著者

庄村 康人 樋口 芳樹

出版者

一般社団法人 日本生物物理学会

雑誌

生物物理 (ISSN:05824052)

巻号頁・発行日

vol.58, no.6, pp.297-302, 2018 (Released:2018-11-27)

参考文献数

29

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Hydrogenases play crucial roles in the hydrogen metabolism by catalyzing the simple reaction: H2 ⇄ 2H+ + 2e–. While the enzymes are of industrial importance, there are a number of serious obstacles to the applications such as the catalytic electrode in the fuel cells, which include the stability to O2. Here we summarize the structural and functional properties of [NiFe]-hydrogenases with focusing the protective mechanism against O2. The recent our studies have revealed that not the catalytic site itself but the Fe-S cluster equipped as the electron pathway is of functional importance for preventing from the attack by O2.

著者

庄村 康人 樋口 芳樹

出版者

一般社団法人 日本生物物理学会

雑誌

生物物理 (ISSN:05824052)

巻号頁・発行日

vol.53, no.2, pp.082-085, 2013 (Released:2013-03-28)

参考文献数

14

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Hydrogenases play crucial roles in the hydrogen metabolism by catalyzing the production and decomposition of H2. The membrane-bound [NiFe]-hydrogenase is a representative member of O2-tolerant hydrogenases, but the mechanism of which is poorly understood. Recently, we and other groups have reported the crystal structures of membrane-bound [NiFe]-hydrogenases, which revealed an unprecedented structure of one of three iron-sulfur clusters in the enzyme. Together with the spectroscopic study that shows the unique iron-sulfur cluster takes three oxidation states under physiological redox potentials, we concluded that the iron-sulfur cluster plays a key role in the O2-tolerant mechanism of the membrane-bound [NiFe]-hydrogenase.

著者

根来 誠司 大木 卓 鶴亀 純也 松本 圭司 武尾 正弘 柴田 直樹 樋口 芳樹

出版者

公益社団法人日本生物工学会

雑誌

日本生物工学会大会講演要旨集

巻号頁・発行日

vol.16, 2004-08-25