Abstract
The radical pair state P +.865 Q −.A (P865: primary donor, QA: quinone acceptor) in Zn-substituted bacterial reaction centers is investigated using transient and pulsed EPR spectroscopy. For photoexcited samples not frozen in the dark but under continuous illumination, a prolonged lifetime of this radical pair state is observed in agreement with previous studies using time resolved optical spectroscopy. The transient EPR spectra revealed neither a different orientation of the quinone acceptor anion nor a change of itsg-anisotropy in the sample frozen in the charge separated state as compared with that frozen in the dark. The latter finding indicates a similar hydrogen bonding situation for Q −.A in both samples. Changes observed in the transient EPR spectra are interpreted as result of contributions from spin-polarized Q −.A which was generated in part of the sample while freezing under illumination. From the out-of-phase echo modulation pattern observed in the pulsed EPR measurements, it follows that the distance between P +.865 and Q −.A is the same in dark frozen samples and in those frozen under continuous illuminaton. This is in contrast to the model suggested by Kleinfeld D., Okamura M.Y., Feher G.: Biochemistry23, 5780 (1984), in which an increased distance and a larger distribution of distances was suggested for samples frozen under illumination. The prolonged lifetime of the radical pair P +.865 Q −.A is discussed in terms of differences in the relaxation behaviour of the protein.
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Dedicated to Harry Kurreck on the occasion of his 65th birthday
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Zech, S.G., Bittl, R., Gardiner, A.T. et al. Transient and pulsed EPR spectroscopy on the radical pair state P +.865 Q −.A to study light-induced changes in bacterial reaction centers. Appl. Magn. Reson. 13, 517–529 (1997). https://doi.org/10.1007/BF03162224
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DOI: https://doi.org/10.1007/BF03162224