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JST Press Release

November 3, 2015
Japan Science and Technology Agency (JST)
5-3, Yonbancho, Chiyoda-ku, Tokyo 102-8666

Reconstitution of active semi-synthetic [Fe]-hydrogenase

[Fe]-hydrogenase catalyzes production and utilization of H2 under gentle conditions. Seigo Shima at Max Planck Institute for Terrestrial Microbiology, who was supported by Japan Science Technology Agency (JST), and his collaborators succeeded to produce active semi-synthetic [Fe]-hydrogenase by incorporation of chemically-synthesized compact metal-compound into apoprotein, which was produced in Escherichia coli. The findings provide a basis for future studies for applied fields including production and utilization of H2.

This work was performed in collaboration with Professor Xile Hu at Ecole Polytechnique Fédérale de Lausanne.

Researcher Information

Research Area “Chemical conversion of light energy”
Research Theme “Studies on biosynthesis of the active-site iron-complex from [Fe]-hydrogenase”

Journal Information

Shima, S., Chen, D., Xu, T., Wodrich, M.D., Fujishiro, T., Schultz, K.M., Kahnt, J., Ataka, K. and Hu, X. “Reconstitution of [Fe]-hydrogenase using model complexes”. Nature Chemistry, Published online 02 November 2015, doi: 10.1038/nchem.2382.


[About Research]
Seigo Shima, Ph.D.
Group Leader, Max Planck Institute for Terrestrial Microbiology
URL: http://www.mpi-marburg.mpg.de/shima/

[About Program]
Sofia Saori Suzuki
Green Innovation Group, Department of Innovation Research, JST


JST, an integrated organization of science and technology in Japan, establishes an infrastructure for the entire process from the creation of knowledge to the return to the society. For more information, visit http://www.jst.go.jp/EN/