Despite a well-developed and growing body of work on the directed evolution of hemoproteins, the potential of hemoproteins to catalyze non-natural reactions remains underexplored. This paper reports a new biocatalytic strategy for the one-pot synthesis of unnatural α-amino acids. Engineered variants of dual-function Vitreoscilla hemoglobin were found to efficiently catalyze N–H insertion and C–H sp3

The authors retract this article after attempts to reproduce the work show that the compounds are silyl indenes, not siloxy indenes. Errors were made in high-resolution mass spectrometry analysis, which has been confirmed by a crystal structure of compound 3aa (CCDC 2285656). The alkylation/carbocyclization/Brook rearrangement proposed in the Letter has not been achieved. The original letter was published

A Data Availability Statement is added to include the data underpinning the calculations and photophysics described in this paper. The research data supporting this publication can be accessed at 10.17630/fd1c4863-0606-4595-9c89-f40ef45fef4d. This article has not yet been cited by other publications.

Research in peptide and protein modification originated in the early 20th century with the groundbreaking work of chemists such as Emil Fischer and Robert Robinson. Their contributions were pivotal in elucidating the structure, reactivity, and synthesis of peptides, establishing the fundamental principles that have shaped subsequent advancements. These early explorations not only laid the foundation