Johnson TW et al (2001) Recruitment of a foreign quinone into the A1 site of photosystem I: in vivo replacement of plastoquinone-9 by media-supplemented naphtoquinones in phylloquinone biosynthetic pathway mutants of Synechocystis sp. Genetic and physiological characterization of phylloquinone biosynthetic pathway mutants in Synechocystis sp. Johnson TW et al (2000) Recruitment of a foreign quinone into the A1 site of photosystem I: I. Inoue K, Fujii T, Yokoyama E, Matsuura K, Hiyama T, Sakurai H (1989) The photoinhibition site of photosystem I in isolated chloroplasts under extremely reducing conditions.
2: mutations near the P700 reaction center chlorophylls provide new insight into the nature of the primary electron donor. Holzwarth AR, Müller MG, Niklas J, Lubitz W (2006) Ultrafast transient absorption studies on photosystem I reaction centers from Chlamydomonas reinhardtii. Hastings G, Bandaranayake KMP, Carrion E (2008) Time-resolved FTIR difference spectroscopy in combination with specific isotope labeling for the study of A(1), the secondary electron acceptor in photosystem 1. Hastings G (2015) Vibrational spectroscopy of photosystem I. Guergova-Kuras M, Boudreaux B, Joliot A, Joliot P, Redding K (2001) Evidence for two active branches for electron transfer in photosystem I. Golbeck JH, Parrett KG, Mehari T, Jones KL, Brand JJ (1988) Isolation of the intact photosystem I reaction center core containing P700 and iron-sulfur center FX. Biochim Biophys Acta 1318:322–373īrettel K, Leibl W (2001) Electron transfer in photosystem I. Biochemistry 38:11585–11592īrettel K (1997) Electron transfer and arrangement of the redox cofactors in photosystem I.
Biochemistry 45:12733–12740īreton J, Nabedryk E, Leibl W (1999) FTIR study of the primary electron donor of photosystem I (P700) revealing delocalization of the charge in P700 + and localization of the triplet character in 3P700. These results and conclusions resolve discrepancies between results from previous low-temperature FTIR and EPR studies on similar PSI samples with PQ incorporated.īandaranayake KM, Wang R, Johnson TW, Hastings G (2006) Time-resolved FTIR difference spectroscopy for the study of photosystem I particles with plastoquinone-9 occupying the A1 binding site. The benzoquinone protonation mechanism likely involves nearby water molecules but does not involve the terminal iron–sulfur clusters F A and F B. If samples are subjected to repetitive flash illumination at room temperature prior to cooling, however, the time-resolved FTIR difference spectra at 77 K display contributions typical of the P700 triplet state ( 3P700), indicating a loss of functionality of the incorporated benzoquinones, that occurs because of double protonation of the incorporated benzoquinones. If PSI samples are cooled in the dark to 77 K, the incorporated benzoquinones are shown to be functional, allowing the production of time-resolved (P700 +A 1 −−P700A 1) FTIR difference spectra. Time-resolved FTIR difference spectroscopy has been used to study photosystem I (PSI) particles with three different benzoquinones incorporated into the A 1 binding site.
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