Faculty Profiles - SHEN Jian-Ren

Papers - SHEN Jian-Ren

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3S4-3 Recent progress on the structural studies of Photosystem II oxygen- evolving complex(3S4 New trend of photosynthesis =New energy innovation based on the photosynthesis=,The 46th Annual Meeting of the Biophysical Society of Japan)

Shen Jian-Ren

Seibutsu Butsuri 48 S18 2008

Aromatic structure of Tyrosine-92 in the extrinsic PsbU protein of red algal Photosystem II is important for its functioning Reviewed International journal

Akinori Okumura, Masanori Sano, Takehiro Suzuki, Hiroyasu Tanaka, Ryo Nagao, Katsuyoshi Nakazato, Masako Iwai, Hideyuki Adachi, Jian-Ren Shen, Isao Enami

FEBS LETTERS 581 ( 27 ) 5255 - 5258 2007.11

Language：English Publishing type：Research paper (scientific journal) Publisher：ELSEVIER SCIENCE BV

PsbU is one of the extrinsic proteins in red algal Photosystem II (PSII) and functions to optimize the availability of Ca2+ and Cl- cofactors for water oxidation. To determine the functional residue of PsbU, we constructed various PsbU mutants from a red alga Cyanidium caldarium and reconstituted these mutants with the red algal PSII. The results revealed that Tyr-92 of PsbU, especially its aromatic ring, was essential for maintaining its function. From the crystal structure of PSII, Tyr-92 is located close to Pro-340 of D1, suggesting that the aromatic ring of Tyr-92 interacts with the CH group of Pro-340 of D1, and this CH/pi interaction is important for the optimal function of the Mn4Ca-cluster. (C) 2007 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

DOI： 10.1016/j.febslet.2007.10.015

Location of PsbY in oxygen-evolving photosystem II revealed by mutagenesis and X-ray crystallography. Reviewed International journal

Keisuke Kawakami, Masako Iwai, Masahiko Ikeuchi, Nobuo Kamiya, Jian-Ren Shen

FEBS letters 581 ( 25 ) 4983 - 7 2007.10

Language：English Publishing type：Research paper (scientific journal) Publisher：WILEY

PsbY is one of the low molecular mass subunits of oxygen-evolving photosystem II (PSII). Its location, however, has not been identified in the current crystal structure of PSII. We constructed a PsbY-deletion mutant of Thermosynechococcus elongatus, crystallized, and analyzed the crystal structure of the mutant PSII dimer. The results obtained showed that PsbY is located in the periphery of PSII close to the alpha- and beta-subunits of cytochrome b559, which corresponded to an unassigned helix in the 3.7A structure of T. vulcanus or helix X2 in the 3.0A structure of T. elongatus. Our results also indicated that the C-terminal loop of PsbY is protruded toward the stromal side, instead of the lumenal side predicted previously.

DOI： 10.1016/j.febslet.2007.09.036

Self-assembling peptide inspired by a barnacle underwater adhesive protein Reviewed International journal

Masahiro Nakano, Jian-Ren Shen, Kei Kamino

BIOMACROMOLECULES 8 ( 6 ) 1830 - 1835 2007.6

Language：English Publishing type：Research paper (scientific journal) Publisher：AMER CHEMICAL SOC

An underwater bioadhesive generally comprises a multiprotein complex that provides a molecular basis for self-assembly. We report here a new class of self-assembling peptide inspired by a 20 kDa barnacle cement protein. Studies on the chemically synthesized 24-residue peptide have revealed that (1) it underwent irreversible self-assembly upon the addition of salt, (2) the self-assembly was started at a salt concentration close to that of seawater with noncovalent intermolecular interactions, (3) the self-assembled material resembled a macroscopic membrane of interwoven nanofilaments, (4) incubation in an alkaline pH range formed the intramolecular disulfide bond of a peptide molecule, thus triggering a conformation change of the molecule, and (5) conformational change of the building block promoted the formation of a nanofiber, resulting in the display of a three-dimensional meshlike mesoscopic structure with defined pores having a diameter of approximately 200 nm. The peptide is likely to provide a suitable basis for further development of peptide-based materials.

DOI： 10.1021/bm0612236

2P330 Introduction of the photosystem II photosynthetic reaction center complex into the silica mesoporous materials(Photobiology-photosynthesis,Poster Presentations)

Noji Tomoyasu, Kawakami Keisuke, Shen Jian-Ren, Kajino Tsutomu, Fukushima Yoshiaki, Sekitoh Takeshi, Itoh Shigeru

Seibutsu Butsuri 47 S195 2007

Lipids in oxygen-evolving photosystem II complexes of cyanobacteria and higher plants Reviewed International journal

Isamu Sakurai, Jian-Ren Shen, Jing Leng, Shunsuke Ohashi, Masami Kobayashi, Hajime Wada

JOURNAL OF BIOCHEMISTRY 140 ( 2 ) 201 - 209 2006.8

Language：English Publishing type：Research paper (scientific journal) Publisher：OXFORD UNIV PRESS

Lipids in dimeric photosystem II complexes prepared from two species of cyanobacteria, Thermosynechococcus vulcanus and Synechocystis sp. PCC6803, and two higher plants, spinach and rice, were analyzed to determine how many lipid molecules and what class of lipids are present in the photosystem Il complexes. It was estimated that 27, 20, 8, and 7 lipid molecules per monomer are bound to the dimeric photosystem Il complexes of T. vulcanus, Synechocystis, spinach, and rice, respectively. In each of the organisms, the lipid composition of the photosystem 11 complexes was quite different from that of the thylakoid membranes used for preparation of the complexes. The content of phosphatidylglycerol. in the photosystem 11 complexes of each organism was much higher than that in the thylakoid membranes. Phospholipase A(2) treatment of the photosystem 11 complexes of Synechocystis that degraded phosphatidylglycerol resulted in impairment of Q(B)-mediated but not Q(A)-mediated electron transport. These findings suggest that phosphatidylglycerol plays important roles in the electron transport at the Q(B)-binding site in photosystem 11 complexes.

DOI： 10.1093/jb/mvj141

Anisotropy of the S-2-state manganese cluster in single crystals of cyanobacterial photosystem II studied by W-band electron paramagnetic resonance spectroscopy Reviewed International journal

Hideto Matsuoka, Ko Furukawa, Tatsuhisa Kato, Hiroyuki Mino, Jian-Ren Shen, Asako Kawamori

JOURNAL OF PHYSICAL CHEMISTRY B 110 ( 26 ) 13242 - 13247 2006.7

Language：English Publishing type：Research paper (scientific journal) Publisher：AMER CHEMICAL SOC

The multiline signal from the S-2-state manganese cluster in the oxygen evolving complex of photosystem II (PSII) was observed in single crystals of a thermophilic cyanobacterium Thermosynechococcus Vulcanus for the first time by W-band (94 GHz) electron paramagnetic resonance (EPR). At W- band, spectra were characterized by the g-anisotropy, which enabled the precise determination of the tensor. Distinct hyperfine splittings (hfs's) as seen in frozen solutions of PSII at X-band (9.5 GHz) were detected in most of the crystal orientations relative to the magnetic field. In some orientations, however, the hfs's disappeared due to overlapping of a large number of EPR lines from eight crystallographic symmetry-related sites of the manganese cluster within the unit cell of the crystal. Analysis of the orientation-dependent spectral features yielded the following g-tensor components: g(x) = 1.988, g(y) = 1.981, g(z) = 1.965. The principal values suggested an approximate axial symmetry around the Mn(III) ion in the cluster.

DOI： 10.1021/jp055008f

Quality control of Photosystem II: an FtsH protease plays an essential role in the turnover of the reaction center D1 protein in Synechocystis PCC 6803 under heat stress as well as light stress conditions. Reviewed International journal

Takashi Kamata, Hideki Hiramoto, Noriko Morita, Jian-Ren Shen, Nicholas H Mann, Yasusi Yamamoto

Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology 4 ( 12 ) 983 - 90 2005.12

Language：English Publishing type：Research paper (scientific journal)

The role of an AAA protease FtsH (slr0228) in the turnover of the D1 protein was studied under moderate heat stress conditions using wild-type cells of the cyanobacterium Synechocystis PCC 6803 and the mutant cells lacking a homologue of FtsH (slr0228). When the growth temperature of the wild-type was shifted from 30 degrees C to 40 degrees C, growth and oxygen-evolving activity were partially inhibited. Under the same heat stress, growth of the mutant was inhibited more significantly (63% inhibition after 5 days heat stress, compared with 26% inhibition with the wild-type cells) and the oxygen-evolving activity was also impaired in parallel. With heat stress at 42 degrees C, the level of the D1 protein of wild type cells was decreased, whereas that in mutant cells was not. The responses of cyanobacterial cells to heat stress observed here are quite similar to those to light stress that were reported previously. From these results, we suggest that the FtsH protease (slr0228) is responsible for both the heat-induced and light-induced degradation of the D1 protein. Notably, the amount of FtsH increased when the wild-type cells were exposed to heat stress or light stress, indicating that the up-regulation of the FtsH protease in the thylakoids is crucial for the cyanobacterial cells to cope with these abiotic stresses.

Distribution of the extrinsic proteins as a potential marker for the evolution of photosynthetic oxygen-evolving photosystem II. Reviewed International journal

Isao Enami, Takehiro Suzuki, Osamu Tada, Yoshiko Nakada, Kumi Nakamura, Akihiko Tohri, Hisataka Ohta, Isao Inoue, Jian-Ren Shen

The FEBS journal 272 ( 19 ) 5020 - 30 2005.10

Language：English Publishing type：Research paper (scientific journal)

Distribution of photosystem II (PSII) extrinsic proteins was examined using antibodies raised against various extrinsic proteins from different sources. The results showed that a glaucophyte (Cyanophora paradoxa) having the most primitive plastids contained the cyanobacterial-type extrinsic proteins (PsbO, PsbV, PsbU), and the primitive red algae (Cyanidium caldarium) contained the red algal-type extrinsic proteins (PsO, PsbQ', PsbV, PsbU), whereas a prasinophyte (Pyraminonas parkeae), which is one of the most primitive green algae, contained the green algal-type ones (PsbO, PsbP, PsbQ). These suggest that the extrinsic proteins had been diverged into cyanobacterial-, red algal- and green algal-types during early phases of evolution after a primary endosymbiosis. This study also showed that a haptophyte, diatoms and brown algae, which resulted from red algal secondary endosymbiosis, contained the red algal-type, whereas Euglena gracilis resulted from green algal secondary endosymbiosis contained the green algal-type extrinsic proteins, suggesting that the red algal- and green algal-type extrinsic proteins have been retained unchanged in the different lines of organisms following the secondary endosymbiosis. Based on these immunological analyses, together with the current genome data, the evolution of photosynthetic oxygen-evolving PSII was discussed from a view of distribution of the extrinsic proteins, and a new model for the evolution of the PSII extrinsic proteins was proposed.

Key cofactors of photosystem II cores from four organisms identified by 1.7-K absorption, CD and MCD. Reviewed International journal

Sindra Peterson Arsköld, Paul J Smith, Jian-Ren Shen, Ron J Pace, Elmars Krausz

Photosynthesis research 84 ( 1-3 ) 309 - 16 2005.6

Language：English Publishing type：Research paper (scientific journal)

Active Photosystem II (PS II) cores were prepared from spinach, pea, Synechocystis PCC 6803, and Thermosynechococcus vulcanus, the latter of which has been structurally determined [Kamiya and Shen (2003) Proc Natl Acad Sci USA 100: 98-103]. Electrochromic shifts resulting from QA reduction by 1.7-K illumination were recorded, and the Qx and Qy absorption bands of the redox-active pheophytin a thus identified in the different organisms. The Qx transition is approximately 3 nm (100 cm-1) to higher energy in cyanobacteria than in the plants. The predominant Qy shift appears in the range 683-686 nm depending on species, and does not appear to have a systematic shift. Low-temperature absorption, circular dichroism (CD) and magnetic circular dichroism (MCD) spectra of the chlorophyll Qy region are very similar in spinach and pea, but vary in cyanobacteria. We assigned CP43 and CP47 trap-chlorophyll absorption features in all species, as well as a P680 transition. Each absorption identified has an area of one chlorophyll a. The MCD deficit, introduced previously for spinach as an indicator of P680 activity, occurs in the same spectral region and has the same area in all species, pointing to a robustness of this as a signature for P680. MCD and CD characteristics point towards a significant variance in P680 structure between cyanobacteria, thermophilic cyanobacteria, and higher plants.

Pressure equilibrium and jump study on unfolding of 23-kDa protein from spinach photosystem II. Reviewed International journal

Cui-Yan Tan, Chun-He Xu, Jun Wong, Jian-Ren Shen, Shinsuke Sakuma, Yasusi Yamamoto, Reinhard Lange, Claude Balny, Kang-Cheng Ruan

Biophysical journal 88 ( 2 ) 1264 - 75 2005.2

Language：English Publishing type：Research paper (scientific journal)

Pressure-induced unfolding of 23-kDa protein from spinach photosystem II has been systematically investigated at various experimental conditions. Thermodynamic equilibrium studies indicate that the protein is very sensitive to pressure. At 20 degrees C and pH 5.5, 23-kDa protein shows a reversible two-state unfolding transition under pressure with a midpoint near 160 MPa, which is much lower than most natural proteins studied to date. The free energy (DeltaG(u)) and volume change (DeltaV(u)) for the unfolding are 5.9 kcal/mol and -160 ml/mol, respectively. It was found that NaCl and sucrose significantly stabilize the protein from unfolding and the stabilization is associated not only with an increase in DeltaG(u) but also with a decrease in DeltaV(u). The pressure-jump studies of 23-kDa protein reveal a negative activation volume for unfolding (-66.2 ml/mol) and a positive activation volume for refolding (84.1 ml/mol), indicating that, in terms of system volume, the protein transition state lies between the folded and unfolded states. Examination of the temperature effect on the unfolding kinetics indicates that the thermal expansibility of the transition state and the unfolded state of 23-kDa protein are closer to each other and they are larger than that of the native state. The diverse pressure-refolding pathways of 23-kDa protein in some conditions were revealed in pressure-jump kinetics.

High frequency EPR of the Mn-cluster in single crystals of cyanobacterial photosystem II Reviewed

Asako Kawamori, Jian-Ren Shen, Hiroyuki Mino, Ko Furukawa, Hideto Matsuoka, Tatsuhisa Kato

Photosynthesis: Fundamental Aspects to Global Perspectives 406 - 408 2005

An icosahedral assembly of the light-harvesting chlorophyll a/b protein complex from pea chloroplast thylakoid membranes. Reviewed International journal

Tomoya Hino, Eiji Kanamori, Jian-Ren Shen, Tsutomu Kouyama

Acta crystallographica. Section D, Biological crystallography 60 ( Pt 5 ) 803 - 9 2004.5

Language：English Publishing type：Research paper (scientific journal)

When the light-harvesting chlorophyll a/b protein complex (LHC-II) from pea thylakoid membranes is co-crystallized with native lipids, an octahedral crystal that exhibits no birefringence is obtained. Cryogenic electron micrographs of a crystal edge showed the crystal to be made up of hollow spherical assemblies with a diameter of 250 A. X-ray diffraction data at 9.5 A resolution revealed the spherical shell of LHC-II to have icosahedral symmetry. A T = 1 icosahedral model of LHC-II, in which the stromal surface of the protein faces outward, was constructed using the previously reported structure of the LHC-II trimer [Kühlbrandt et al. (1994), Nature (London), 367, 614-621]. The present result shows the first example of a well ordered three-dimensional crystal of icosahedral proteoliposomes.

pH-induced conformational changes in the soluble manganese-stabilizing protein of photosystem II. Reviewed International journal

Jun Weng, Cuiyan Tan, Jian-Ren Shen, Yong Yu, Xiaomei Zeng, Chunhe Xu, Kangcheng Ruan

Biochemistry 43 ( 16 ) 4855 - 61 2004.4

Language：English Publishing type：Research paper (scientific journal)

In this paper, we analyzed the pH-induced changes in the conformational states of the manganese-stabilizing protein (MSP) of photosystem II. Distinct conformational states of MSP were identified using fluorescence spectra, far-UV circular dichroism, and pressure-induced unfolding at varying suspension pH values, and four different conformational states of MSP were clearly distinguished using the center of fluorescence spectra mass when suspension pH was altered from 2 to 12. MSP was completely unfolded at a suspension pH above 11 and partly unfolded below a pH of 3. Analysis of the center of fluorescence spectral mass showed that the MSP structure appears stably folded around pH 6 and 4. The conformational state of MSP at pH 4 seems more stable than that at pH 6. Studies of peak positions of tryptophan fluorescence and MSP-bound 1-anilinonaphthalene-8-sulfonic acid fluorescence spectra supported this observation. A decrease in the suspension pH to 2 resulted in significant alterations in the MSP structure possibly because of protonation of unprotonated residues at lower pH, suggesting the existence of a large number of unprotonated amino acid residues at neutral pH possibly useful for proton transport in oxygen evolution. The acidic pH-induced conformational changes of MSP were reversible upon increase of pH to neutral pH; however, N-bromosuccinimide modification of tryptophan (Trp241) blocks the recovery of pH-induced conformational changes in MSP, implying that Trp241 is a key residue for the unfolded protein to form a functional structure. Thus, pH-induced structural changes of stable MSP (pH 6-4) may be utilized to analyze its functionality as a cofactor for oxygen evolution.

The orientations of core antenna chlorophylls in photosystem II are optimized to maximize the quantum yield of photosynthesis. Reviewed International journal

Sergei Vasil'ev, Jian-Ren Shen, Nobuo Kamiya, Doug Bruce

FEBS letters 561 ( 1-3 ) 111 - 6 2004.3

Language：English Publishing type：Research paper (scientific journal)

In photosystem II (PSII) the probability that energy absorbed by core antenna chlorophyll (Chl) is transferred to the reaction center (RC) is extremely high. Although close proximity between antenna Chl ensures a high transfer efficiency, relative pigment orientation can fractionally modify it. This level of refinement has often been assumed to be superfluous as so many subsequent processes limit the overall efficiency of photosynthesis. Nevertheless, did natural selection act on the most efficient step of energy conversion in PSII by optimizing the orientation of antenna Chl? Our Monte Carlo simulations sampled the orientation space of Chls in kinetic models for excitation energy transfer based on the X-ray structures of PSII from Thermosynechococcus vulcanus and Synechocystis elongatus. Our results revealed that the orientations of key antenna Chls are optimized to maximize photosynthesis while the orientations of the two peripheral RC Chls (Chl(Z)) are not.

Isolation of photosystem II-enriched membranes and the oxygen-evolving complex subunit proteins from higher plants. Reviewed International journal

Yasusi Yamamoto, Shinsuke Sakuma, Jian-Ren Shen

Methods in molecular biology (Clifton, N.J.) 274 29 - 36 2004

Language：English Publishing type：Research paper (scientific journal)

Methods for the isolation of highly active oxygen-evolving photosystem (PS)II membranes from higher plants and the purification of the oxygen-evolving complex (OEC) subunits are described. Membrane samples used as the material for various in vitro studies of PSII are prepared by solubilization of thylakoid membranes with the non-ionic detergent Triton X-100. The OEC subunit proteins are dissociated from the PSII-enriched membranes by alkaline treatment or salt treatment, and then purified by ion-exchange chromatography using an automated high-performance liquid chromatography system.

1SD52 Functional implications of photosystem II from its crystal structural analysis

Shen J.-R., Kamiya N.

Seibutsu Butsuri 44 S12 2004

Extrinsic proteins of photosystem II: an intermediate member of PsbQ protein family in red algal PS II. Reviewed International journal

Hisataka Ohta, Takehiro Suzuki, Masaji Ueno, Akinori Okumura, Shizue Yoshihara, Jian-Ren Shen, Isao Enami

European journal of biochemistry 270 ( 20 ) 4156 - 63 2003.10

Language：English Publishing type：Research paper (scientific journal)

The oxygen-evolving photosystem II (PS II) complex of red algae contains four extrinsic proteins of 12 kDa, 20 kDa, 33 kDa and cyt c-550, among which the 20 kDa protein is unique in that it is not found in other organisms. We cloned the gene for the 20-kDa protein from a red alga Cyanidium caldarium. The gene consists of a leader sequence which can be divided into two parts: one for transfer across the plastid envelope and the other for transfer into thylakoid lumen, indicating that the gene is encoded by the nuclear genome. The sequence of the mature 20-kDa protein has low but significant homology with the extrinsic 17-kDa (PsbQ) protein of PS II from green algae Volvox Carteri and Chlamydomonas reinhardtii, as well as the PsbQ protein of higher plants and PsbQ-like protein from cyanobacteria. Cross-reconstitution experiments with combinations of the extrinsic proteins and PS IIs from the red alga Cy. caldarium and green alga Ch. reinhardtii showed that the extrinsic 20-kDa protein was functional in place of the green algal 17-kDa protein on binding to the green algal PS II and restoration of oxygen evolution. From these results, we conclude that the 20-kDa protein is the ancestral form of the extrinsic 17-kDa protein in green algal and higher plant PS IIs. This provides an important clue to the evolution of the oxygen-evolving complex from prokaryotic cyanobacteria to eukaryotic higher plants. The gene coding for the extrinsic 20-kDa protein was named psbQ' (prime).

Comparison of binding and functional properties of two extrinsic components, Cyt c550 and a 12 kDa protein, in cyanobacterial PSII with those in red algal PSII. Reviewed

Isao Enami, Masako Iwai, Ai Akiyama, Takehiro Suzuki, Akinori Okumura, Takara Katoh, Osamu Tada, Hisataka Ohta, Jian-Ren Shen

Plant & cell physiology 44 ( 8 ) 820 - 7 2003.8

Language：English Publishing type：Research paper (scientific journal)

Cyt c550 and 12 kDa protein are two extrinsic proteins of photosystem II (PSII) found in cyanobacteria and some eukaryotic algae. The binding patterns of these two extrinsic proteins are different between cyanobacterial (Thermosynechococcus vulcanus) and red algal (Cyanidium caldarium) PSIIs [Shen and Inoue (1993) Biochemistry 32: 1825; Enami et al. (1998) Biochemistry 39: 2787]. In order to elucidate the possible causes responsible for these differences, we first cloned the psbV gene encoding Cyt c550 from a red alga, Cyanidium caldarium, which was compared with the homologous sequences from other organisms. Cross-reconstitution experiments were then performed with different combinations of the extrinsic proteins and the cyanobacterial or red algal PSII. (1). Both the cyanobacterial and red algal Cyt c550 bound directly to the cyanobacterial PSII, whereas none of them bound directly to the red algal PSII, indicating that direct binding of Cyt c550 to PSII principally depends on the structure of PSII intrinsic proteins but not that of Cyt c550 itself. (2). Cyt c550 was functionally exchangeable between the red algal and the cyanobacterial PSII, and the red algal 12 kDa protein functionally bound to the cyanobacterial PSII, whereas the cyanobacterial 12 kDa protein did not bind to the red algal PSII. (3). The antibody against the cyanobacterial or red algal 12 kDa protein reacted with its original one but not with the homologous protein from the other organism, whereas the antibody against the red algal Cyt c550 reacted with both cyanobacterial and red algal Cyt c550. These results imply that the structure and function of Cyt c550 have been largely conserved, whereas those of the 12 kDa protein have been changed, in the two organisms studied here.

Dynamic Interaction between the D1 protein, CP43 and OEC33 at the lumenal side of photosystem II in spinach chloroplasts: evidence from light-induced cross-Linking of the proteins in the donor-side photoinhibition. Reviewed

Takahiro Henmi, Hitoshi Yamasaki, Shinsuke Sakuma, Yuka Tomokawa, Noriaki Tamura, Jian-Ren Shen, Yasusi Yamamoto

Plant & cell physiology 44 ( 4 ) 451 - 6 2003.4

Language：English Publishing type：Research paper (scientific journal)

During the donor-side photoinhibition of spinach photosystem II, the reaction center D1 protein cross-linked with the antenna chlorophyll binding protein CP43 of photosystem II lacking the oxygen-evolving complex (OEC) subunit proteins. The cross-linking did not occur upon illumination of photosystem II samples that retained the OEC33, nor when OEC33-depleted photosystem II samples were reconstituted with the OEC33 prior to illumination. These results suggest that the D1 protein, CP43 and the OEC33 are located in close proximity at the lumenal side of photosystem II, and that the OEC33 suppresses the unnecessary contact between the D1 protein and CP43. Previously we presented data showing the D1 protein located adjacent to CP43 on the stromal side of photosystem II [Ishikawa et al. (1999) BIOCHIM: Biophys. Acta 1413: 147]. The present data suggest that the spatial arrangement of the D1 protein and CP43 at the lumenal side of photosystem II in spinach chloroplasts is similar to that at the stromal side of photosystem II and is consistent with the assignment of these proteins recently proposed on the crystal structures of the photosystem II complexes from cyanobacteria [Zouni et al. (2001) Nature 409: 739, Kamiya and Shen 2003 PROC: Natl. Acad. Sci. USA, 100: 98]. Moreover, the data suggest that the binding condition and positioning of the OEC33 in the photosystem II complex from higher plants may be different from those in cyanobacteria.

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