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
A PSII reaction center complex consisting of three polypeptides, D<sub>1</sub>, D<sub>2</sub> and Cyt. b<sub>559</sub>, was first purified from broad bean leaves. The complex was fa...A PSII reaction center complex consisting of three polypeptides, D<sub>1</sub>, D<sub>2</sub> and Cyt. b<sub>559</sub>, was first purified from broad bean leaves. The complex was fairly active inDCIP photoreduction in the presence of DPC, and showed signal Ⅱs either in the dark or under illumination. The complex also contained manganese atoms. Its Mn<sup>2+</sup>-EPR intensity decreased by about 40% under continuous illumination and recovered to the original level when the complex was transferred to the dark. The above results indicated that the complex reported here contains all of the PSII electron transport chain components from the secondary donor Z to the stable primary electron acceptor Q<sub>A</sub>, and it is possible that the complex contains manganese binding sites. The alternation in dark and illumination can induce reversible valence changes of the manganese atoms in the purified 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Project supported by the National Natural Science Foundation of China
文摘A PSII reaction center complex consisting of three polypeptides, D<sub>1</sub>, D<sub>2</sub> and Cyt. b<sub>559</sub>, was first purified from broad bean leaves. The complex was fairly active inDCIP photoreduction in the presence of DPC, and showed signal Ⅱs either in the dark or under illumination. The complex also contained manganese atoms. Its Mn<sup>2+</sup>-EPR intensity decreased by about 40% under continuous illumination and recovered to the original level when the complex was transferred to the dark. The above results indicated that the complex reported here contains all of the PSII electron transport chain components from the secondary donor Z to the stable primary electron acceptor Q<sub>A</sub>, and it is possible that the complex contains manganese binding sites. The alternation in dark and illumination can induce reversible valence changes of the manganese atoms in the purified complex.
