Scientists discover nickel enzymes with unprecedented hydride transfer abilities

Scientists have uncovered a new family of nickel-dependent enzymes capable of intermolecular hydride transfer. These enzymes were isolated from microbial sources, where their unique catalytic functions may provide adaptive benefits. The discovery challenges previous assumptions about nickel enzymes, which were typically linked to intramolecular reactions or electron transfer. Historically, nickel enzymes were known for their role in intramolecular processes. This new family, however, facilitates hydride movement between separate substrate molecules—a rare function for nickel centres in intermolecular contexts.

The enzymes' three-dimensional structures were determined using X-ray crystallography and advanced nuclear magnetic resonance. Mechanistic studies revealed that hydride shuttling occurs through a precision-tuned relay system involving amino acid residues and the metal centre. Their remarkable substrate selectivity allows them to modulate reaction outcomes via subtle conformational shifts and microenvironmental adjustments.

Beyond hydride transfer, these enzymes also catalyse redox reactions essential to metabolic pathways. Their catalytic versatility expands the known range of metalloenzymes and offers new possibilities for bioinspired design. The discovery broadens the understanding of metalloenzymes and their potential applications. Harnessing these enzymes or their synthetic versions could transform catalytic processes in green chemistry and bioelectrochemical systems. Their unique properties open doors for sustainable and efficient chemical solutions.