Photoinduced cyclic electron transfer in Rhodocyclus tenuis cells: participation of HiPIP or cyt c8 depending on the ambient redox potential.
We demonstrate the participation of a cytochrome c8 and a high-potential iron-sulfur protein (HiPIP) in the photoinduced electron transfer in whole cells of Rhodocyclus tenuis depending on the redox state or background continuous illumination. At high redox potentials (above 350 mV) or under a strong background illumination (5 W m-2), the cytochrome c8 acts as the physiological electron donor to the photo-oxidized high-potential hemes of the tetraheme cytochrome bound to the reaction center. For redox potentials ranging from 200 to 310 mV or under weak background illumination (1. 25 W m-2), the electron carrier is the HiPIP. The electron transfer between cyt c8 and HiPIP and the tetraheme cytochrome has half-times of 300 and 480 micros, respectively. A slow electrogenic phase of the membrane potential is linked to their rereduction. This phase is sensitive to a specific inhibitor of the cyt bc1 complex, indicating involvement of cyt c8 and HiPIP in the photoinduced cyclic electron transfer at these two redox conditions.
Menin
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L
C.E.A., DEVM-LBC, C.E.A. Cadarache, Saint-Paul-lez-Durance, France.
Schoepp
B
B
Parot
P
P
Verméglio
A
A
D000042:Absorption; D001426:Bacterial Proteins; D003574:Cytochrome c Group / Q000378:metabolism*; D004579:Electron Transport; D014450:Electron Transport Complex III / Q000378:metabolism / Q000502:physiology; D007506:Iron-Sulfur Proteins / Q000378:metabolism*; D007834:Lasers; D010084:Oxidation-Reduction; D010777:Photochemistry; D012245:Rhodospirillales / Q000166:cytology / Q000201:enzymology* / Q000378:metabolism*
D001426:Bacterial Proteins; D003574:Cytochrome c Group; D007506:Iron-Sulfur Proteins; C017167:cytochrome C(551); D014450:Electron Transport Complex III