4 publications
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A Rhodium Complex-Linked β-Barrel Protein as a Hybrid Biocatalyst for Phenylacetylene Polymerization
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Chem. Commun. 2012, 48, 9756, 10.1039/C2CC35165J
Our group recently prepared a hybrid catalyst containing a rhodium complex, Rh(Cp)(cod), with a maleimide moiety at the peripheral position of the Cp ligand. This compound was then inserted into a β-barrel protein scaffold of a mutant of aponitrobindin (Q96C) via a covalent linkage. The hybrid protein is found to act as a polymerization catalyst and preferentially yields trans-poly(phenylacetylene) (PPA), although the rhodium complex without the protein scaffold normally produces cis PPA.
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A Whole Cell E. coli Display Platform for Artificial Metalloenzymes: Poly(phenylacetylene) Production with a Rhodium–Nitrobindin Metalloprotein
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ACS Catal. 2018, 8, 2611-2614, 10.1021/acscatal.7b04369
Whole cell catalysis is, in many cases, a prerequisite for the cost-effective production of chemicals by biotechnological means. Synthetic metal catalysts for bioorthogonal reactions can be inactivated within cells due to abundant thiol derivatives. Here, a cell surface display-based whole cell biohybrid catalyst system (termed ArMt bugs) is reported as a generally applicable platform to unify cost-effective whole cell catalysis with biohybrid catalysis. An inactivated esterase autotransporter is employed to display the nitrobindin protein scaffold with a Rh catalyst on the E. coli surface. Stereoselective polymerization of phenylacetylene yielded a high turnover number (TON) (39 × 106 cell–1) for the ArMt bugs conversion platform.
Metal: RhHost protein: Nitrobindin variant NB4Anchoring strategy: Cystein-maleimideOptimization: ---Notes: Calculated in vivo TON assuming 12800 metalloenzymes per E. coli cell
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Polymerization of Phenylacetylene by Rhodium Complexes within a Discrete Space of apo-Ferritin
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J. Am. Chem. Soc. 2009, 131, 6958-6960, 10.1021/ja901234j
Polymerization reactions of phenylacetylene derivatives are promoted by rhodium complexes within the discrete space of apo-ferritin in aqueous media. The catalytic reaction provides polymers with restricted molecular weight and a narrow molecular weight distribution. These results suggest that protein nanocages have potential for use as various reaction spaces through immobilization of metal catalysts on the interior surfaces of the protein cages.
Metal: RhLigand type: NorbornadieneHost protein: FerritinAnchoring strategy: DativeOptimization: ---Notes: ---
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Rhodium-Complex-Linked Hybrid Biocatalyst: Stereo-Controlled Phenylacetylene Polymerization within an Engineered Protein Cavity
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ChemCatChem 2014, n/a-n/a, 10.1002/cctc.201301055
The incorporation of a Rh complex with a maleimide moiety into the cavity of the nitrobindin β‐barrel scaffold by a covalent linkage at the 96‐position (Cys) provides a hybrid biocatalyst that promotes the polymerization of phenylacetylene. The appropriate structural optimization of the cavity by mutagenesis enhances the stereoselectivity of the polymer with a trans content of 82 % at 25 °C and pH 8.0. The X‐ray crystal structure of one of the hybrid biocatalysts at a resolution of 2.0 Å reveals that the Rh complex is located in the β‐barrel cavity without any perturbation to the total protein structure. Crystal structure analysis and molecular modeling support the fact that the stereoselectivity is enhanced by the effective control of monomer access to the Rh complex within the limited space of the protein cavity.
Metal: RhHost protein: Nitrobindin (Nb)Anchoring strategy: Cystein-maleimideOptimization: GeneticNotes: ---