ArticleNature chemistry2026
Discovery and characterization of a nickel enzyme family that catalyses intermolecular hydride shuttling.
Article in Nature chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Nickel-dependent enzymes catalyse incredible transformations. However, few have been discovered so far, limiting our understanding of the role of nickel in nature. Here we develop a bioinformatic pipeline to discover a family of nickel pincer mononucleotide (NPMN)-dependent enzymes with structures that are completely distinct from previously reported NPMN-dependent enzymes. We characterize one family member, NPMN-dependent hydride transferase (NphT), and find that it catalyses intermolecular hydride transfer, which we elucidate through its promiscuous disproportionation of sugars. We solve a 1.3-Å resolution crystal structure of NphT bound to NPMN and interrogate its mechanism through mutagenesis. We discover that NphT is one of many unexplored nickel enzymes within the large aldo-keto reductase superfamily, which catalyses reactions on a wide range of molecules, including secondary metabolites, sugars and drugs. This work reveals a unique enzymatic scaffold that can harness nickel, expands the known NPMN-catalysed transformations to intermolecular hydride transfer and establishes a pipeline for the discovery of distinct families of nickel-dependent enzymes.
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