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  • Chlamydomonas  (1)
  • electron paramagnetic resonance (EPR)  (1)
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  • 1
    ISSN: 1573-5079
    Keywords: Photoinhibition ; Photosystem II ; quinone-iron complex ; electron paramagnetic resonance (EPR) ; thermoluminescence (TL)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Photosystem II particles were exposed to 800 W m−2 white light at 20 °C under anoxic conditions. The Fo level of fluorescence was considerably enhanced indicating formation of stable-reduced forms of the primary quinone electron acceptor, QA. The Fm level of fluorescence declined only a little. The g=1.9 and g=1.82 EPR forms characteristic of the bicarbonate-bound and bicarbonate-depleted semiquinone-iron complex, QA −Fe2+, respectively, exhibited differential sensitivity against photoinhibition. The large g=1.9 signal was rapidly diminished but the small g=1.82 signal decreased more slowly. The S2-state multiline signal, the oxygen evolution and photooxidation of the high potential form of cytochrome b-559 were inhibited approximately with the same kinetics as the g=1.9 signal. The low potential form of oxidized cytochrome b-559 and Signal IIslow arising from TyrD + decreased considerably slower than the g=1.9 semiquinone-iron signal. The high potential form of oxidized cytochrome b-559 was diminished faster than the low potential form. Photoinhibition of the g=1.9 and g=1.82 forms of QA was accompanied with the appearance and gradual saturation of the spin-polarized triplet signal of P 680. The amplitude of the radical signal from photoreducible pheophytin remained constant during the 3 hour illumination period. In the thermoluminescence glow curves of particles the Q band (S2QA − charge recombination) was almost completely abolished. To the contrary, the C band (TyrD +QA − charge recombination) increased a little upon illumination. The EPR and thermoluminescence observations suggest that the Photosystem II reaction centers can be classified into two groups with different susceptibility against photoinhibition.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-5079
    Keywords: Chlamydomonas ; mutation ; photosynthesis ; Photosystem 1 ; PsaA ; reaction center
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The psaA and psaB genes of the chloroplast genome in oxygenic photosynthetic organisms code for the major peptides of the Photosystem 1 reaction center. A heterodimer of the two polypeptides PsaA and PsaB is thought to bind the reaction center chlorophyll, P700, and the early electron acceptors A0, A1 and Fe-SX. Fe-SX is a 4Fe4S center requiring 4 cysteine residues as ligands from the protein. As PsaA and PsaB have only three and two conserved cysteine residues respectively, it has been proposed by several groups that Fe-SX is an unusual inter-peptide center liganded by two cysteines from each peptide. This hypothesis has been tested by site directed mutagenesis of PsaA residue C575 and the adjacent D576. The C575D mutant does not assemble Photosystem 1. The C575H mutant contains a photoxidisable chlorophyll with EPR properties of P700, but no other Photosystem 1 function has been detected. The D576L mutant assembles a modified Photosystem 1 in which the EPR properties of the Fe-SA/B centers are altered. The results confirm the importance of the conserved cysteine motif region in Photosystem 1 structure.
    Type of Medium: Electronic Resource
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