The oxidative inactivation of FeFe hydrogenase reveals the flexibility of the H-cluster

Fourmond, Vincent; Greco, Claudio; Sybirna, Kateryna; Baffert, Carole; Wang, Po Hung; Ezanno, Pierre; Montefiori, Marco; Bruschi, Maurizio; Meynial-Salles, Isabelle; Soucaille, Philippe; Blumberger, Jochen; Bottin, Herv�; De Gioia, Luca; L�ger, Christophe

Abstract

Nature is a valuable source of inspiration in the design of catalysts, and various approaches are used to elucidate the mechanism of hydrogenases, the enzymes that oxidize or produce H 2. In FeFe hydrogenases, H 2 oxidation occurs at the H-cluster, and catalysis involves H 2 binding on the vacant coordination site of an iron centre. Here, we show that the reversible oxidative inactivation of this enzyme results from the binding of H 2 to coordination positions that are normally blocked by intrinsic CO ligands. This flexibility of the coordination sphere around the reactive iron centre confers on the enzyme the ability to avoid harmful reactions under oxidizing conditions, including exposure to O 2. The versatile chemistry of the diiron cluster in the natural system might inspire the design of novel synthetic catalysts for H 2 oxidation. © 2014 Macmillan Publishers Limited.

Citation

Fourmond, V., Greco, C., Sybirna, K., Baffert, C., Wang, P. H., Ezanno, P., …Léger, C. (2014). The oxidative inactivation of FeFe hydrogenase reveals the flexibility of the H-cluster. Nature Chemistry, 6(4), 336-342. https://doi.org/10.1038/nchem.1892

• Journal Article Type: Article
• Acceptance Date: Feb 11, 2014
• Online Publication Date: Mar 16, 2014
• Publication Date: 2014-04
• Deposit Date: Jan 4, 2021
• Journal: Nature Chemistry
• Print ISSN: 1755-4330
• Electronic ISSN: 1755-4349
• Publisher: Nature Publishing Group
• Peer Reviewed: Peer Reviewed
• Volume: 6
• Issue: 4
• Pages: 336-342
• DOI: https://doi.org/10.1038/nchem.1892
• Public URL: https://nottingham-repository.worktribe.com/output/3164444
• Publisher URL: https://www.nature.com/articles/nchem.1892