Functioning of quinone acceptors in the reaction center of the green photosynthetic bacterium Chloroflexus aurantiacus.
The photosynthetic reaction centers (RC) of the green bacterium Chloroflexus aurantiacus have been investigated by spectral and electrometrical methods. In these reaction centers, the secondary quinone was found to be reconstituted by the addition of ubiquinone-10. The equilibrium constant of electron transfer between primary (QA) and secondary (QB) quinones was much higher than that in RC of purple bacteria. The QB binding to the protein decreased under alkalinization with apparent pK 8.8. The single flash-induced electric responses were about 200 mV. An additional electrogenic phase due to the QB protonation was observed after the second flash in the presence of exogenous electron donors. The magnitude of this phase was 18% of that related to the primary dipole (P+QA-) formation. Since the C. aurantiacus RC lacks H-subunit, this subunit was not an obligatory component for electrogenic QB protonation.
A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, USSR.
M A
MA
Kutuzov
M D
MD
Mamedov
Semenov AYu
V P
VP
Shinkarev
M I
MI
Verkhovsky
N G
NG
Abdulaev
L A
LA
Drachev
D001419:Bacteria / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008027:Light; D008081:Liposomes / Q000378:metabolism; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism*; D011510:Proteolipids / Q000378:metabolism; D011809:Quinones / Q000378:metabolism*; D013053:Spectrophotometry
D008081:Liposomes; D045322:Photosynthetic Reaction Center Complex Proteins; D011510:Proteolipids; D011809:Quinones; C020485:proteoliposomes