9FNR

Artificial metalloenzyme with a nickel-based 1,10-phenanthroline cofactor and streptavidin S112V mutant

This is a non-PDB format compatible entry.

Summary for 9FNR

• Entry DOI: 10.2210/pdb9fnr/pdb
• Related: 9FFJ
• Descriptor: Streptavidin, N-methyl-N-[(4,4,6,6-tetrahydroxy-4,6-dioxido-1,3,3a,5,6a-tetrahydrothien[3,4-d]imidazol-4-ium-2-yl)methyl]-5-(2,4,4-trihydroxy-2-keto-3,3a,5,6-tetrahydro-1H-thien[3,4-d]imidazol-4-ium-6-yl, SULFATE ION, ... (4 entities in total)
• Functional Keywords: artificial metalloenzyme, nickel, metal binding protein
• Biological source: Streptomyces avidinii
• Total number of polymer chains: 1
• Total formula weight: 17251.42

Authors

Lau, K.,Wang, W.,Pojer, F.,Larabi, A. (deposition date: 2024-06-10, release date: 2025-01-15, Last modification date: 2025-02-26)

Primary citation

Wang, W.,Tachibana, R.,Zhang, K.,Lau, K.,Pojer, F.,Ward, T.R.,Hu, X.
Artificial Metalloenzymes with Two Catalytic Cofactors for Tandem Abiotic Transformations.
Angew.Chem.Int.Ed.Engl., 64:e202422783-e202422783, 2025

PubMed Abstract: Artificial metalloenzymes (ArMs) enable the integration of abiotic cofactors within a native protein scaffold, allowing for non-natural catalytic activities. Previous ArMs, however, have primarily relied on single cofactor systems, limiting them to only one catalytic function. Here we present an approach to construct ArMs embedding two catalytic cofactors based on the biotin-streptavidin technology. By incorporating multiple catalytic cofactors into the four binding sites of streptavidin, we engineered programmable ArMs for tandem abiotic transformations including an enantioselective formal C-H hydroxylation and a photooxidation-Michael addition. This work thus outlines a promising strategy for the development of ArMs embedding multiple cofactors.

PubMed: 39760306
DOI: 10.1002/anie.202422783

Experimental method

X-RAY DIFFRACTION (1.64 Å)