Premium
Application to Photocatalytic H 2 Production of a Whole‐Cell Reaction by Recombinant Escherichia coli Cells Expressing [FeFe]‐Hydrogenase and Maturases Genes
Author(s) -
Honda Yuki,
Hagiwara Hidehisa,
Ida Shintaro,
Ishihara Tatsumi
Publication year - 2016
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201600177
Subject(s) - clostridium acetobutylicum , escherichia coli , hydrogenase , recombinant dna , photocatalysis , chemistry , biocatalysis , enzyme , biochemistry , gene , catalysis , reaction mechanism , butanol , ethanol
A photocatalytic H 2 production system using an inorganic–bio hybrid photocatalyst could contribute to the efficient utilization of solar energy, but would require the development of a new approach for preparing a H 2 ‐forming biocatalyst. In the present study, we constructed a recombinant strain of Escherichia coli expressing the genes encoding the [FeFe]‐hydrogenase and relevant maturases from Clostridium acetobutylicum NBRC 13948 for use as a biocatalyst. We investigated the direct application of a whole‐cell of the recombinant E . coli . The combination of TiO 2 , methylviologen, and the recombinant E . coli formed H 2 under light irradiation, demonstrating that whole cells of the recombinant E . coli could be employed for photocatalytic H 2 production without any time‐consuming and costly manipulations (for example, enzyme purification). This is the first report of the direct application of a whole‐cell reaction of recombinant E . coli to photocatalytic H 2 production.