title: Light-induced oxidation-reduction reactions of cytochromes in the green sulfur photosynthetic bacterium Prosthecochloris aesturarii.
abstract: The light-induced oxidation-reduction reactions of cytochromes in intact cells, starved cells, and chlorobium vesicle fractions of the green sulfur photosynthetic bacterium Prosthecochloris aesturarii were studied under anaerobic conditions. On the basis of both kinetic and spectral properties, at least three cytochrome species were found to be involved in the light-induced oxidation-reduction reactions of intact cells. These cytochromes were designated according to the positions of alpha-band maxima as C555 (rapid and slow components) and C552 (intermediate). By comparing the light-minus-dark difference spectra with the reduced-minus-oxidized difference spectra of purified cytochromes of this organism, rapid component C555 and intermediate component C552 are suggested to correspond to the purified cytochromes c-555(550) and c-551.5, respectively. Although the identity of the slow-phase component is uncertain, one possibility is that the slow phase is due to the bound form of c-555(550). In substrate-depleted (starved) cells, only one cytochrome species, C555 remained in the reduced state in the dark and oxidized upon actinic illumination. This corresponds to the rapid C555 component in intact cells. In the case of chlorobium vesicle fractions, one cytochrome species having an alpha-band maximum at 554 nm was oxidized by actinic light. The effects of several inhibitors on the absorbance changes of intact cells were studied. Antimycin A decreased the rate of the dark reduction of rapid C555 component. The complex effects of CCCP (carbonyl cyanide m-chlorophenylhydrazone) on the oxidation-reduction reactions of cytochromes were interpreted as the results of inhibition of the electron donation to oxidized C552 and C555 (slow), and a shift of the dark steady-state redox levels of cytochromes. Based on these findings, it is suggested that the rapid C555 component is located in a cyclic electron transfer pathway. The other two cytochromes, C552 and C555 (slow), may be located in non-cyclic electron transfer pathways and receive electrons from exogenous substrates such as sodium sulfide. A tentative scheme for the electron transfer system in Prosthecochloris aestuarii is presented and its nature is discussed.
mesh_terms: D000968:Antimycin A / Q000494:pharmacology; D001419:Bacteria / Q000187:drug effects / Q000378:metabolism*; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone / Q000494:pharmacology; D003580:Cytochromes / Q000378:metabolism*; D003624:Darkness; D004579:Electron Transport; D007700:Kinetics; D008027:Light; D010084:Oxidation-Reduction; D010788:Photosynthesis; D013053:Spectrophotometry
chemical_list: D003580:Cytochromes; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone; D000968:Antimycin A