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

Jankowski, U; Merroun, ML; Selenska-Pobell, S; Fahmy, K

HERO ID

1438587

Reference Type

Journal Article

Year

2010

HERO ID 1438587
In Press No
Year 2010
Title S-Layer protein from Lysinibacillus sphaericus JG-A12 as matrix for Au-III sorption and Au-nanoparticle formation
Authors Jankowski, U; Merroun, ML; Selenska-Pobell, S; Fahmy, K
Journal Spectroscopy
Volume 24
Issue 1-2
Page Numbers 177-181
Abstract 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 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 similar to 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.
Doi 10.3233/SPE-2010-0408
Wosid WOS:000278029800026
Is Certified Translation No
Dupe Override No
Comments Source: Web of Science WOS:000278029800026
Is Public Yes
Keyword Bioremediation; biotemplate; heavy metal binding; infrared spectroscopy; X-ray absorption