S-Layer protein from Lysinibacillus sphaericus JG-A12 as matrix for Au ~(III) sorption and Au-nanoparticle formation

摘要

The strain Lysinibacillus sphaericus JG-A12, isolated from the uranium mining site at Haberland, Saxony (Germany) selectively and reversibly accumulates radionuclides and toxic metals. Metal binding occurs to its surface layer (S-layer) surrounding the cells. Here, we have studied by Fourier-transform infrared (FTIR) spectroscopy the protein structure and stability as a function of Au~(III) binding and the subsequent reductively induced formation of Au-nanoclusters. Similar to previously studied complexes with Pd~(II), Au-treated S-layers become resistant to acid denaturation evidenced by little response of their amide I absorption frequency. However, the strong effect of Pd~(II) exerted on the side chain carboxylate IR absorption intensity is not observed with gold. Particularly after reduction, the carboxyl absorption responds little to acidification and a fraction appears to be protonated already at neutral pH. We ascribe this to a hydrophobic environment of the carboxyl groups after formation of Au-nanoclusters. EXAFS spectra agree with the metallic Au-Au distance but the reduced coordination number indicates that the Au-nanoclusters do not exceed ～ 2 nm. Thus, the S-layer of L. sphaericus JG-A12 provides a biotemplate for efficient Au-nanocluster formation in an acid-resistant matrix and independently of cysteins.