Site-selective enzymatic C‒H amidation for synthesis of diverse lactams

03 January 2020, Version 2
This content is a preprint and has not undergone peer review at the time of posting.


Please note that this work has been retracted by the authors.

After publication of the Report “Site-selective enzymatic C‒H amidation for synthesis of diverse lactams” in Science (1, also linked in metadata), efforts to reproduce the work showed that the enzymes do not catalyze the reactions with the activities and selectivities claimed. Careful examination of the first author’s lab notebook then revealed missing contemporaneous entries and raw data for key experiments. The authors therefore have retracted the article from Science and are now retracting the preprint from ChemRxiv. The original paper can be accessed by selecting “Version 1” of the preprint below, or by accessing

Inha Cho, Zhi-Jun Jia, Frances H. Arnold*

Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.

*Corresponding author. Email: [email protected]


1. I. Cho, Z.-J. Jia, F. H. Arnold, Science 364, 575 (2019). DOI: 10.1126/science.aaw9068


Directed evolution of cytochrome P450 enzymes fine-tunes site selectivity of new-to-nature C‒H amidation for modular, sustainable and scalable preparation of enantio-enriched β-, γ- and δ-lactams.


C‒H Amidation
biocatalysis strategies
Cytochrome P450s
lactam ring


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