How Fe(II)/2-Oxoglutarate Oxygenase Chooses Chlorination over Hydroxylation: Electric Field-Driven Ligand Exchange Governs C–Cl Formation
Simahudeen Bathir Jaber Sathik Rifayee, Midhun George Thomas, Anandhu Krishnan, Kritika Gupta, Carter Davis, Tatyana Karabencheva-Christova, Christo Z. Christov · 2026
Read How Fe(II)/2-Oxoglutarate Oxygenase Chooses Chlorination over Hydroxylation: Electric Field-Driven Ligand Exchange Governs C–Cl Formation by Simahudeen Bathir Jaber Sathik Rifayee, Midhun George Thomas, Anandhu Krishnan, Kritika Gupta, Carter Davis, Tatyana Karabencheva-Christova, Christo Z. Christov (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/pmc-13244439.txt.
Description
Simahudeen Bathir Jaber Sathik Rifayee and colleagues explain how one enzyme favors chlorine over oxygen in 2026 computer work. The enzyme BesD adds chlorine to the amino acid lysine with sharp precision. Its close cousins add oxygen instead, and the switch between the two paths was puzzling.
Simulations tracked the enzyme's iron center step by step during the reaction. The chlorine and oxygen partners swap places in two moves before the key bond forms. That swap puts chlorine where the protein's electric field pulls hardest on the iron-chlorine bond. Cousin enzymes edited toward chlorination used the same swap. The results give engineers a recipe for turning oxygen-adding enzymes into chlorine-adding ones.
Catalog record
| CREATOR | Simahudeen Bathir Jaber Sathik Rifayee, Midhun George Thomas, Anandhu Krishnan, Kritika Gupta, Carter Davis, Tatyana Karabencheva-Christova, Christo Z. Christov |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 75 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |