Analysis of the electron transfer from Pheo- to QA in PS II membrane fragments from spinach by time resolved 325 nm absorption changes in the picosecond domain.
Absorption changes at 325 nm (delta A325) induced by 15 ps laser flashes (lambda = 650 nm) in PS II membrane fragments were measured with picosecond time-resolution. In samples with the reaction centers (RCs) kept in the open state (P I QA) the signals are characterized by a very fast rise (not resolvable by our equipment) followed by only small changes within our time window of 1.6 ns. In the closed state (PI QA-) of the reaction center the signal decays with an average half-life time of about 250 ps. It is shown that under our excitation conditions (E = 2 x 10(14) photons/cm2 per pulse) subtraction of the absorption changes in closed RCs (delta A closed 325) from those in open RCs (delta A open 325) leads to a difference signal which is dominated by the reduction kinetics of QA. From the rise kinetics of this signal and by comparison with data in the literature it is inferred that QA becomes reduced by direct electron transfer from Pheo- with a time constant of about 350 +/- 100 ps.
Eckert
H J
HJ
Max-Volmer-Institut für Biophysikalische und Physikalische Chemie, Berlin, Germany.
Wiese
N
N
Bernarding
J
J
Eichler
H J
HJ
Renger
G
G
D002474:Cell-Free System; D002734:Chlorophyll / Q000031:analogs & derivatives* / Q000502:physiology*; D004579:Electron Transport; D066298:In Vitro Techniques; D007700:Kinetics; D045342:Light-Harvesting Protein Complexes; D010084:Oxidation-Reduction; D010674:Pheophytins / Q000502:physiology*; D045322:Photosynthetic Reaction Center Complex Proteins; D010940:Plant Proteins / Q000502:physiology*; D010944:Plants; D010971:Plastoquinone / Q000502:physiology*; D011809:Quinones / Q000502:physiology*
D045342:Light-Harvesting Protein Complexes; D010674:Pheophytins; D045322:Photosynthetic Reaction Center Complex Proteins; D010940:Plant Proteins; D011809:Quinones; D002734:Chlorophyll; D010971:Plastoquinone