Articolo in rivista, 2020, ENG, 10.1016/j.bioelechem.2020.107456
Borghese, Roberto; Malferrari, Marco; Brucale, Marco; Ortolani, Luca; Franchini, Martina; Rapino, Stefania; Borsetti, Francesca; Zannoni, Davide
Univ Bologna; Univ Bologna; CNR; CNR ISMN; Univ Bologna
Cells of the facultative photosynthetic bacterium Rhodobacter capsulatus exploit the simultaneous presence in the cultural medium of the toxic oxyanion tellurite (TeO32-) and the redox mediator lawsone (2-hydroxy-1,4-naphthoquinone) by reducing tellurite to metal Te-0 nanoprecipitates (TeNPs) outside the cells. Here we have studied the mechanism by which lawsone interacts with metabolically active cells and analysed both structure and composition of the TeNPs collected from the growth medium of phototrophycally grown R. capsulatus. High Resolution Transmission Electron Microscopy (HR-TEM) images and Energy-Dispersive X-ray (EDX) microanalysis of TeNPs showed a central core of polycrystalline tellurium interspersed in an organic matrix with a predominant protein-based composition. The main proteins from Te-0 nanostructures were identified by Liquid Chromatography tandem-Mass Spectrometry and were all correlated with the cell outer membrane composition. The interaction of reduced lawsone with tellurite and with the bacterial cells was probed by Cyclic Voltammetry and Scanning ElectroChemical Microscopy (SECM). We concluded that lawsone is required for the reduction of tellurite to metal Te-0 in a reaction mechanism dependent on reducing equivalents deriving from the cell photosynthetic metabolism. SECM experiments demonstrate that lawsone, by diffusing inside the bacterial cells, is effectively available at the membrane site of the photosynthetic electron transport chain. (C) 2020 Published by Elsevier B.V.
Bioelectrochemistry (Amsterdam) 133
Lawsone, Tellurite, Tellurium nanoprecipitates, Rhodobacter capsulatus, Scanning ElectroChemical Microscopy (SECM)
ID: 449435
Year: 2020
Type: Articolo in rivista
Creation: 2021-03-24 10:39:06.000
Last update: 2021-05-11 10:56:50.000
CNR authors
External IDs
CNR OAI-PMH: oai:it.cnr:prodotti:449435
DOI: 10.1016/j.bioelechem.2020.107456
ISI Web of Science (WOS): 000531827700002