Abstract
The Front Cover represents the discovery of a novel path during a scientist′s journey towards the biocatalytic incorporation of chlorine into L-proline. In their Communication, A. Papadopoulou et al describe the remodeling of an Fe/αKG hydroxylase into a halogenase utilizing the tools of protein engineering. By employing several rounds of directed evolution, a remodeled halogenase variant with a 98-fold improved apparent kcat/Km was generated. The reprogrammed biocatalyst is the first example of a stereo- and regioselective halogenase derivatizing L-proline at the C3 position and highlights the possibility to successfully access the diverse chemistries of Fe/αKG-dependent dioxygenases to expand the biocatalytic toolbox. More information can be found in the Communication by A. Papadopoulou et al.
Highlights
The introduction of a halogen into a molecule’s scaffold can alter its bioactivity or act as a useful synthetic handle for diversification and modification of late-stage synthetic [b] Dr T
The recently discovered non heme iron/αketoglutarate (Fe/αKG) halogenases, e. g., WelO5,[3] WelO5*,[4] Wi-WelO15,[5] AmbO5[6] and BesD,[7] acting on free-standing substrates have broadened the biocatalytic potential of radical halogenation by overcoming the complexity barrier of previously known Fe/αKG halogenases requiring carrier-proteintethered substrates (BarB1 and BarB2,[8] SyrB2,[9] CytC3,[10] CmaB,[11] HctB,[12] CurA,[13] KthP[14])
Fe/αKG halogenases belong to the superfamily of α-ketoglutarate-dependent oxygenases which coordinate the co-factor Fe(II) by two conserved histidine residues, a carboxylate residue and the cofactor α-ketoglutarate in their active site
Summary
The introduction of a halogen into a molecule’s scaffold can alter its bioactivity or act as a useful synthetic handle for diversification and modification of late-stage synthetic [b] Dr T.
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