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- W2013529250 abstract "Photosystem I (PS I) contains two symmetric branches of electron transfer cofactors. In both the A- and B-branches, the phylloquinone in the A(1) site is pi-stacked with a tryptophan residue and is H-bonded to the backbone nitrogen of a leucine residue. In this work, we use optical and electron paramagnetic resonance (EPR) spectroscopies to investigate cyanobacterial PS I complexes, where these tryptophan residues are changed to phenylalanine. The time-resolved optical data show that backward electron transfer from the terminal electron acceptors to P(700) (.+) is affected in the A- and B-branch mutants, both at ambient and cryogenic temperatures. These results suggest that the quinones in both branches take part in electron transport at all temperatures. The electron-nuclear double resonance (ENDOR) spectra of the spin-correlated radical pair P(700) (.+)A(1) (.-) and the photoaccumulated radical anion A(1) (.-), recorded at cryogenic temperature, allowed the identification of characteristic resonances belonging to protons of the methyl group, some of the ring protons and the proton hydrogen-bonded to phylloquinone in the wild type and both mutants. Significant changes in PS I isolated from the A-branch mutant are detected, while PS I isolated from the B-branch mutant shows the spectral characteristics of wild-type PS I. A possible short-lived B-branch radical pair cannot be detected by EPR due to the available time resolution; therefore, only the A-branch quinone is observed under conditions typically employed for EPR and ENDOR spectroscopies." @default.
- W2013529250 created "2016-06-24" @default.
- W2013529250 creator A5017223449 @default.
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- W2013529250 date "2009-12-31" @default.
- W2013529250 modified "2023-09-27" @default.
- W2013529250 title "Investigation of the Stationary and Transient A 1 ·− Radical in Trp → Phe Mutants of Photosystem I" @default.
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- W2013529250 doi "https://doi.org/10.1007/s00723-009-0112-5" @default.
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