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8P5Z

Artificial transfer hydrogenase with a Mn-5 cofactor and Streptavidin S112Y-K121M mutant

Summary for 8P5Z
Entry DOI10.2210/pdb8p5z/pdb
DescriptorStreptavidin, 5-[(3~{a}~{S},4~{S},6~{a}~{R})-2-oxidanylidene-1,3,3~{a},4,6,6~{a}-hexahydrothieno[3,4-d]imidazol-4-yl]-~{N}-[2-[(5-methylpyridin-2-yl)methylamino]ethyl]pentanamide, MANGANESE (II) ION, ... (6 entities in total)
Functional Keywordsartificial meatlloenzyme, transfer hydrogenase, manganese, metal binding protein
Biological sourceStreptomyces avidinii
Total number of polymer chains4
Total formula weight68790.10
Authors
Lau, K.,Wang, W.,Pojer, F.,Larabi, A. (deposition date: 2023-05-24, release date: 2023-09-13, Last modification date: 2023-10-25)
Primary citationWang, W.,Tachibana, R.,Zou, Z.,Chen, D.,Zhang, X.,Lau, K.,Pojer, F.,Ward, T.R.,Hu, X.
Manganese Transfer Hydrogenases Based on the Biotin-Streptavidin Technology.
Angew.Chem.Int.Ed.Engl., 62:e202311896-e202311896, 2023
Cited by
PubMed Abstract: Artificial (transfer) hydrogenases have been developed for organic synthesis, but they rely on precious metals. Native hydrogenases use Earth-abundant metals, but these cannot be applied for organic synthesis due, in part, to their substrate specificity. Herein, we report the design and development of manganese transfer hydrogenases based on the biotin-streptavidin technology. By incorporating bio-mimetic Mn(I) complexes into the binding cavity of streptavidin, and through chemo-genetic optimization, we have obtained artificial enzymes that hydrogenate ketones with nearly quantitative yield and up to 98 % enantiomeric excess (ee). These enzymes exhibit broad substrate scope and high functional-group tolerance. According to QM/MM calculations and X-ray crystallography, the S112Y mutation, combined with the appropriate chemical structure of the Mn cofactor plays a critical role in the reactivity and enantioselectivity of the artificial metalloenzyme (ArMs). Our work highlights the potential of ArMs incorporating base-meal cofactors for enantioselective organic synthesis.
PubMed: 37671593
DOI: 10.1002/anie.202311896
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.56 Å)
Structure validation

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