Abstract
Photosystem II (PSII) from a red alga, Cyanidium caldarium, contains four extrinsic proteins of 33, 20, and 12 kDa and cytochrome (cyt) c550 [Enami, I., et al., (1995) Biochim. Biophys. Acta 1232, 208-216]. The binding and functional properties of these four proteins in the red algal PSII were studied by release-reconstitution experiments. Of the four components, the 33 kDa protein binds to PSII completely by itself, and the 20 kDa protein binds to a level 61% of that in native PSII in the absence of other proteins. In contrast, cyt c550 and the 12 kDa protein cannot bind to PSII efficiently by themselves; their effective binding requires the other three extrinsic proteins. In particular, a strong interaction was observed between cyt c550 and the 12 kDa protein, and a weaker interaction was observed between cyt c550 and the 20 kDa protein. While binding of the 33 kDa protein alone or cyt c550 and the 12 kDa protein in the presence of the 33 and/or the 20 kDa protein generally enhanced oxygen evolution, binding of the 20 kDa protein did not. Oxygen evolution was strongly dependent on Ca2+ and Cl- in the absence of cyt c550 and the 12 kDa protein, suggesting that these two proteins have functions similar to those of the 23 and 17 kDa proteins in higher plant PSII. From these results, we propose that the unique 20 kDa extrinsic protein found only in the red algal PSII functions in maintaining the proper binding of cyt c550 and the 12 kDa protein but is not involved directly in oxygen evolution. The binding and functional properties of these four proteins were compared with those of the three extrinsic proteins found in cyanobacterial and higher plant PSII in an evolutionary point of view.
| Original language | English |
|---|---|
| Pages (from-to) | 2787-2793 |
| Number of pages | 7 |
| Journal | Biochemistry |
| Volume | 37 |
| Issue number | 9 |
| DOIs | |
| Publication status | Published - Mar 3 1998 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Biochemistry
Cite this
Binding and functional properties of four extrinsic proteins of photosystem II from a red alga, Cyanidium caldarium, as studied by release- reconstitution experiments. / Enami, Isao; Kikuchi, Sanae; Fukuda, Tetsuya; Ohta, Hisataka; Shen, Jian-Ren.
In: Biochemistry, Vol. 37, No. 9, 03.03.1998, p. 2787-2793.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Binding and functional properties of four extrinsic proteins of photosystem II from a red alga, Cyanidium caldarium, as studied by release- reconstitution experiments
AU - Enami, Isao
AU - Kikuchi, Sanae
AU - Fukuda, Tetsuya
AU - Ohta, Hisataka
AU - Shen, Jian-Ren
PY - 1998/3/3
Y1 - 1998/3/3
N2 - Photosystem II (PSII) from a red alga, Cyanidium caldarium, contains four extrinsic proteins of 33, 20, and 12 kDa and cytochrome (cyt) c550 [Enami, I., et al., (1995) Biochim. Biophys. Acta 1232, 208-216]. The binding and functional properties of these four proteins in the red algal PSII were studied by release-reconstitution experiments. Of the four components, the 33 kDa protein binds to PSII completely by itself, and the 20 kDa protein binds to a level 61% of that in native PSII in the absence of other proteins. In contrast, cyt c550 and the 12 kDa protein cannot bind to PSII efficiently by themselves; their effective binding requires the other three extrinsic proteins. In particular, a strong interaction was observed between cyt c550 and the 12 kDa protein, and a weaker interaction was observed between cyt c550 and the 20 kDa protein. While binding of the 33 kDa protein alone or cyt c550 and the 12 kDa protein in the presence of the 33 and/or the 20 kDa protein generally enhanced oxygen evolution, binding of the 20 kDa protein did not. Oxygen evolution was strongly dependent on Ca2+ and Cl- in the absence of cyt c550 and the 12 kDa protein, suggesting that these two proteins have functions similar to those of the 23 and 17 kDa proteins in higher plant PSII. From these results, we propose that the unique 20 kDa extrinsic protein found only in the red algal PSII functions in maintaining the proper binding of cyt c550 and the 12 kDa protein but is not involved directly in oxygen evolution. The binding and functional properties of these four proteins were compared with those of the three extrinsic proteins found in cyanobacterial and higher plant PSII in an evolutionary point of view.
AB - Photosystem II (PSII) from a red alga, Cyanidium caldarium, contains four extrinsic proteins of 33, 20, and 12 kDa and cytochrome (cyt) c550 [Enami, I., et al., (1995) Biochim. Biophys. Acta 1232, 208-216]. The binding and functional properties of these four proteins in the red algal PSII were studied by release-reconstitution experiments. Of the four components, the 33 kDa protein binds to PSII completely by itself, and the 20 kDa protein binds to a level 61% of that in native PSII in the absence of other proteins. In contrast, cyt c550 and the 12 kDa protein cannot bind to PSII efficiently by themselves; their effective binding requires the other three extrinsic proteins. In particular, a strong interaction was observed between cyt c550 and the 12 kDa protein, and a weaker interaction was observed between cyt c550 and the 20 kDa protein. While binding of the 33 kDa protein alone or cyt c550 and the 12 kDa protein in the presence of the 33 and/or the 20 kDa protein generally enhanced oxygen evolution, binding of the 20 kDa protein did not. Oxygen evolution was strongly dependent on Ca2+ and Cl- in the absence of cyt c550 and the 12 kDa protein, suggesting that these two proteins have functions similar to those of the 23 and 17 kDa proteins in higher plant PSII. From these results, we propose that the unique 20 kDa extrinsic protein found only in the red algal PSII functions in maintaining the proper binding of cyt c550 and the 12 kDa protein but is not involved directly in oxygen evolution. The binding and functional properties of these four proteins were compared with those of the three extrinsic proteins found in cyanobacterial and higher plant PSII in an evolutionary point of view.
UR - http://www.scopus.com/inward/record.url?scp=0032478292&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032478292&partnerID=8YFLogxK
U2 - 10.1021/bi9724624
DO - 10.1021/bi9724624
M3 - Article
C2 - 9485429
AN - SCOPUS:0032478292
VL - 37
SP - 2787
EP - 2793
JO - Biochemistry
JF - Biochemistry
SN - 0006-2960
IS - 9
ER -