Photodamage of some pigments in the isolated photosystem Ⅱ (PS Ⅱ) reaction center D1/D2/Cyt b559 complex from spinach has been investigated by means of high performance liquid chromatography. The light induced damag...Photodamage of some pigments in the isolated photosystem Ⅱ (PS Ⅱ) reaction center D1/D2/Cyt b559 complex from spinach has been investigated by means of high performance liquid chromatography. The light induced damage of pheophytin a (pheo a) in the complex was observed for the first time. The content of pheo a decreased about 47% by illumination, suggesting only one of the two pheo a molecules in the PSⅡ reaction center complex was damaged. No damage of β carotene was found.展开更多
Photodamage of pheophytin a (pheo a) in the isolated photosystem Ⅱ (PSⅡ) reaction center D1/D2/Cyt b559 complex from spinach has been investigated by high performance liquid chromatographic method in detail. The res...Photodamage of pheophytin a (pheo a) in the isolated photosystem Ⅱ (PSⅡ) reaction center D1/D2/Cyt b559 complex from spinach has been investigated by high performance liquid chromatographic method in detail. The results showed that: (1) There is one pheo a molecule which is not associated with the primary photochemistry in the PSⅡ reaction center complex. It may be considered that there are two different electron transfer branches in the PSⅡ reaction center just as in the purple bacterium photosynthetic reaction center. (2) The damaged pheo a may be attributed to the one bonding to the D2 protein comparing the D2 subunit in the PSⅡ reaction center with M subunit in the purple bacterium photosynthetic reaction center. (3) A possible arrangement model of redox cofactors in the PSⅡ reaction center was proposed based on our experiment.展开更多
It was studied by spectroscopy that PSII reaction center complex consisting of three polypeptides, D1, D2 and Cytb559, were purified from PSII particle of CeCl3 treated spinach. The results of the experiment show that...It was studied by spectroscopy that PSII reaction center complex consisting of three polypeptides, D1, D2 and Cytb559, were purified from PSII particle of CeCl3 treated spinach. The results of the experiment show that Ce3+ could improve the growth of spinach, and accelerate electron transport of PSII particles. Of chl-a of UV-Vis spectrum of D1/D2/Cytb559 complex, Soret band was blue-shifted by 3 nm and Q band by 2 nm, respectively, and the fluorescence emission peak was blue-shifted by 5 nm in CeCl3-treated spinach compared with the one in control. By the extended X-ray absorption fine structure (EXAFS) spectroscopy methods, it has been found that Ce3+ is coordinated with 8 nitrogen atoms in the first coordination shell with Ce-N bond length of 0.253 nm, and Ce3+ with 6 oxygen atoms in the second coordination shell with Ce-O bond length of 0.32 nm. However, the secondary structure of D1/D2/Cytb559 complex by circular dichroism (CD) spectroscopy has no significant change after CeCl3 treated. It might be that Ce3+ binds to porphyrin rings of chlorophyll and oxygen of amino acid residue of polypeptide in D1/D2/Cytb559 complex, and then accelerates the primary reaction of PSII, intensifies function of P680+ primary electron donor of D1/D2/Cytb559, but there is little change in conformation of PSII reaction center complex.展开更多
文摘Photodamage of some pigments in the isolated photosystem Ⅱ (PS Ⅱ) reaction center D1/D2/Cyt b559 complex from spinach has been investigated by means of high performance liquid chromatography. The light induced damage of pheophytin a (pheo a) in the complex was observed for the first time. The content of pheo a decreased about 47% by illumination, suggesting only one of the two pheo a molecules in the PSⅡ reaction center complex was damaged. No damage of β carotene was found.
文摘Photodamage of pheophytin a (pheo a) in the isolated photosystem Ⅱ (PSⅡ) reaction center D1/D2/Cyt b559 complex from spinach has been investigated by high performance liquid chromatographic method in detail. The results showed that: (1) There is one pheo a molecule which is not associated with the primary photochemistry in the PSⅡ reaction center complex. It may be considered that there are two different electron transfer branches in the PSⅡ reaction center just as in the purple bacterium photosynthetic reaction center. (2) The damaged pheo a may be attributed to the one bonding to the D2 protein comparing the D2 subunit in the PSⅡ reaction center with M subunit in the purple bacterium photosynthetic reaction center. (3) A possible arrangement model of redox cofactors in the PSⅡ reaction center was proposed based on our experiment.
基金This work was supported by the National Natural Science Foundation of China (Grant No. 29805003) Person of Ability Recommended Foundation of Suzhou University (Grant No. XQ316011).
文摘It was studied by spectroscopy that PSII reaction center complex consisting of three polypeptides, D1, D2 and Cytb559, were purified from PSII particle of CeCl3 treated spinach. The results of the experiment show that Ce3+ could improve the growth of spinach, and accelerate electron transport of PSII particles. Of chl-a of UV-Vis spectrum of D1/D2/Cytb559 complex, Soret band was blue-shifted by 3 nm and Q band by 2 nm, respectively, and the fluorescence emission peak was blue-shifted by 5 nm in CeCl3-treated spinach compared with the one in control. By the extended X-ray absorption fine structure (EXAFS) spectroscopy methods, it has been found that Ce3+ is coordinated with 8 nitrogen atoms in the first coordination shell with Ce-N bond length of 0.253 nm, and Ce3+ with 6 oxygen atoms in the second coordination shell with Ce-O bond length of 0.32 nm. However, the secondary structure of D1/D2/Cytb559 complex by circular dichroism (CD) spectroscopy has no significant change after CeCl3 treated. It might be that Ce3+ binds to porphyrin rings of chlorophyll and oxygen of amino acid residue of polypeptide in D1/D2/Cytb559 complex, and then accelerates the primary reaction of PSII, intensifies function of P680+ primary electron donor of D1/D2/Cytb559, but there is little change in conformation of PSII reaction center complex.
