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8OQC

Dirhodium tetraacetate/ribonuclease A adduct in the P3221 space group (1 h soaking)

Summary for 8OQC
Entry DOI10.2210/pdb8oqc/pdb
DescriptorRibonuclease pancreatic, tri-(mi2-acetato-(O, O')-diaqua-dirhodium(II, II), FORMIC ACID, ... (6 entities in total)
Functional Keywordsmetal/protein adduct, dirhodium tetraacettate, catalysis, porous material, hydrolase
Biological sourceBos taurus (cattle)
Total number of polymer chains1
Total formula weight14691.26
Authors
Loreto, D.,Merlino, A.,Maity, B.,Ueno, T. (deposition date: 2023-04-12, release date: 2023-06-14, Last modification date: 2024-10-16)
Primary citationLoreto, D.,Maity, B.,Morita, T.,Nakamura, H.,Merlino, A.,Ueno, T.
Cross-Linked Crystals of Dirhodium Tetraacetate/RNase A Adduct Can Be Used as Heterogeneous Catalysts.
Inorg.Chem., 62:7515-7524, 2023
Cited by
PubMed 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 (321 space group) for fixing [Rh(OAc)] and developing a heterogeneous catalyst to perform reactions in an aqueous medium. The structure of the [Rh(OAc)]/RNase A adduct was investigated by X-ray crystallography: the metal complex structure remains unperturbed upon protein binding. Using a number of crystal structures, metal complex accumulation over time, within the RNase A crystals, and structures at variable temperatures were evaluated. We also report the large-scale preparation of microcrystals (∼10-20 μm) of the [Rh(OAc)]/RNase A adduct and cross-linking reaction with glutaraldehyde. The catalytic olefin cyclopropanation reaction and self-coupling of diazo compounds by these cross-linked [Rh(OAc)]/RNase A crystals were demonstrated. The results of this work reveal that these systems can be used as heterogeneous catalysts to promote reactions in aqueous solution. Overall, our findings demonstrate that the dirhodium paddlewheel complexes can be fixed in porous biomolecule crystals, like those of RNase A, to prepare biohybrid materials for catalytic applications.
PubMed: 37144589
DOI: 10.1021/acs.inorgchem.3c00852
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

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건을2025-07-23부터공개중

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