Faculty Profiles - SHEN Jian-Ren

Papers - SHEN Jian-Ren

Division display 261 - 280 of about 280 ／ All the affair displays >>

Near-IR irradiation of the S2 state of the water oxidizing complex of photosystem II at liquid helium temperatures produces the metalloradical intermediate attributed to S1Y(Z*). Reviewed International journal

Dionysios Koulougliotis, Jian-Ren Shen, Nikolaos Ioannidis, Vasili Petrouleas

Biochemistry 42 ( 10 ) 3045 - 53 2003.3

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

Near-IR (NIR) excitation at liquid He temperatures of photosystem II (PSII) membranes from the cyanobacterium Synechococcus vulcanus or from spinach poised in the S2 state results in the production of a g = 2.035 EPR resonance, reminiscent of metalloradical signals. The signal is smaller in the spinach preparations, but it is significantly enhanced by the addition of exogenous quinones. Ethanol (2-3%, v/v) eliminates the ability to trap the signal. The g = 2.035 signal is identical to the one recently obtained by Nugent et al. by visible-light illumination of the S1 state, and preferably assigned to S1Y(Z*) [Nugent, J. H. A., Muhiuddin, I. P., and Evans, M. C. W. (2002) Biochemistry 41, 4117-4126]. The production of the g = 2.035 signal by liquid He temperature NIR excitation of the S2 state is paralleled by a significant reduction (typically 40-45% in S. vulcanus) of the S2 state multiline signal. This is in part due to the conversion of the Mn cluster to higher spin states, an effect documented by Boussac et al. [Boussac, A., Un, S., Horner, O., and Rutherford, A. W. (1998) Biochemistry 37, 4001-4007], and in part due to the conversion to the g = 2.035 configuration. Following the decay of the g = 2.035 signal at liquid helium temperatures (decay halftimes in the time range of a few to tens of minutes depending on the preparation), annealing at elevated temperatures (-80 degrees C) results in only partial restoration of the S2 state multiline signal. The full size of the signal can be restored by visible-light illumination at -80 degrees C, implying that during the near-IR excitation and subsequent storage at liquid helium temperatures recombination with Q(A-) (and therefore decay of the S2 state to the S1 state) occurred in a fraction of centers. In support of this conclusion, the g = 2.035 signal remains stable for several hours (at 11 K) in centers poised in the S2...Q(A) configuration before the NIR excitation. The extended stability of the signal under these conditions has allowed the measurement of the microwave power saturation and the temperature dependence in the temperature range of 3.8-11 K. The signal intensity follows Curie law temperature dependence, which suggests that it arises from a ground spin state, or a very low-lying excited spin state. The P1/2 (microwave power at half-saturation) value is 1.7 mW at 3.8 K and increases to 96 mW at 11 K. The large width of the g = 2.035 signal and its relatively fast relaxation support the assignment to a radical species in the proximity of the Mn cluster. The whole phenomenology of the g = 2.035 signal production is analogous to the effects of NIR excitation on the S3 state [Ioannidis, N., Nugent, J. H. A., and Petrouleas, V. (2002) Biochemistry 41, 9589-9600] producing an S2'Y(Z*) intermediate. In the present case, the intermediate is assigned to S1Y(Z*). The NIR-induced increase in the oxidative capability of the Mn cluster is discussed in relation to the photochemical properties of a Mn(III) ion that exists in both S2 and S3 states. The EPR properties of the S1Y(Z*) intermediate cannot be reconciled easily with our current understanding of the magnetic properties of the S1 state. It is suggested that oxidation of tyr Z alters the magnetic properties of the Mn cluster via exchange of a proton.

PubMed

researchmap

ATP-induced hexameric ring structure of the cyanobacterial circadian clock protein KaiC. Reviewed International journal

Fumio Hayashi, Hirofumi Suzuki, Ryo Iwase, Tatsuya Uzumaki, Asako Miyake, Jian-Ren Shen, Katsumi Imada, Yukio Furukawa, Koji Yonekura, Keiichi Namba, Masahiro Ishiura

Genes to cells : devoted to molecular & cellular mechanisms 8 ( 3 ) 287 - 96 2003.3

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

BACKGROUND: KaiA, KaiB and KaiC are cyanobacterial circadian clock proteins. KaiC contains two ATP/GTP-binding Walker's motif As, and mutations in these regions affect the clock oscillations. RESULTS: ATP induced the hexamerization of KaiC. The Km value for the ATP for the hexamerization was 1.9 micro m. Triphosphate nucleotides bound to the two Walker's motif As, and their binding functioned cooperatively for the hexamerization. An unhydrolysable substrate, 5'-adenylylimidodiphosphate (AMPPNP), also induced the hexamerization, indicating that nucleotide binding, but not its hydrolysis, is essential for the hexamerization. Mutations in each of the two Walker's motif As that affect the clock phenotype increased the Km value for ATP and inhibited the hexamerization. Thus, the KaiC hexamerization seems to be necessary for its clock function. The KaiC hexamer has the shape of a hexagonal pot with a diameter and height of approximately 100 A and with a relatively large cavity (73 A deep and 18-34 A wide) inside. This pot-shaped structure suggests that KaiC functions in a similar manner to F1-ATPase, helicase or ATP-dependent protease/chaperon, all of which have dynamic activities inside the central cavity of their hexameric rings. CONCLUSION: ATP-induced KaiC hexamerization is necessary for the clock function of KaiC.

PubMed

researchmap

Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-A resolution. Reviewed International journal

Nobuo Kamiya, Jian-Ren Shen

Proceedings of the National Academy of Sciences of the United States of America 100 ( 1 ) 98 - 103 2003.1

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

Photosystem II (PSII) is a multisubunit membrane protein complex performing light-induced electron transfer and water-splitting reactions, leading to the formation of molecular oxygen. The first crystal structure of PSII from a thermophilic cyanobacterium Thermosynechococcus elongatus was reported recently [Zouni, A., Witt, H. T., Kern, J., Fromme, P., Krauss, N., Saenger, W. & Orth, P. (2001) Nature 409, 739-743)] at 3.8-A resolution. To analyze the PSII structure in more detail, we have obtained the crystal structure of PSII from another thermophilic cyanobacterium, Thermosynechococcus vulcanus, at 3.7-A resolution. The present structure was built on the basis of the sequences of PSII large subunits D1, D2, CP47, and CP43; extrinsic 33- and 12-kDa proteins and cytochrome c550; and several low molecular mass subunits, among which the structure of the 12-kDa protein was not reported previously. This yielded much information concerning the molecular interactions within this large protein complex. We also show the arrangement of chlorophylls and cofactors, including two beta-carotenes recently identified in a region close to the reaction center, which provided important clues to the secondary electron transfer pathways around the reaction center. Furthermore, possible ligands for the Mn-cluster were determined. In particular, the C terminus of D1 polypeptide was shown to be connected to the Mn cluster directly. The structural information obtained here provides important insights into the mechanism of PSII reactions.

PubMed

researchmap

Comparison of the structure of the extrinsic 33 kDa protein from different organisms. Reviewed

Akihiko Tohri, Takehiro Suzuki, Satoshi Okuyama, Kei Kamino, Akihiro Motoki, Masahiko Hirano, Hisataka Ohta, Jian-Ren Shen, Yasushi Yamamoto, Isao Enami

Plant & cell physiology 43 ( 4 ) 429 - 39 2002.4

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

The psbO gene encoding the extrinsic 33 kDa protein of oxygen-evolving photosystem II (PSII) complex was cloned and sequenced from a red alga, Cyanidium caldarium. The gene encodes a polypeptide of 333 residues, of which the first 76 residues served as transit peptides for transfer across the chloroplast envelope and thylakoid membrane. The mature protein consists of 257 amino acids with a calculated molecular mass of 28,290 Da. The sequence homology of the mature 33 kDa protein was 42.9-50.8% between the red alga and cyanobacteria, and 44.7-48.6% between the red alga and higher plants. The cloned gene was expressed in Escherichia coli, and the recombinant protein was purified, subjected to protease-treatments. The cleavage sites of the 33 kDa protein by chymotrypsin or V8 protease were determined and compared among a cyanobacterium (Synechococcus elongatus), a euglena (Euglena gracilis), a green alga (Chlamydomonas reinhardtii) and two higher plants (Spinacia oleracea and Oryza sativa). The cleavage sites by chymotrypsin were at 156F and 190F for the cyanobacterium, 159M, 160F and 192L for red alga, 11Y and 151F for euglena, 10Yand 150F for green alga, and 16Y for spinach, respectively. The cleavage sites by V8 protease were at 181E (cyanobacterium), 182E and 195E (red alga), 13E, 67E, 69E, 153D and 181E (euglena), 176E and 180E (green alga), and 18E or 19E (higher plants). Since most of the residues at these cleavage sites were conserved among the six organisms, the results indicate that the structure of the 33 kDa protein, at least the structure based on the accessibility by proteases, is different among these organisms. In terms of the cleavage sites, the structure of the 33 kDa protein can be divided into three major groups: cyanobacterial and red algal-type has cleavage sites at residues around 156-195, higher plant-type at residues 16-19, and euglena and green algal-type at residues of both cyanobacterial and higher plant-types.

PubMed

researchmap

3H1330 X-ray crystallographic study of the icosahedral assembly of light-harvesting chlorophyll a/b protein complex

Hino T., Shen J-R., Kouyama T.

Seibutsu Butsuri 42 ( 2 ) S170 2002

EPR Studies of spin Centers in the even-number oxidation states of Water Oxidizing Center in Photosystem II

Arao S., Yamada S., Kawamori A., Shen J-R., Ionnidis Nikolaos, Petrouleas Vasili

Seibutsu Butsuri 41 S72 2001

Formation mechanism of icosahedral structure of light-harvesting chlorophyll a/b protein complex

Hino T., Kanamori E., Okumura H., Matsui Y., Shen JR., Inoue Y., Kouyama T.

Seibutsu Butsuri 40 S158 2000

Crystallizaion of oxygen-evolving photosystem II complex.

Shen J.-R., Kamiya N.

Seibutsu Butsuri 39 S106 1999

X-ray crystallographic study of spherical assembly of light-harvesting cholorophyll a/b protein complex

Kanamori E., Hino T., Okumura H., Matsui Y., Shen J-R., Inoue Y., Kouyama T.

Seibutsu Butsuri 39 S106 1999

Cloning and expression of genes encoding a 12 kDa protein and cytochrome c(550), two extrinsic proteins of PSII, from a red alga Cyanidium caldarium Reviewed

H Ohta, A Okumura, T Katoh, Shen, JR, M Kamo, Enami, I

PHOTOSYNTHESIS: MECHANISMS AND EFFECTS, VOLS I-V 2979 - 2982 1998

Possible functional differences between dimer and monomer of photosystem II complex Reviewed

Shen, JR

PHOTOSYNTHESIS: MECHANISMS AND EFFECTS, VOLS I-V 941 - 944 1998

Topological analysis of PS II reaction center using monoclonal antibodies Reviewed

Tatsuya Tomo, Kenji Ogawa, Yorinao Inoue, Jian-Ren Shen

Photosynthesis: Mechanisms and Effects 2 993 - 996 1998

Functional characterization of Synechocystis sp. PCC 6803 delta psbU and delta psbV mutants reveals important roles of cytochrome c-550 in cyanobacterial oxygen evolution Reviewed

SHEN J. -R.

Biochemistry 37 1551 - 1558 1998

Identification of domains on the 43KDa chlorophyll-carring protein(CP43)that are shielded from tryptic attack by binding of the extrinsic 33KDa protein with photosystem II complex Reviewed

Enami, I, Tohri, A, Kamo, M, Ohta, H, Shen, J. R

Biochim Biophys Acta 1320 17 - 26 1997.5

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

The structural association of the spinach 33 kDa extrinsic protein with the 43 kDa chlorophyll-carrying protein (CP43) in oxygen-evolving photosystem II (PS II) complexes was investigated by comparing the peptide mappings and N-terminal sequences of the trypsin-digested products of NaCl-washed PS II membranes, which bind the 33 kDa protein, with those of CaCl2-washed PS II membranes, which lack the 33 kDa protein. (1) Peptide from N-terminus to Arg26 of CP43, which is exposed to stromal side, was digested in both PS II membranes, independent of binding of the 33 kDa protein. (2) Peptide bond of Arg357-Phe358 located in the large extrinsic loop E of CP43, which is exposed to lumenal side, was cleaved by trypsin in CaCl2-washed PS II membranes but not in NaCl-washed PS II membranes. This indicates that the region around Arg357-Phe358 in loop E of CP43 is shielded from tryptic attack by binding of the 33 kDa protein to PS II. (3) Trypsin treatment of CaCl2-washed PS II membranes also cleaved peptide bond between Lys457 and Gly458 in C-terminal region of CP43, while no cleavage of this region was detected by trypsin treatment of NaCl-washed PS II membranes. This implies that a conformational change of the C-terminal region of CP43 which is exposed to stromal side occurred upon removal of the 33 kDa protein, which makes the C-terminal region accessible to trypsin. (4) Release of peptide from Gln60 to C-terminus of the alpha-subunit of cytochrome b-559 was detected only in trypsin treatment of CaCl2-washed PS II membranes, indicating that the C-terminal region of this subunit is shielded from tryptic attack by binding of the 33 kDa protein. (5) The PS II membranes, in which Arg357-Phe358, Lys457-Gly458 of CP43 and the C-terminal part of the cytochrome b-559 alpha-subunit had been cleaved by trypsin, was no longer able to bind the 33 kDa protein. This strongly suggests that a domain in loop E of CP43 and/or the C-terminal region of the cytochrome b-559 alpha-subunit are necessary for binding of the extrinsic 33 kDa protein to PS II.

DOI： 10.1016/S0005-2728(97)00005-4

PubMed

CiNii Article

researchmap

Identification of domains on the extrinsic 33KDa protein possibly involved in electrostatic interaction with photosystem II complex by means of chemical modification Reviewed

Miura, T, Shen, J. R, Takahashi, S, Kamo, M, Nakamura, E, Ohta, H, Kamei, A, Inoue, Y, Domae, N, Takio, K, Nakazato, K, Enami, I

J Biol Chem 272 ( 6 ) 3788 - 3798 1997.2

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

The extrinsic 33-kDa protein of photosystem II (PSII) was modified with various reagents, and the resulting proteins were checked for the ability to rebind to PSII and to reactivate oxygen evolution. While modification of more than eight carboxyl groups of aspartyl and glutamyl residues with glycine methyl ester did not affect the rebinding and reactivating capabilities, modification of amino groups of lysyl residues with either N-succinimidyl propionate or 2, 4,6-trinitrobenzene sulfonic acid or modification of guanidino groups of arginyl residues with 2,3-butanedione resulted in a loss of rebinding and reactivating capabilities of the 33-kDa protein. Moreover, the number of lysyl and arginyl residues susceptible to modification was significantly decreased when the protein was bound to PSII as compared with when it was free in solution, whereas the number of carboxyl groups modified was little affected. These results suggested that positive charges are important for the electrostatic interaction between the extrinsic 33-kDa protein and PSII intrinsic proteins, whereas negative charges on the protein do not contribute to such interaction. By a combination of protease digestion and mass spectroscopic analysis, the domains of lysyl residues accessible to N-succinimidyl propionate or 2,4, 6-trinitrobenzene sulfonic acid modification only when the 33-kDa protein is free in solution were determined to be Lys4, Lys20, Lys66-Lys76, Lys101, Lys105, Lys130, Lys159, Lys186, and Lys230-Lys236. These domains include those previously reported accessible to N-hydroxysuccinimidobiotin only in solution (Frankel and Bricker (1995) Biochemistry 34, 7492-7497), and may be important for the interaction of the 33-kDa protein with PSII intrinsic proteins.

DOI： 10.1074/jbc.272.6.3788

PubMed

CiNii Article

researchmap

Isolation and characterization of photosystem II core complex from the red alga Cyanidium caldarium : association of cytochrome c-550 and 12kDa protein with the complex Reviewed

Enami, I, Murayama, H, Ohta, H, Kamo, M, Nakazato, K, Shen, J. R

Biochim Biophys Acta 1232 208 - 216 1995.12

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

A Photosystem II (PS II) complex was purified from an acidophilic as well as a thermophilic red alga, Cyanidium caldarium. The purified PS II complex was essentially devoid of phycobiliproteins and other contaminating components, and showed a high oxygen-evolving activity of 2375 mumol O2/mg Chl per h using phenyl-p-benzoquinone as the electron acceptor. The expression of this high activity did not require addition of exogenous Ca2+, although EDTA reduced the activity by 40%. This effect of EDTA can be reversed not only by Ca2+ but also by Mg2+; a similar Mg2+ effect has been observed in purified cyanobacterial PS II but not in higher plant PS II. Immunoblotting analysis indicated the presence of major intrinsic polypeptides commonly found in PS II from cyanobacteria and higher plants as well as the extrinsic 33 kDa protein. Antibodies against the extrinsic 23 and 17 kDa proteins of higher plant PS II, however, did not crossreact with any polypeptides in the purified PS II, indicating the absence of these proteins in the red alga. In contrast, two other extrinsic proteins of 17 and 12 kDa were present in the red algal PS II; they were released by 1 M Tris or Urea/NaCl treatment but not by 1 M NaCl. The 17 kDa polypeptide was identified to be cytochrome c-550 from heme-staining, immunoblot analysis and N-terminal amino acid sequencing, and the 12 kDa protein was found to be homologous to the 12 kDa extrinsic protein of cyanobacterial PS II from its N-terminal sequence. These results indicate that PS II from the red alga is closely related to PS II from cyanobacteria rather than to that from higher plants, and that the replacement of PS II extrinsic cytochrome c-550 and the 12 kDa protein by the extrinsic 23 and 17 kDa proteins occurred during evolution from red algae to green algae and higher plants.

DOI： 10.1016/0005-2728(95)00122-0

PubMed

CiNii Article

researchmap

An independent role of cytochrome c-550 in cyanobacterial photosystem II as revealed by double-deletion mutagenesis of the psbO and psbV genes in Synechocystis sp. PCC 6803 Reviewed

SHEN J.-R.

Biochemistry 34 12661 - 12668 1995

CAUSE FOR DARK, CHILLING-INDUCED INACTIVATION OF PHOTOSYNTHETIC OXYGEN-EVOLVING SYSTEM IN CUCUMBER LEAVES Reviewed

SHEN, JR, TERASHIMA, I, S KATOH

PLANT PHYSIOLOGY 93 ( 4 ) 1354 - 1357 1990.8

ISOLATION AND CHARACTERIZATION OF PHOTOSYSTEM-II COMPLEXES WHICH LACK LIGHT-HARVESTING CHLOROPHYLL-A/B PROTEINS BUT RETAIN 3 EXTRINSIC PROTEINS RELATED TO OXYGEN EVOLUTION FROM SPINACH Reviewed

ENAMI, I, K KAMINO, SHEN, JR, K SATOH, S KATOH

BIOCHIMICA ET BIOPHYSICA ACTA 977 ( 1 ) 33 - 39 1989.10

NEAREST NEIGHBOR RELATIONSHIPS AMONG CONSTITUENT PROTEINS OF OXYGEN-EVOLVING PHOTOSYSTEM-II MEMBRANES - BINDING AND FUNCTION OF THE EXTRINSIC 33 KDA PROTEIN Reviewed

ENAMI, I, T MIYAOKA, Y MOCHIZUKI, SHEN, JR, K SATOH, S KATOH

BIOCHIMICA ET BIOPHYSICA ACTA 973 ( 1 ) 35 - 40 1989.1

　 PREV - NEXT 　

< SHEN Jian-Ren >

Papers - SHEN Jian-Ren