4.4 Article

C-H Amination via Nitrene Transfer Catalyzed by Mononuclear Non-Heme Iron-Dependent Enzymes

Journal

CHEMBIOCHEM
Volume 21, Issue 14, Pages 1981-1987

Publisher

WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201900783

Keywords

non-heme iron-dependent oxidases; Rieske diooxygenases; nitrene transfer; C-H amination; protein engineering

Funding

  1. U.S. National Science Foundation [CHE-0840410, CHE-0946653, CHE-1609550, CHE-1834390]
  2. CSIC-UdelaR [INI-1828]
  3. Agencia Nacional de Investigacion e Innovacion (ANII - Uruguay) [FCE 103485]
  4. PhosAgro/UNESCO/IUPAC Partnership in Green Chemistry for Life
  5. CAP-UdelaR
  6. PEDECIBA

Ask authors/readers for more resources

Expanding the reaction scope of natural metalloenzymes can provide new opportunities for biocatalysis. Mononuclear non-heme iron-dependent enzymes represent a large class of biological catalysts involved in the biosynthesis of natural products and catabolism of xenobiotics, among other processes. Here, we report that several members of this enzyme family, including Rieske dioxygenases as well as alpha-ketoglutarate-dependent dioxygenases and halogenases, are able to catalyze the intramolecular C-H amination of a sulfonyl azide substrate, thereby exhibiting a promiscuous nitrene transfer reactivity. One of these enzymes, naphthalene dioxygenase (NDO), was further engineered resulting in several active site variants that function as C-H aminases. Furthermore, this enzyme could be applied to execute this non-native transformation on a gram scale in a bioreactor, thus demonstrating its potential for synthetic applications. These studies highlight the functional versatility of non-heme iron-dependent enzymes and pave the way to their further investigation and development as promising biocatalysts for non-native metal-catalyzed transformations.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.4
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available