z-logo
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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom