Redox-dependent conformational changes of a proximal [4Fe–4S] cluster in Hyb-type [NiFe]-hydrogenase to protect the active site from O2. Issue 87 (17th October 2018)

• Record Type: Journal Article
• Authors: Noor, Noor Dina Muhd; 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
• Is Part Of: Chemical communications. Volume 54:Issue 87(2018)
• Page Start: 12385
• Page End: 12388
• Publication Date: 2018-10-17
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c8cc06261g
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : Citrobacter sp. S-77 [NiFe]-hydrogenase harbors a standard [4Fe–4S] cluster proximal to the Ni–Fe active site. 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.