muramidase has been researched along with acetophenone* in 1 studies
1 other study(ies) available for muramidase and acetophenone
Article | Year |
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Porous protein crystals as catalytic vessels for organometallic complexes.
Porous protein crystals, which are protein assemblies in the solid state, have been engineered to form catalytic vessels by the incorporation of organometallic complexes. Ruthenium complexes in cross-linked porous hen egg white lysozyme (HEWL) crystals catalyzed the enantioselective hydrogen-transfer reduction of acetophenone derivatives. The crystals accelerated the catalytic reaction and gave different enantiomers based on the crystal form (tetragonal or orthorhombic). This method represents a new approach for the construction of bioinorganic catalysts from protein crystals. Topics: Acetophenones; Catalysis; Crystallization; Molecular Structure; Muramidase; Organometallic Compounds; Protein Conformation; Proteins; Ruthenium | 2014 |