Myoglobin-Catalyzed Azide Reduction Proceeds via an Anionic Metal Amide Intermediate.

ABSTRACT: Nitrene transfer reactions catalyzed by heme proteins have broad potential for the stereoselective formation of carbon-nitrogen bonds. However, competition between productive nitrene transfer and the undesirable reduction of nitrene precursors limits the broad implementation of such biocatalytic methods. Here, we investigated the reduction of azides by the model heme protein myoglobin to gain mechanistic insights into the factors that control the fate of key reaction intermediates. In this system, the reaction proceeds via a proposed nitrene intermediate that is rapidly reduced and protonated to give a reactive ferrous amide species, which we characterized by UV/vis and Mössbauer spectroscopies, quantum mechanical calculations, and X-ray crystallography. Rate-limiting protonation of the fe

SUBMITTER: Tinzl M 

PROVIDER: S-EPMC10811658 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature