Preparation and catalytic reaction of Au/Pd bimetallic nanoparticles in Apo-ferritin

Abstract

We have succeeded in preparing Au/Pd core-shell nanoparticles in apo-ferritin and improving the catalytic reactivity of olefin hydrogenation relative to Pd0 nanoparticles in the cage.

Chemistry at the protein–mineral interface in L-ferritin assists the assembly of a functional (μ 3 -oxo)Tris[(μ 2 -peroxo)] triiron(III) cluster

“…Despite several structures of HuLf and HoLf, ferritins have been determined in complex with different metal ions (13,16,19), and no structural observation of iron binding to the mineralization site has been reported in the literature, the only iron(III) ion reported in HoLf being bound to an exogenous ligand (20). To the goal of obtaining insights into the ferritin biomineralization process, we have obtained the crystal structures of the iron-loaded HuLf and HoLf cages.…”

MnO2 Submicroparticles from Chinese Brush and Their Application in Treatment of Methylene Blue Contaminated Wastewater

“…Biotemplates like organisms (butterfly wing, 2 hair, 3 wood fiber 4,5 and pollen 6 ), microorganisms (bacteria, 7,8 fungus, 9,10 and viruses 11 ) and biological macromolecules (DNA, [12][13][14] RNA, 15 proteins, [16][17][18][19] and polysaccharides 20 ) were reported to prepare inorganic materials. Among these templates, proteins have gained more popularity by researchers, 21 ranging from ferritin, [22][23][24][25] bovine serum albumin (BSA) [26][27][28][29][30][31] to collagen [32][33][34] . However, proteins from natural extracted or artificial synthetic are difficult to obtain and thus cost a lot.…”

Elucidation of Metal‐Ion Accumulation Induced by Hydrogen Bonds on Protein Surfaces by Using Porous Lysozyme Crystals Containing RhIIIIons as the Model Surfaces

“…A similar observation was reported for ferritin containing Au III ions. [24] Binding Site B: There have been no previous reports of metal ions binding to this site, which is located on a narrower pore (Figure 3 b). Two Rh atoms, Rh4 and Rh5, coordinate with…”

“…[16,29] Many crystal structures of ferritins (Frs), which include various metal ions have been reported with the aim of elucidating the metal accumulation process that occurs within the cage. [20][21][22][23][24] We have reported on the accumulation process of Pd II ions on the interior surface of apo-ferritin (apo-Fr) by investigating a series of X-ray crystal structures of apo-Fr that contain different amounts of Pd II ions. The results indicate that the number of Pd II ions accumulated by apo-Fr increases when different coordination structures are adopted at the specific binding sites on the interior surface of apo-Fr.…”