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

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

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...

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Bibliographic Details
Main Authors: Muhd Noor, Noor Dina, Matsuura, Hiroaki, Nishikawa, Koji, Tai, Hulin, Hirota, Shun, Kim, Jaehyun, Kang, Jiyoung, Tateno, Masaru, Yoon, Ki-Seok, Ogo, Seiji, Kubota, Shintaro, Shomura, Yasuhito, Higuchi, Yoshiki
Format: Article
Language:English
Published: Royal Society of Chemistry 2018
Online Access:http://psasir.upm.edu.my/id/eprint/73727/1/Redox-dependent%20conformational%20changes%20of%20a%20proximal%20%5B4Fe-4S%5D%20cluster%20in%20Hyb-type%20%5BNiFe%5D-hydrogenase%20to%20protect%20the%20active%20site%20from%20O2.pdf

Internet

http://psasir.upm.edu.my/id/eprint/73727/1/Redox-dependent%20conformational%20changes%20of%20a%20proximal%20%5B4Fe-4S%5D%20cluster%20in%20Hyb-type%20%5BNiFe%5D-hydrogenase%20to%20protect%20the%20active%20site%20from%20O2.pdf

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