ArticleInorganic chemistry2023
Cross-Linked Crystals of Dirhodium Tetraacetate/RNase A Adduct Can Be Used as Heterogeneous Catalysts.
Article in Inorganic chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 8 citations in OpenAlex.
- Coordination of a Dirhodium(II) Center to Methionine and Cysteine Side Chains: Evidence from X-Ray Structure of the Adduct Formed by Dirhodium Tetraacetate with a C-Phycocyanin.International journal of molecular sciences · 2025Article
- Dirhodium Tetraacetate Binding to Lysozyme at Body Temperature.International journal of molecular sciences · 2025Article
- Real-time observation of a metal complex-driven reaction intermediate using a porous protein crystal and serial femtosecond crystallography.Nature communications · 2024Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Due to their unique coordination structure, dirhodium paddlewheel complexes are of interest in several research fields, like medicinal chemistry, catalysis, etc. Previously, these complexes were conjugated to proteins and peptides for developing artificial metalloenzymes as homogeneous catalysts. Fixation of dirhodium complexes into protein crystals is interesting to develop heterogeneous catalysts. Porous solvent channels present in protein crystals can benefit the activity by increasing the probability of substrate collisions at the catalytic Rh binding sites. Toward this goal, the present work describes the use of bovine pancreatic ribonuclease (RNase A) crystals with a pore size of 4 nm (
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