Optimizing the Electron Transfer Reactions at the Cathode of Microbial Fuel Cells.

摘要

We exploited a novel spectrophotometer where the cuvette is a reflecting cavity completely filled with an absorbing suspension of live, intact bacteria to monitor the in situ absorbance changes in bacteria as they respired aerobically on soluble ferrous ions. Our prior observations suggested the following hypothesis: acidophilic bacteria that belong to different phyla express different types of electron transfer proteins to respire on extracellular iron. We tested this hypothesis using six different organisms that represented each of the six phyla of microorganisms that respire aerobically on iron. Each of these six organisms expressed spectrally different biomolecules that were redox-active during aerobic respiration on iron. In all six cases, compelling kinetic evidence was collected to indicate that the biomolecules in question were obligatory intermediates in their respective respiratory chains. Additional experiments with intact Acidithiobacillus ferrooxidans revealed that the crowded electron transport proteins in this organism s periplasm constituted a semi-conducting medium where the network of protein interactions functioned in a concerted fashion as a single ensemble. Thus the molecular oxygen-dependent oxidation of the multi-center respiratory chain occurred with a single macroscopic rate constant, regardless of the proteins individual redox potentials or their putative positions in the aerobic iron respiratory chain.