9OET

Hydrox with succinate and vanadium(IV)-oxo

Summary for 9OET

• Entry DOI: 10.2210/pdb9oet/pdb
• Descriptor: Lysine hydroxylase, oxovanadium(2+), SUCCINIC ACID, ... (4 entities in total)
• Functional Keywords: halogenase, fe/2og oxidase, biosynthetic protein
• Biological source: Streptomyces roseifaciens
• Total number of polymer chains: 2
• Total formula weight: 59824.73

Authors

Kissman, E.N.,Yang, A.Y.,Whitten, A.M.,Chang, M.C.Y. (deposition date: 2025-04-29, release date: 2025-11-19, Last modification date: 2025-12-03)

Primary citation

Kissman, E.N.,Kipouros, I.,Slater, J.W.,Stone, E.A.,Yang, A.Y.,Braun, A.,Ensberg, A.R.,Whitten, A.M.,Chatterjee, K.,Bogacz, I.,Yano, J.,Martin Bollinger Jr., J.,Chang, M.C.Y.
Dynamic metal coordination controls chemoselectivity in a radical halogenase.
Nat.Chem.Biol., 2025

PubMed Abstract: The activation of inert C(sp)-H bonds by nonheme Fe enzymes provides a powerful biocatalytic platform for the chemical synthesis of molecules with increased sp complexity. In this context, Fe/α-ketoglutarate-dependent radical halogenases are uniquely capable of carrying out transfer of a diverse array of bound anions following C-H activation. Here, we provide experimental evidence that bifurcation of radical rebound after H-atom abstraction can be driven both by the ability of a dynamic metal coordination sphere to reorganize and by a second-sphere hydrogen-bonding network where only two residues are sufficient. In addition, we present crystallographic data supporting the existence of an early peroxyhemiketal intermediate in the O activation pathway of Fe/α-ketoglutarate-dependent enzymes. These data provide a paradigm for understanding the evolution of catalytic plasticity in these enzymes and yields insight into the design principles by which to expand their reaction scope.

PubMed: 41272319
DOI: 10.1038/s41589-025-02077-x

Experimental method

X-RAY DIFFRACTION (1.9 Å)