ATR-FTIR Spectroscopy Reveals Bond Formation During Bacterial Adhesion to Iron Oxide

• Published in: Langmuir 2006-09, Vol.22 (20), p.8492-8500
• Main Authors: Parikh, Sanjai J, Chorover, Jon
• Format: Article
• Language: English
• Subjects: Adsorption; Bacillus subtilis; Bacteria - chemistry; Bacteria - ultrastructure; Bacterial Adhesion; Chemistry; Exact sciences and technology; Ferric Compounds - chemistry; General and physical chemistry; Pseudomonas aeruginosa; Selenium Compounds - chemistry; Shewanella oneidensis; Spectroscopy, Fourier Transform Infrared; Zinc Compounds - chemistry
• ISSN: 0743-7463; 1520-5827
• DOI: 10.1021/la061359p

The contribution of various bacterial surface functional groups to adhesion at hematite and ZnSe surfaces was examined using attenuated total reflectance (ATR) Fourier transform infrared (FTIR) spectroscopy. When live Shewanella oneidensis, Pseudomonas aeruginosa, and Bacillus subtilis cells were introduced to a horizontal hematite (α-Fe2O3)-coated internal reflection element (IRE), FTIR peaks emerged corresponding to bacterial phosphate group binding. These IR peaks were not observed when bacteria were introduced to the uncoated ZnSe IRE. When cells were added to colloidal suspensions of α-Fe2O3 at pH 7, spectra included peaks corresponding to P−OFe and ν(COOH), the latter being attributed to bridging of carboxylate at mineral surface OH groups. Selected model organic compounds with P-containing functionalities (phenylphosphonic acid [PPA], adenosine 5‘-monophosphate [AMP], 2‘-deoxyadenyl(3‘→5‘)-2‘-deoxyadenosine [DADA], and deoxyribonucleic acid [DNA]) produce spectra with similar peaks corresponding to P−OFe when adsorbed to α-Fe2O3. The data indicate that both terminal phosphate/phosphonate and phosphodiester groups, either exuded from the cell or present as surface biomolecules, are involved in bacterial adhesion to Fe-oxides through formation of innersphere Fe-phosphate/phosphonate complexes.