Sequential oxidation of <scp>l</scp> -lysine by a non-heme iron hydroxylase
2-Oxoglutarate-dependent non-heme iron hydroxylases offer a direct route to functionalizing C(sp<sup>3</sup>)-H bonds across a range of substrates, making them prime candidates for chemoenzymatic synthetic strategies. Here, we demonstrate the ability of a non-heme iron L-lysine dioxygenase to perform sequential oxidation and computationally explore structural elements that promote this reactivity.
Authors
- Anoop R. Damodaran (ORCID: https://orcid.org/0000-0002-2094-9956)
- Ambika Bhagi‐Damodaran (ORCID: https://orcid.org/0000-0002-4901-074X)
- Thomas G. Smith (ORCID: https://orcid.org/0000-0002-5197-5030)
- Edward S. Reynolds
Institutions
- University of Minnesota (US)
Publication Details
- Journal
- Chemical Communications
- Published
- 2025-01-01
- DOI
- https://doi.org/10.1039/d5cc00541h
- Primary Topic
- Amino Acid Enzymes and Metabolism
- Type
- article
- Field-Weighted Citation Impact
- 0.00