Investigating Catalase Activity Through Hydrogen Peroxide Decomposition by Bacteria Biofilms in Real Time Using Scanning Electrochemical Microscopy
| Autor: | Anthony J. Patelunas, Douglas Miller, Renaud Cornut, Erwin G. Abucayon, Michele K. Nishiguchi, Neng Ke, Cynthia G. Zoski |
|---|---|
| Přispěvatelé: | Department of Chemistry and Biochemistry, New Mexico State University, Laboratoire Innovation en Chimie des Surfaces et NanoSciences (LICSEN), Nanosciences et Innovation pour les Matériaux, la Biomédecine et l'Energie (ex SIS2M) (NIMBE UMR 3685), Institut Rayonnement Matière de Saclay (IRAMIS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Institut Rayonnement Matière de Saclay (IRAMIS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Department of Biology, Laboratoire Innovation en Chimie des Surfaces et NanoSciences (LICSEN UMR 3685), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut Rayonnement Matière de Saclay (IRAMIS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 2013 |
| Předmět: |
biology
Chemistry Biofilm Analytical chemistry Hydrogen Peroxide [CHIM.MATE]Chemical Sciences/Material chemistry Catalase biology.organism_classification Electrochemistry Aliivibrio fischeri Decomposition Analytical Chemistry Enzyme Activation Scanning electrochemical microscopy chemistry.chemical_compound Computer Systems Biofilms squid euprymna-scolopes hawaiian bobtail squid vibrio-rumoiensis s-1(t) oxidative stress light organ fischeri resistance colonization symbiosis electrode biology.protein Microscopy Electrochemical Scanning Hydrogen peroxide Incubation Bacteria Nuclear chemistry |
| Zdroj: | Analytical Chemistry Analytical Chemistry, American Chemical Society, 2014, 86 (1), pp.498-505. ⟨10.1021/ac402475m⟩ Analytical Chemistry, 2014, 86 (1), pp.498-505. ⟨10.1021/ac402475m⟩ |
| ISSN: | 1520-6882 0003-2700 |
| DOI: | 10.1021/ac402475m |
| Popis: | International audience; Catalase activity through hydrogen peroxide decomposition in a 1 mM bulk solution above Vibrio fischeri (gamma-Protebacteria-Vibrionaceae) bacterial biofilms of either symbiotic or free-living strains was studied in real time by scanning electrochemical microscopy (SECM). The catalase activity, in units of micromoles hydrogen peroxide decomposed per minute over a period of 348 s, was found to vary with incubation time of each biofilm in correlation with the corresponding growth curve of bacteria in liquid culture. Average catalase activity for the same incubation times ranging from 1 to 12 h was found to be 0.28 +/- 0.07 mu mol H2O2/min for the symbiotic biofilms and 0.31 +/- 0.07 mu mol H2O2/min for the free-living biofilms, suggesting similar catalase activity. Calculations based on Comsol Multiphysics simulations in fitting experimental biofilm data indicated that approximately (3 +/- 1) x 10(6) molecules of hydrogen peroxide were decomposed by a single bacterium per second, signifying the presence of a highly active catalase. A 2-fold enhancement in catalase activity was found for both free-living and symbiotic biofilms in response to external hydrogen peroxide concentrations as low as 1 nM in the growth media, implying a similar mechanism in responding to oxidative stress. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|