ArticleChemical science2022
An N⋯H⋯N low-barrier hydrogen bond preorganizes the catalytic site of aspartate aminotransferase to facilitate the second half-reaction.
Article in Chemical science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 19 citations in OpenAlex.
- Structural insights into RNase H catalytic mechanism from room-temperature X-ray and neutron crystallography of apo- and RNA/DNA hybrid-bound enzyme.Current research in structural biology · 2026Article
- Mutation of active site glutamate in serine hydroxymethyltransferase allows trapping a reactive intermediate: a combined neutron and X-ray crystallography study.RSC advances · 2026Article
- Environmental Contributions to Proton Sharing in Protein Low-Barrier Hydrogen Bonds.Biochemistry · 2026Article
- Investigating operational stability and causes of cofactor release in fold type I amine transaminase.Protein science : a publication of the Protein Society · 2026Article
- Anomalous rotational-symmetry breaking in proton arrangement of surface-confined cyclic hydrogen bonds revealed by atomic force spectroscopy.Nature communications · 2025Article
- Environmental Contributions to Proton Sharing in Protein Low-Barrier Hydrogen Bonds.bioRxiv : the preprint server for biology · 2025Article
- Counter-diffusion studies of human transthyretin: the growth of high-quality crystals for X-ray and neutron crystallography.Journal of applied crystallography · 2025Article
- Universality of critical active site glutamate as an acid-base catalyst in serine hydroxymethyltransferase function.Chemical science · 2024Article
- Dynamic interchange between two protonation states is characteristic of active sites of cholinesterases.Protein science : a publication of the Protein Society · 2024Article
- Neutron diffraction from a microgravity-grown crystal reveals the active site hydrogens of the internal aldimine form of tryptophan synthase.Cell reports. Physical science · 2024Article
- Chemical features and machine learning assisted predictions of protein-ligand short hydrogen bonds.Scientific reports · 2023Article
- Revealing protonation states and tracking substrate in serine hydroxymethyltransferase with room-temperature X-ray and neutron crystallography.Communications chemistry · 2023Article
- Chemical Features and Machine Learning Assisted Predictions of Protein-Ligand Short Hydrogen Bonds.Research square · 2023Article
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Authors and funding
10 authors at 5 institutions in 3 countries.
Funding
Abstract
Pyridoxal 5'-phosphate (PLP)-dependent enzymes have been extensively studied for their ability to fine-tune PLP cofactor electronics to promote a wide array of chemistries. Neutron crystallography offers a straightforward approach to studying the electronic states of PLP and the electrostatics of enzyme active sites, responsible for the reaction specificities, by enabling direct visualization of hydrogen atom positions. Here we report a room-temperature joint X-ray/neutron structure of aspartate aminotransferase (AAT) with pyridoxamine 5'-phosphate (PMP), the cofactor product of the first half reaction catalyzed by the enzyme. Between PMP N
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