Discovery and characterization of a nickel enzyme family that catalyses intermolecular hydride shuttling
Zoë L Semersky, Conor G Raymond, John M Rossi, Heike Hofstetter, Pranav Rao, Monica E Neugebauer · 2026
Read Discovery and characterization of a nickel enzyme family that catalyses intermolecular hydride shuttling by Zoë L Semersky, Conor G Raymond, John M Rossi, Heike Hofstetter, Pranav Rao, Monica E Neugebauer (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/PMC13524815.txt.
Description
Zoë L. Semersky and colleagues announce, in a 2026 study, a new family of nickel-dependent enzymes found through a bioinformatic search pipeline. Nickel enzymes catalyze demanding reactions in nature, from methane formation to hydrogen handling, yet only about a dozen were known. The pipeline hunted for enzymes using a nickel pincer nucleotide cofactor.
One family member, named NphT, was characterized in detail. It moves a hydride, a hydrogen atom with its electrons, between separate molecules, shown through its scrambling of sugars. A very high-resolution crystal structure captured the enzyme with its cofactor, and mutation studies probed the mechanism. The family sits inside the large aldo-keto reductase superfamily and acts on varied substrates including sugars and drugs. The authors offer the pipeline as a route to more nickel enzymes.
Catalog record
| CREATOR | Zoë L Semersky, Conor G Raymond, John M Rossi, Heike Hofstetter, Pranav Rao, Monica E Neugebauer |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 66939 |
| LICENSE | https://creativecommons.org/licenses/by/4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |