 | ||||||||||||||||||||||||||||||
Number: | 26 | ||||||||||||||||||||||||||||||
Page Range: | pp. 8541-8549 | ||||||||||||||||||||||||||||||
DOI: | 10.1021/jacs.5b03737 | ||||||||||||||||||||||||||||||
Status: | Peer Reviewed | ||||||||||||||||||||||||||||||
Publication Status: | Published | ||||||||||||||||||||||||||||||
Access rights to Published version: | Open Access (Creative Commons) | ||||||||||||||||||||||||||||||
Date of first compliant deposit: | 11 September 2019 | ||||||||||||||||||||||||||||||
Date of first compliant Open Access: | 19 September 2019 | ||||||||||||||||||||||||||||||
RIOXX Funder/Project Grant: |
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