期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 137, 期 26, 页码 8541-8549出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.5b03737
关键词
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资金
- U.K. Engineering and Physical Sciences Research Council [EP/H00338X/2, EP/G037221/1]
- U.K. Biology and Biotechnological Sciences Research Council [BB/K002627/1, BB/K010220/1]
- Marie Curie Intra-European Fellowship [PIEF-GA-2013-625034]
- Marie Curie International Incoming Fellowship [PIIF-GA-2012-328085]
- CEA
- CNRS
- Royal Society
- Biotechnology and Biological Sciences Research Council [BB/K010220/1, BB/K002627/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/H00338X/2, 979919] Funding Source: researchfish
- BBSRC [BB/K002627/1, BB/K010220/1] Funding Source: UKRI
- EPSRC [EP/H00338X/2] Funding Source: UKRI
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 H-2 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 H-2 and O-2 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.
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