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JST Press Release

Oct. 29, 2013
Japan Science and Technology Agency (JST)
5-3, Yonbancho, Chiyoda-ku, Tokyo 102-8666
URL http://www.jst.go.jp/EN/index.html

Discovery of an enzyme responsible for the [Fe]-hydrogenase active-site biosynthesis

Platinum or other rare metals are required as catalysts for industrial processes involving conversion of hydrogen gas (H2). However, since such rare metals are very expensive and their amounts are quite limited, invention of alternative catalysts is desired. Hydrogenases, a type of enzymes of microorganisms, catalyze H2-production and –utilization. Construction of new catalysts by mimicking the hydrogenases enzymes is a hot topic in chemistry. Shima and his coworkers discovered a novel enzyme involved in biosynthesis of the [Fe]-hydrogenase active-site. This finding will lead researches developing new catalysts for artificial photosynthesis and for fuel-cell electrodes in future.

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

Takashi Fujishiro et al. “Identification of the HcgB Enzyme in [Fe]-Hydrogenase-Cofactor Biosynthesis”
Angewandte Chemie International Edition, Published online 7 November 2013
doi: 10.1002/anie.201306745


[About Research]
Seigo Shima, Ph.D.
Biochemistry group leader, Max Planck Institute for Terrestrial Microbiology
PRESTO researcher, Japan Science and Technology Agency

[About Program]
Masashi Furukawa, Koji Matsuo, Sofia Suzuki
Green Innovation Group, Department of Innovation Research,
Japan Science and Technology Agency


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/