Redox-dependent conformational changes of a proximal [4Fe–4S] cluster in Hyb-type [NiFe]-hydrogenase to protect the active site from O2

Noor Dina Muhd Noor; Hiroaki Matsuura; Koji Nishikawa; Hulin Tai; Shun Hirota; Jaehyun Kim; Jiyoung Kang; Masaru Tateno; Ki-Seok Yoon; Seiji Ogo; Shintaro Kubota; Yasuhito Shomura; Yoshiki Higuchi

doi:10.1039/C8CC06261G

Redox-dependent conformational changes of a proximal [4Fe–4S] cluster in Hyb-type [NiFe]-hydrogenase to protect the active site from O₂†

Noor Dina Muhd Noor,‡§^ab Hiroaki Matsuura,‡^ab Koji Nishikawa,‡^abc Hulin Tai,

‡^bd Shun Hirota,

^bd Jaehyun Kim,^a Jiyoung Kang,¶^a Masaru Tateno,^a Ki-Seok Yoon,^ef Seiji Ogo,^ef Shintaro Kubota,^ag Yasuhito Shomura^bh and Yoshiki Higuchi

*^abc

Author affiliations

* Corresponding authors

^a Department of Life Science, Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan
E-mail: hig@sci.u-hyogo.ac.jp

^b Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency (JST), 4-1-8 Honcho, Kawaguchi-shi, Saitama 332-0012, Japan

^c RIKEN SPring-8 Center, 1-1-1 Koto, Sayo-gun, Sayo-cho, Hyogo 679-5148, Japan

^d Division of Materials Science, Graduate School of Science and Technology, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan

^e Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, 744 Moto-oka, Nishi-ku, Fukuoka 819-0395, Japan

^f International Institute for Carbon Neutral Energy Research (WPI-I2CNER), Kyushu University, 744 Moto-oka, Nishi-ku, Fukuoka 819-0395, Japan

^g Institute for Research Promotion and Collaboration, University of Hyogo, 123 Minamiekimae-cho, Himeji, Hyogo 670-0962, Japan

^h Institute of Quantum Beam Science, Graduate School of Science and Engineering, Ibaraki University, 4-12-1 Nakanarusawa, Hitachi, Ibaraki 316-8511, Japan

Abstract

Citrobacter sp. S-77 [NiFe]-hydrogenase harbors a standard [4Fe–4S] cluster proximal to the Ni–Fe active site. The presence of relocatable water molecules and a flexible aspartate enables the [4Fe–4S] to display redox-dependent conformational changes. These structural features are proposed to be the key aspects that protect the active site from O₂ attack.

Chemical Communications

Redox-dependent conformational changes of a proximal [4Fe–4S] cluster in Hyb-type [NiFe]-hydrogenase to protect the active site from O₂†

Abstract

Supplementary files

Article information

Download Citation

Permissions

Redox-dependent conformational changes of a proximal [4Fe–4S] cluster in Hyb-type [NiFe]-hydrogenase to protect the active site from O₂

Social activity

Search articles by author

Spotlight

Advertisements

Chemical Communications