Silicomolybdate substitutes for the function of a primary electron acceptor and stabilizes charge separation in the photosystem II reaction center complex
- 11 September 1989
- journal article
- Published by Wiley in FEBS Letters
- Vol. 255 (1) , 133-138
- https://doi.org/10.1016/0014-5793(89)81076-2
Abstract
Effects of silicomolybdate on the charge recombination between P680+ and the reduced pheophytin were studied by absorption and electron paramagnetic resonance spectroscopies in the photosystem II D1/D2/cytochrome b‐559 reaction center complex. This preparation lacks the primary and secondary quinone acceptors, QA and QB, and exhibits the charge recombination which produces the triplet state of P680 to a large extent. In the presence of silicomolybdate, the light‐induced triplet signal of P680 was almost completely eliminated at cryogenic temperatures as well as at 4°C. Under these conditions, two types of signals, one reversible and the other irreversible, which are ascribable to P680+ and the cation radical of antenna chlorophyll a, respectively, were generated upon illumination at cryogenic temperatures. These results indicate that silicomolybdate, which is known to be an artificial electron acceptor of QA, rapidly receives electrons from the reduced pheophytin even at cryogenic temperatures and thus suppresses the radical pair recombination which occurs in the time range of nanosecond. P680+ formed by flash excitation in the presence of silicomolybdate relaxed mainly with a long half decay time of 74 ms at 4°C. This indicates that the reduction of P680+ by the secondary electron donor, Z, is significantly decreased.Keywords
This publication has 25 references indexed in Scilit:
- Evidence for the photo‐induced oxidation of the primary electron donor P680 in the isolated photosystem II reaction centreFEBS Letters, 1989
- Vitamin K1 (phylloquinone) restores the turnover of FeS centers in the ether‐extracted spinach PS I particlesFEBS Letters, 1989
- Directed mutagenesis indicates that the donor to P 680+ in photosystem II is tyrosine-161 of the D1 polypeptideBiochemistry, 1988
- Reconstitution of plastoquinone in the D1/D2/cytochrome b‐559 photosystem II reaction centre complexFEBS Letters, 1988
- Oxidation-reduction potential dependence of reaction centre triplet formation in the isolated D1/D2/cytochromeb-559 photosystem II complexFEBS Letters, 1988
- A comparative study of the reduction of EPR signal IIslow by iodide and the iodo‐labeling of the D2‐protein in photosystem IIFEBS Letters, 1987
- Characterisation of a PS II reaction centre isolated from the chloroplasts ofPisum sativumFEBS Letters, 1987
- The primary reaction of photosystem II in the D1‐D2‐cytochrome b‐559 complexFEBS Letters, 1987
- Specific125I labeling of D1 (herbicide‐binding protein)FEBS Letters, 1987
- Identification of the site of iodide photooxidation in the photosystem II reaction center complexFEBS Letters, 1986