Takeshi Hiromoto Koji Nishikawa Seiya Inoue Hideaki Ogata Yuta Hori Katsuhiro Kusaka Yu Hirano Kazuo Kurihara Yasuteru Shigeta Taro Tamada Yoshiki Higuchi
Chemical Science 14(35) 9306-9315 2023年 [査読有り]
We report the first neutron structure of [NiFe]-hydrogenase in its oxidized state. This study leads to new insights into the oxidized active site and visualization of the protons characteristic of the oxidized enzyme.
Hydrogenases catalyze the reversible oxidation of H2. Carbon monoxide (CO) is known to be a competitive inhibitor of O2-sensitive [NiFe]-hydrogenases. Although the activities of some O2-tolerant [NiFe]-hydrogenases are unaffected by CO, the partia...
Takeshi Hiromoto Koji Nishikawa Taro Tamada Yoshiki Higuchi
TOPICS IN CATALYSIS 64(9-12) 622-630 2021年8月 [査読有り]
X-ray crystallography is the most powerful tool for obtaining structural information about protein molecules, affording accurate and precise positions for all of the atoms in the protein except for hydrogen. However, hydrogen species play crucial ...
A membrane-bound hydrogenase from Desulfovibrio vulgaris Miyazaki F is a metalloenzyme that contains a binuclear Ni-Fe complex in its active site and mainly catalyzes the oxidation of molecular hydrogen to generate a proton gradient in the bacteri...
Hydrogenases control the proton concentration in cells, which is an essential function for hydrogen metabolism in several microorganisms. Some [NiFe]-hydrogenases are catalytically active under air and are thus of great interest for developing bio...
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理学研究科