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ortho–para-Directing Deactivators: Halogens

ortho–para-Directing Deactivators: Halogens

Halogens are ortho–para directors. They are more electronegative than carbon. Therefore, as ring substituents, they can withdraw electrons through the inductive effect and deactivate the aromatic ring towards electrophilic substitution. Halogens also have an electron-donating resonance effect on the ring, which influences the orientation of the incoming electrophile. If an electrophile attacks at the ortho or the para position, the halogen donates electrons and stabilizes the intermediate...

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Updated: Feb 21, 2026

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry

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Published on: March 18, 2012

Understanding Flavin-Dependent Halogenase Reactivity via Substrate Activity Profiling.

Mary C Andorfer¹, Jonathan E Grob², Christine E Hajdin²

¹Department of Chemistry, University of Chicago, Chicago, IL 60637.

|October 10, 2017

Summary

This summary is machine-generated.

Four native and four engineered formaldehyde dehydrogenases (FDHs) were studied for their activity on arenes. Findings reveal FDH enzymes can halogenate diverse substrates, with binding influencing selectivity.

Keywords:

C-H functionalization biocatalysis flavin halogenase site selective

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Area of Science:

Biocatalysis
Enzyme Engineering
Organic Chemistry

Background:

Formaldehyde dehydrogenases (FDHs) are enzymes with potential applications in organic synthesis.
Understanding FDH substrate specificity is crucial for expanding their synthetic utility.
Previous studies recognized a limited range of FDH substrates.

Purpose of the Study:

To profile the substrate activity of native and engineered FDHs on a diverse set of arenes.
To elucidate the impact of substrate properties (class, substitution, electronics, binding) on FDH activity and selectivity.
To establish trends in FDH reactivity for improved enzyme engineering and application.

Main Methods:

Enzyme activity assays using four native and four engineered FDH variants.
Testing on 93 low molecular weight arene substrates.
Computational docking simulations to analyze enzyme-substrate interactions.

Main Results:

FDHs exhibited broader substrate activity than previously known, halogenating a wide range of arenes.
Significant variations in substrate specificity and selectivity were observed among the FDH variants.
Electronic activation and substrate binding were identified as key factors influencing halogenation conversion.
Docking simulations indicated that substrate binding can overcome electronic effects, even for non-native compounds.

Conclusions:

FDH enzymes possess a wider substrate scope than previously appreciated.
Enzyme engineering can modulate FDH selectivity for specific substrate classes.
Understanding the interplay between electronic effects and substrate binding is key to predicting and controlling FDH reactivity.
These insights provide a foundation for utilizing FDHs in tailored organic synthesis applications.