Photocatalytic hydrogen evolution systems constructed in cross-linked porous protein crystals

Abstract

Cross-linked hen egg white lysozyme crystals (CL-HEWL) have been employed as supports to construct heterogeneous catalysts for photocatalytic hydrogen (H2) evolution, where rose bengal (RB) and Pt nanoparticles (PtNPs) acted as a photosensitizer and H2-evolution catalysts, respectively. Single-crystal X-ray structure analyses of the CL-HEWL immobilizing a precursor for PtNPs suggested that a coordination site of the precursor locates in immediate proximity to potential adsorption sites for RB. The accumulation of the components facilitated photo-induced electron transfer, resulting in efficient H2 evolution. These results suggest that porous protein crystals are promising platforms to periodically and rationally accumulate catalytic components by using molecular interactions.

Cross-Linked Crystals of Dirhodium Tetraacetate/RNase A Adduct Can Be Used as Heterogeneous Catalysts

“…22 CLPC-based catalysts can be recycled several times before inactivation. 22 Cross-linked NikA (a nickel binding protein) crystals have been functionalized with Fe-EDTA-like compounds (EDTA = ethylenediaminotetraacetate) and employed as oxidation catalysts for C−C double bond, using O 2 as an oxidant. 23 Despite the tremendous advantages that arise from the metal functionalization of CLPCs, those mentioned above are the only known examples of the use of these systems as catalysts.…”

“…CLPCs catalyzed the transfer hydrogenation reaction better than the metal/protein adduct in solution . CL_HEWL crystals have also been used for growing platinum nanoparticles (from H 2 PtCl 6 ), useful as hydrogen evolution promoters . CLPC-based catalysts can be recycled several times before inactivation .…”

In-Cell Engineering of Protein Crystals with Nanoporous Structures for Promoting Cascade Reactions

“…Recently, nanoporous solid materials from metal–organic frameworks (MOFs), zeolites, silica, DNA, and protein crystals have been reported as useful crystalline scaffolds for the immobilization of enzymes. ,− Such crystalline materials can provide various functions in vitro and in vivo that contribute to the improvement of catalytic activities under harsh conditions and recycling. ,− Protein crystals are among the most interesting of nanoporous materials because they can be genetically modified and because they have diverse types of porous structures and biocompatibility. ,, Engineering of protein crystals has been demonstrated as a useful method for developing various integrated crystalline materials containing metallic compounds, − photo-active molecules, − and artificial solid catalysts. − Notably, the sizes and shapes of nanopores within protein crystals are essential for immobilizing multiple enzymes in a useful strategy for the construction of artificial catalysts for cascade reactions. ,, The engineering of protein crystals can expand the nanopore sizes to enhance the uptake efficiency of foreign molecules. , However, obtaining stable protein crystals with large pore sizes remains challenging.…”

LEAFY protein crystals with a honeycomb structure as a platform for selective preparation of outstanding stable bio-hybrid materials

“…Taking advantage of both the versatility of synthetic materials and the properties of controlled assembly of biomolecules, several biohybrid systems combining either nanoparticles, organic synthetic molecules or metal complexes on or within a protein assembly were reported for applications in various domains such as biocatalysis, nanodevices, medical imaging, drug delivery, diagnosis and therapy. [9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25] Yet, even if it is a field in full expansion, the variety and the number of proteins used remains poorly exploited despite their high potential. This is particularly true for protein crystals that appear to be promising candidates for the design of functional materials since they offer the following advantageous properties: i) a highly ordered monomers arrangements that form a variety of porous structures, ii) a confined and chiral interior space with solvent-filled channels that allows the diffusion of various small functional molecules, iii) a high catalyst loading capacity can be expected due to high molecular concentrations and finally iv) the possibility to design improved biocatalysts guided by the atomic resolution details of crystal structures.…”