Binding of exogenous cyanide reveals new active-site states in [FeFe] hydrogenases

Journal article

Hydrogen could provide a suitable means for storing energy from intermittent renewable sources for later use on demand. However, many challenges remain regarding the activity, specificity, stability and sustainability of current hydrogen production and consumption methods. The lack of efficient catalysts based on abundant and sustainable elements lies at the heart of this problem. Nature's solution led to the evolution of hydrogenase enzymes capable of reversible hydrogen conversion at high rates using iron- and nickel-based active sites. Through a detailed understanding of these enzymes, we can learn how to mimic them to engineer a new generation of highly active synthetic catalysts. Incredible progress has been made in our understanding of biological hydrogen activation over the last few years. In particular, detailed studies of the [FeFe] hydrogenase class have provided substantial insight into a sophisticated, optimised, molecular catalyst, the active site H-cluster. In this short perspective, we will summarise recent findings and highlight the missing pieces needed to complete the puzzle

Authors: Martini, MA; Bikbaev, K; Pang, Y; Lorent, C; Wiemann, C

• Publication status: Published
• Peer review status: Peer reviewed
• Publisher: Royal Society of Chemistry
• Journal: Chemical Science
• Volume: 14
• Issue: 11
• Pages: 2826-2838
• Publication date: 2023-03-15
• DOI: 10.1039/d2sc06098a
• EISSN: 2041-6539
• ISSN: 2041-6520
• Language: English
• Keywords: Cofactor; Active site; Photochemistry; Physics; Catalysis; Hydrogenase; Cyanide; Acceptor; Enzyme; Chemistry; Binding site; Inorganic chemistry; Biochemistry