Few-Layer Graphene Sheet-Passivated Porous Silicon Toward Excellent Electrochemical Double-Layer Supercapacitor Electrode.

Few-layer graphene sheet-passivated porous silicon (PSi) as an outstanding electrochemical double-layer supercapacitor electrode was demonstrated. The PSi matrix was formed by electrochemical etching of a doped silicon wafer and was further surface-passivated with few-layer graphene sheets by a Ni-assisted chemical vapor deposition process where a wide range of porous PSi structures, including mesoporous, macroporous, and hybrid porous structures were created during the graphene growth as temperature increases. The microstructural and graphene-passivation effects on the capacitive performance of the PSi were investigated in detail. The hybrid porous PSi electrode, optimized in terms of capacitive performances, achieves a high areal capacitance of 6.21 mF/cm2 at an ultra-high scan rate of 1000 mV/s and an unusual progressing cyclic stability of 131% at 10,000 cycles. Besides mesopores and macropores, micropores were introduced onto the surfaces of the passivating few-layer graphene sheets with a KOH activation process to further increase the functioning surface area of the hierarchical porous PSi electrode, leading to a boost in the areal capacitance by 31.4% up to 8.16 mF/cm2. The present designed hierarchical porous PSi-based supercapacitor proves to be a robust energy storage device for microelectronic applications that require stable high rate capability.

The function of Asp70, Glu77 and Lys79 in the Escherichia coli MutH protein.

The MutH protein, which is part of the Dam-directed mismatch repair system of Escherichia coli, introduces nicks in the unmethylated strand of a hemi-methylated DNA duplex. The latent endonuclease activity of MutH is activated by interaction with MutL, another member of the repair system. The crystal structure of MutH suggested that the active site residues include Asp70, Glu77 and Lys79, which are located at the bottom of a cleft where DNA binding probably occurs. We mutated these residues to alanines and found that the mutant proteins were unable to complement a chromosomal mutH deletion. The purified mutant proteins were able to bind to DNA with a hemi-methylated GATC sequence but had no detectable endonuclease activity with or without MutL. Although the data are consistent with the prediction of a catalytic role for Asp70, Glu77 and Lys79, it cannot be excluded that they are also involved in binding to MutL.