Proteins and protein-rich biomass as environmentally friendly adsorbents selective for precious metal ions.

Proteins exhibit specific interactions with various metal ions, which play important roles in a living cell. Here, we found that various proteins selectively adsorbed precious metal ions at a wide range of pH values. Studies on protein sequences and on synthesized peptides revealed that a histidine-containing sequence had specific interactions with precious metal ions (Au3+ and Pd2+). We then investigated a few types of protein-rich biomass as adsorbents for precious metal ions. In the presence of various transition metal ions, Au3+ and Pd2+ were also selectively adsorbed onto the biomass tested. The bound precious metal ions were recovered by aqua regia after charring the metal-bound biomass. Finally, we demonstrated the successful recovery of Au3+ and Pd2+ from a metal refining solution and a metal plating waste using the biomass. We propose an environmentally friendly recycling system for precious metal ions using protein-rich biomass.

Inhibitiory effects of gold(III) ions on ribonuclease and deoxyribonuclease.

Inhibitory effects of gold(III) ions (Au(III)) on ribonuclease A (RNase A) and deoxyribonuclease I (DNase I) were investigated at neutral pH. RNase A was completely inhibited by 3 molar equivalents of Au(III) ions. DNase I was inhibited by 10 molar equivalents of Au(III) ions. Stoichiometric analyses suggest that Au(III) ions were coordinated to RNase A molecules. The Au(III)-inhibited RNase A and DNase I were renatured to exhibit 80% and 60% of their intrinsic activity, when the bound Au(III) ions were eliminated from the nucleases by addition of thiourea, which forms a strong complex with gold ions. This suggests that RNase A and DNase I were not oxidized to lose their activity, but reversibly complexed with Au(III) ions to lose their activity. Au(III) ions were probably considered to be bound to histidine and methionine residues in the nucleases, resulting in the inhibition of their activity. CD spectra revealed that the Au(III)-induced inhibition caused a conformational change in RNase A molecules and that the addition of thiourea induced refolding of the Au(III)-inhibited RNase A.