Scientists Discover Nickel Enzymes That Transfer Hydrides Between Molecules

Researchers have uncovered a new family of nickel-dependent enzymes capable of transferring hydrides between molecules. This discovery challenges the long-standing view that nickel enzymes primarily handle intramolecular reactions or electron transfers. The study, led by Semersky, Raymond, and Rossi, sheds light on a previously unrecognised catalytic function in biology. The enzymes were first isolated from microbial sources where their unique catalytic abilities may provide adaptive benefits. Their three-dimensional structures were then revealed using X-ray crystallography and advanced nuclear magnetic resonance techniques.

Mechanistic investigations showed that hydride transfer occurs through a precisely coordinated relay system involving amino acid residues and the nickel centre. Unlike typical nickel enzymes, these newly discovered proteins facilitate intermolecular hydride shuttling, a process crucial for many biological transformations.

Further analysis demonstrated their catalytic versatility beyond hydride transfer. They also excel in redox reactions essential for metabolic pathways. The enzymes exhibit high substrate selectivity, fine-tuning reactions through subtle conformational changes and environmental adjustments. These findings expand the known range of metalloenzymes. They also pave the way for bioinspired catalytic design and sustainable chemical applications. Nickel’s role in intermolecular hydride transfer now opens fresh perspectives in enzymatic catalysis.