Grubbs-Hoveyda catalysts conjugated to a ß-barrel protein: Effect of halide substitution on aqueous olefin metathesis activity.
J Inorg Biochem
; 258: 112616, 2024 Sep.
Article
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| MEDLINE
| ID: mdl-38833874
ABSTRACT
The effect of halide substitution in Grubbs-Hoveyda II catalysts (GHII catalysts) embedded in the engineered ß-barrel protein nitrobindin (NB4exp) on metathesis activity in aqueous media was studied. Maleimide tagged dibromido and diiodido derivates of the GHII catalyst were synthesized and covalently conjugated to NB4exp. The biohybrid catalysts were characterized spectroscopically confirming the structural integrity. When the two chloride substituents at ruthenium center were exchanged against bromide and iodide, the diiodo derivative was found to show significantly higher catalytic activity in ring-closing metathesis of α,ω-diolefins, whereas the dibromido derivative was less efficient when compared with the parent dichlorido catalyst. Using the diiodido catalyst, high turnover numbers of up to 75 were observed for ring-closing metathesis (RCM) yielding unsaturated six- and seven-membered N-heterocycles.
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01-internacional
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MEDLINE
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Revista:
J Inorg Biochem
Año:
2024
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Article
País de afiliación:
Alemania