Formation of charge separated state P+OA- and triplet state 3P at low temperature in Rhodobacter sphaeroides (R-26) reaction centers in which bacteriopheophytin a is replaced by plant pheophytin a.
Low temperature optical and photochemical properties of Rhodobacter sphaeroides (R-26) reaction centers, in which bacteriopheophytin a has been replaced by plant pheophytin a, are reported. Modified reaction centers preserve the ability for photoinduced electron transfer from the primary electron donor P to the primary quinone acceptor QA at 80K. The triplet state ESR signal of modified reaction centers with prereduced QA at 10K shows an electron spin polarization pattern and ZFS parameters analogous to those for the triplet state 3P in non-treated reaction centers. It was found that at low temperature both P+QA- and 3P states are formed via a precursor radical pair P+I- in which I is the introduced plant pheophytin molecule. This shows that acceptor systems of bacterial and plant (photosystem II) reaction centers are mutually replacable in structural and functional aspects.
Shkuropatov Aya
Institute of Soil Science and Photosynthesis, Russian Academy of Sciences, Pushchino, Moscow Region.
Proskuryakov
I I
II
Shkuropatova
V A
VA
Zvereva
M G
MG
Shuvalov
V A
VA
D002942:Circular Dichroism; D004578:Electron Spin Resonance Spectroscopy; D004579:Electron Transport; D010674:Pheophytins / Q000378:metabolism*; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism*; D010944:Plants / Q000737:chemistry; D012242:Rhodobacter sphaeroides / Q000737:chemistry / Q000378:metabolism*; D013053:Spectrophotometry
D010674:Pheophytins; D045322:Photosynthetic Reaction Center Complex Proteins; C006678:bacteriopheophytin; C061694:pheophytin a