Quinone exchange at the A{sub 1} site in photosystem I [PSI]
- Argonne National Lab., IL (United States)
- Brown Univ., Providence, RI (United States)
Quinones play an essential role in light-induced electron transport in photosynthetic reaction centers (RC). Study of quinone binding within the protein matrix of the RC is a focal point of understanding the biological optimization of photosynthesis. In plant and cyanobacterial PSI, phylloquinone (K{sub 1}) is believed to be the secondary electron acceptor, A{sub 1}, similar to Q{sub a} in the purple bacterial RC. Photoinduced electron transfer is initiated by reduction of the electron acceptor (A{sub 0}), a chlorophyll species, by the photoexcited primary donor *P{sub 700}. A{sub 1} acts as a transient redox intermediate between A{sub 0} and the iron-sulfur centers (FeS). We have examined the characteristic PSI electron spin polarized (ESP) electron paramagnetic resonance (EPR) signal as a marker of the interacting radical pairs developed during electron transfer.
- Research Organization:
- Argonne National Lab., IL (United States)
- Sponsoring Organization:
- USDOE, Washington, DC (United States)
- DOE Contract Number:
- W-31109-ENG-38
- OSTI ID:
- 207425
- Report Number(s):
- ANL/CHM/CP--86354; CONF-9508202--6; ON: DE96005232
- Country of Publication:
- United States
- Language:
- English
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