In photosynthetic green sulfur bacteria excitation energy is transferred from large bacteriochlorophyll (BChl) c chlorosome antennas via small BChl a antennas to the reaction centers which then transfer electrons from cytochrome c to low-potential iron-sulfur proteins. Under oxidizing conditions a reversible mechanism is activated in the chlorosomes which quenches excited BChl c. We used flash-induced cytochrome c oxidation to investigate the effect of this quenching on photosynthetic electron transfer in whole cells of Chlorobium tepidum. The extent of cytochrome c photooxidation under aerobic conditions decreased to approx. 3% of that under anaerobic conditions when BChl c was excited under light-limiting conditions. Photooxidation obtained by excitation of BChl a was similar under aerobic and anaerobic conditions. We interpret this drastic decrease in energy transfer from BChl c to the reaction center as a consequence of the quenching mechanism which is activated by O2. This reversible uncoupling of the chlorosome antenna might prevent formation of toxic reactive oxygen species from photosynthetically produced reductants under aerobic conditions. The green filamentous bacterium Chloroflexus aurantiacus also contains chlorosomes but energy transfer from the BChl c and BChl a antennas to the reaction center in this species was not affected by O2.