Faculty Profiles - SHEN Jian-Ren

Structural basis for silicic acid permeation mechanism by rice silicic acid channel

齊藤恭紀, 三谷(上野)奈見季, 斉藤圭亮, 斉藤圭亮, 松木謙悟, HUANG Sheng, YANG Lingli, 山地直樹, 石北央, 石北央, SHEN Jian-Ren, SHEN Jian-Ren, MA Jian Feng, 菅倫寛, 菅倫寛, 菅倫寛

日本分子生物学会年会プログラム・要旨集(Web) 44th 2021

クライオ電子顕微鏡単粒子解析による光合成超分子複合体の構造解析 Reviewed

宮崎直幸, 長尾遼, 加藤公児, 沈建仁, 秋田総理

光合成研究 28 112 - 118 2018

The crystal structure of Deg9 reveals a novel octameric-type HtrA protease. International journal

Min Ouyang, Xiaoyi Li, Shun Zhao, Hua Pu, Jianren Shen, Zach Adam, Tim Clausen, Lixin Zhang

Nature plants 3 ( 12 ) 973 - 982 2017.12

Language：English Publisher：NATURE PUBLISHING GROUP

The high temperature requirement A (HtrA) proteases (also termed Deg proteases) play important roles in diverse organisms by regulating protein quality and quantity. One of the 16 Arabidopsis homologs, Deg9, is located in the nucleus where it modulates cytokinin- and light-mediated signalling via degrading the ARABIDOPSIS RESPONSE REGULATOR 4 (ARR4). To uncover the structural features underlying the proteolytic activity of Deg9, we determined its crystal structure. Unlike the well-established trimeric building block of HtrAs, Deg9 displays a novel octameric structure consisting of two tetrameric rings that have distinct conformations. Based on the structural architecture, we generated several mutant variants of Deg9, determined their structure and tested their proteolytic activity towards ARR4. The results of the structural and biochemical analyses allowed us to propose a model for a novel mechanism of substrate recognition and activity regulation of Deg9. In this model, protease activation of one tetramer is mediated by en-bloc reorientation of the protease domains to open an entrance for the substrate in the opposite (inactive) tetramer. This study provides the structural basis for understanding how the levels of nuclear signal components are regulated by a plant protease.

DOI： 10.1038/s41477-017-0060-2

PubMed

X線自由電子レーザーを利用した光化学系IIの原子構造と水分解反応機構の解明

Molecular mechanism of photosynthetic water-splitting reaction

262 400 - 406 2017

菅倫寛, 秋田総理, 沈建仁

レーザー学会誌「レーザー研究」 45 ( 8 ) 475 - 479 2017

植物光化学系I-集光性アンテナI 超複合体におけるエネルギー伝達の構造基盤

菅倫寛, 沈建仁

SPring-8/SACLA利用者情報 22 ( 3 ) 233 - 237 2017

Structural basis for the photosynthetic water-splitting/oxygenevolving reaction

Fusamichi Akita, Michihiro Suga, Jian-Ren Shen

Seikagaku 89 ( 5 ) 699 - 709 2017

シリアルフェムト秒結晶解析により明らかにした光化学系IIの反応中間体の構造と酸素発生機構

菅倫寛, 秋田総理, 菅原道泰, 久保稔, 岩田想, 沈建仁

日本放射光学会誌 30 ( 5 ) 228 - 234 2017

光合成水分解反応の分子機構

沈建仁

医学のあゆみ 262 400 - 406 2017

放射光X 線結晶構造解析による光合成・光化学系IIの水分解・酸素発生機構の解明

神谷信夫, 沈建仁

日本結晶学会誌 59 ( 2 ) 1 - 8 2017

Elucidation of the water-splitting and oxygen evolution mechanism of photosynthetic photosystem II by synchrotron radiation X-ray crystallography

Journal of the Japanese Crystallography Society 59 1 - 8 2017

Structural basis for the photosynthetic water-splitting/oxygen-evolving reaction

Journal of the Japanese Biochemical Society 89 699 - 709 2017

Toward artificial photosynthesis -- Synthesis of model compounds of photosynthetic water-splitting catalyst

Chemistry 72 46 - 50 2016

フェムト秒Ｘ線レーザーを用いて決定した光化学系II複合体の無損傷構造

菅倫寛, 秋田総理, 沈建仁, 山本雅貴, 吾郷日出夫

日本結晶学会誌 58 ( 3 ) 126 - 132 2016

Structural biology of photosynthesis

Biophysics 56 ( 2 ) 79 - 86 2016

Structural Biology of Photosynthetic Systems

SHEN Jian-Ren, AKITA Fusamichi, SUGA Michihiro

Seibutsu Butsuri 56 ( 2 ) 79 - 86 2016

Language：Japanese Publisher：The Biophysical Society of Japan General Incorporated Association

Oxygenic photosynthesis synthesizes sugars from water and carbon dioxide using light energy from the sun, thereby converts light energy into chemical energy and provides oxygen for aerobic life on the earth. The light-harvesting, electron transfer, and water-splitting reactions of photosynthesis are catalyzed by two large membrane-protein complexes photosystem II (PSII) and photosystem I (PSI). Through high-resolution crystal structural analysis by synchrotron X-rays as well as femtosecond X-ray free electron lasers, the mechanisms of these reactions have become understandable at the atomic level. Here we review the recent progresses in analyzing the structures of PSII and PSI as well as their functional implications.

DOI： 10.2142/biophys.56.079

PsbA3-D1 タンパク質を発現する光化学系II 複合体の結晶構造

Other Link： https://jlc.jst.go.jp/DN/JLC/20021928091?from=CiNii

SACLAが解き明かす光合成の仕組み

沈建仁

月刊 OPTRONICS 409 31 - 35 2016

光合成水分解触媒のモデル化合物の合成ー人工光合成の実現に向けて

沈建仁

化学 72 46 - 50 2016

Damage-free structure of photosystem II determined by femtosecond X-ray free electron laser

Journal of the Japanese Crystallography Society 58 ( 3 ) 126 - 132 2016

Mechanism of photosynthetic water-splitting revealed by SACLA

OPTRONICS 409 31 - 35 2016

X線自由電子レーザーで決定した光化学系II複合体の無損傷結晶構造と水分解反応機構

放射光学会誌 28 177 - 181 2015

Damage-free structure of photosystem determined by X-ray free electron laser and the mechanism of water-splitting

28 177 - 181 2015

鵜飼奈津美, 菅倫寛, 杉浦美羽

光合成研究 25 ( 1 ) 22 - 27 2015

高等植物の光化学系I-光捕集アンテナI超複合体におけるエネルギー伝達経路の構造基盤

ライフサイエンス新着論文レビュー 2015

Protein 3D structures -- Photosystem II complex

55 226 2015

Crystal structure of Photosystem II with the D1 protein encoded by the psbA3 gene

Photosynthesis Research 25 22 - 27 2015

タンパク質立体構造散歩光化学系II複合体

生物物理 55 226 2015

Large-scale QM/MM calculations of hydrogen bonding networks for proton transfer and water inlet channels for water oxidation—Theoretical system models of the oxygen-evolving complex of Photosystem II

Mitsuo Shoji, Hiroshi Isobe, Shusuke Yamanaka, Yasufumi Umena, Keisuke Kawakami, Nobuo Kamiya, Jian-Ren Shen, Takahito Nakajima, Kizashi Yamaguchi

Advances in Quantum Chemistry 70 325 - 413 2015

The mystery of photosynthesis revealed by crystal structural analysis

7 22 - 25 2014

結晶構造解析が解き明かす光合成の謎

ミルシル 7 22 - 25 2014

フェムト秒X線レーザーにより明らかにされた1.95Å分解能における光化学系II複合体の天然状態の構造

ライフサイエンス新着論文レビュー 2014

光化学系II複合体の高分解能構造と水分解反応の機構

実験医学増刊号「構造生命科学で何がわかるのか，何ができるのか」 32 142 - 147 2014

Native structure of photosystem II at 1.95 A resolution revealed by femtosecond X-ray laser

2014

Crystal structure of Extrinsic protein in photosystem II Reviewed

R. Nagao, M. Suga, A. Niikura, A. Okumura, F.H.M. Koua, T. Suzuki, T. Tomo, I. Enami, J.R. Shen

2013.9

26aXC-1 Light-harvesting processes of photosynthetic reaction centers of plants : toward its understanding based on the structural information 2

Shibata Y., Nishi S., Kawakami K., Shen J. R., Renger Thomas

Meeting abstracts of the Physical Society of Japan 68 ( 1 ) 414 - 414 2013.3

光合成の水分解・酸素発生機構の解明に向けて

神谷信夫, 川上恵典, 梅名泰史, 沈建仁

放射光学会誌 26 3 - 10 2013

High resolution structure of photosystem II and the mechanism of water-splitting

Jian-Ren Shen, Yasufumi Umena, Keisuke Kawakami, Nobuo Kamiya

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS 1817 S2 - S3 2012.10

Mechanism of photosynthetic water-splitting and oxygen evolution based on high resolution structure of photosystem II

Jian-Ren Shen

67 15 - 19 2012

光合成最大の謎を解明

沈建仁

教科研究理科 195 12 - 16 2012

高分解能結晶構造に基づく光合成水分解・酸素発生の分子機構

沈建仁

酵素工学ニュース 67 15 - 19 2012

Mechanism of Photosynthetic Water-splitting Based on the High Resolution Structure of Photosystem II

SHEN Jian-Ren, UMENA Yasufumi, KAWAKAMI Keisuke, KAMIYA Nobuo

Seibutsu Butsuri 52 ( 3 ) 140 - 143 2012

Language：Japanese Publisher：The Biophysical Society of Japan General Incorporated Association

Photosystem II (PSII) is a membrane-protein complex consisting of 17 trans-membrane subunits and 3 peripheral, extrinsic subunits with a total molecular mass of 350 kDa for a monomer. PSII performs a series of light-induced electron transfer reactions, leading to the conversion of light energy into biologically useful chemical energy, coupled with this is the splitting of water and generation of molecular oxygen. Both the chemical energy converted and molecular oxygen generated by PSII are indispensible for sustaining life on the earth; thus PSII is an extremely important protein complex. We have succeeded in crystallizing the PSII complex at a resolution of 1.9 Å, and analyzed its structure. Here we describe the structure of PSII, in particular the Mn₄CaO₅-cluster, which is the catalytic center of water-splitting, analyzed at the atomic resolution. Based on these, we discuss the possible mechanisms of light-induced water-splitting and its implications in artificial photosynthesis.<br>

DOI： 10.2142/biophys.52.140

Mechanism of photosynthetic water-splitting based on high resolution structure of photosystem II

Other Link： https://jlc.jst.go.jp/DN/JALC/10000488562?from=CiNii

Running on sun

M. M, Najafpour, J. Barber, J-R. Shen, G. F. Moore, Govindjee

Chemistry World 2012 ( November ) 43 2012

Jian-Ren Shen, Yasufumi Umena, Keisuke Kawakami, Nobuo Kamiya

Biophysics 52 ( 3 ) 140 - 143 2012

Language：Japanese Publisher：The Biophysical Society of Japan General Incorporated Association

DOI： 10.2142/biophys.52.140

Other Link： https://jlc.jst.go.jp/DN/JALC/10000488562?from=CiNii

Elucidating the largest mystery of photosynthesis

Jian-Ren Shen

195 12 - 16 2012

光化学系IIにおける酸素発生中心Mnクラスターの多周波EPR研究

松岡秀人, SHEN Jian-Ren, 伊東信哉, 古川貢, 中村敏和, 山内清語

電子スピンサイエンス学会年会講演要旨集 51st 2012

25pGP-7 Densily functional study of electronic structures of the manganese cluster in photosystem II

Yamanaka S., Kanda K., Umena Y., Kawakami K., Shen J.-R., Kamiya N., Okumura M., Nakamura H., Yamaguchi K.

Meeting abstracts of the Physical Society of Japan 66 ( 1 ) 378 - 378 2011.3

25pGP-2 Atomic resolution structure of photosystem II that enables photosynthetic oxygen evolution

Shen Jian-Ren, Umena Yasufumi, Kawakami Keisuke, Kamiya Nobuo

Meeting abstracts of the Physical Society of Japan 66 ( 1 ) 376 - 376 2011.3

27pHC-12 Simulation of time-resolved fluorescence spectrum of photosystem II on the basis of structural information

Shibata Y., Nishi S., Noji T., Kawakami K., Shen J. R., Renaer Thomas

Meeting abstracts of the Physical Society of Japan 66 ( 1 ) 794 - 794 2011.3

光合成水分解・酸素発生を可能にする光化学系IIの原子構造

沈建仁

光合成研究 21 72 - 79 2011

Location and function of chloride ions in oxygen-evolving photosystem II revealed by X-Ray crystallography

Jian-Ren Shen

SPring-8 Research Frontiers 2009 22 - 23 2010

系II複合体の精製法

沈建仁, 榎並勲

低温科学 67 275 - 283 2009

電子伝達活性

沈建仁

低温科学 67 551 - 560 2009

光化学系IIの例から見る膜タンパク質複合体の結晶化と構造解析

沈建仁, 川上恵典

光合成研究 19 19 - 25 2009

単結晶光化学系II複合体の高周波CW/パルスESR研究

松岡秀人, SHEN Jian-Ren, 西山圭, 大庭裕範, 山内清語, 古川貢, 中村敏和, 河盛阿佐子

電子スピンサイエンス学会年会講演要旨集 48th 2009

A brief introduction of Kimiyuki Satoh TRIBUTE

Isao Enami, Jian-Ren Shen

PHOTOSYNTHESIS RESEARCH 98 ( 1-3 ) 7 - 11 2008.10

Language：English Publisher：SPRINGER

In this Special Issue of Photosynthesis Research (Structure, Function, and Dynamics of Photosystem II) in honor of Kimiyuki Satoh and Thomas J. Wydrzynski, we present here a brief introduction to the scientific career and achievements of Kimiyuki Satoh, a great scientist with numerous important contributions in photosynthesis research, especially in the field of photosystem II.

DOI： 10.1007/s11120-008-9338-6

光化学系2複合体の構造と機能 (生命秩序を担う生体超分子) -- (超分子による生体エネルギー・物質変換とその制御)

Purification and crystallization of photosystem II dimmer complex

Hideyuki Adachi, Isao Enami, Takahiro Henmi, Nobuo Kamiya, Jian-Ren Shen

Photosynthesis. Energy from the Sun 1 351 - 356 2008

光化学系II反応中心の多周波EPR研究

松岡秀人, SHEN Jian-Ren, 西山圭, 古川貢, 中村敏和, 山内清語, 河盛阿佐子

電子スピンサイエンス学会年会講演要旨集 47th 2008

Purification and crystallization of photosystem II complex from a red alga Cyanidium Caldarium.

Hideyuki Adachi, Isao Enami, Takahiro Henmi, Nobuo Kamiya, Jian-Ren Shen

PLANT AND CELL PHYSIOLOGY 48 S98 - S98 2007

Crystal structure analysis of a mutant photosystemII complex lacking PsbM from Thermosynechococcus vulcanus.

Yosuke Kawabata, Takahiro Henmi, Masako Iwai, Takashi Suemasu, Keisuke Kawakami, Chika Aoyama, Masahiko Ikeuchi, Nobuo Kamiya, Jian-Ren Shen

PLANT AND CELL PHYSIOLOGY 48 S97 - S97 2007

Roles of lipids in photosystem II from cyanobacteria

J Leng, Sakurai, I, H Wada, Shen, JR

PLANT AND CELL PHYSIOLOGY 47 S162 - S162 2006

Current status and prospects of PSII structure analysis

Shen, JR, H Naitow, M Furuse, S Saijo, A Ohkuma, K Kawakami, T Henmi, N Kamiya

PLANT AND CELL PHYSIOLOGY 47 S9 - S9 2006

神谷信夫, 沈建仁

蛋白質核酸酵素 50 ( 10 ) 1174 - 1179 2005.8

光化学系II複合体の構造と機能

神谷信夫, 沈建仁

蛋白質核酸酵素 50, 1174-1179. 2005

W-band EPR studies of Mn-cluster in the S-0 and S-2 states of Cyanobacterial single crystals.

A Kawamori, Shen, JR, K Furukawa, E Matsuoka, T Kato

PLANT AND CELL PHYSIOLOGY 45 S81 - S81 2004

Thermodynamic and kinetic analysis of unfolding of P23k protein isolated from spinach photosystem II

CY Tan, CH Xu, Shen, JR, S Sukuma, Y Yamamoto, C Balny, KC Ruan

ACTA BIOCHIMICA ET BIOPHYSICA SINICA 35 ( 7 ) 677 - 681 2003.7

Language：Chinese Publisher：SHANGHAI INST BIOCHEMISTRY, ACADEMIA SINICA

The unfolding of 23kD (P23k) protein isolated from spinach photosystem II particle was studied by high pressure and fluorescence spectroscopy. The thermal equilibrium study indicated that the protein could be totally unfolded by 180 or 160 MPa at 20 degreesC and 3 degreesC, respectively. The standard free energy and standard volume change of the protein for unfolding at 20 degreesC is 23.45 kJ/mol and - 150.3 ml/mol, respectively. Kinetics study indicated that at 20 degreesC the activation volume for unfolding, Delta V-u(double dagger), was negative ( - 66.2 ml/mol), meanwhile the activation volume for folding, Delta V-f(double dagger), was positive (84.1 ml/mol). The rate constants for folding and unfolding (K-0f, K-0u) were 1.87 s(-1) and 1.3 x 10(-4) s(-1), respectively, these results provide some clues to explain why the protein is so sensitive to pressure.

Functional Analysis of psbV and a Novel c-type Cytochrome Gene psbV2 of the Thermophilic Cyanobacterium Thermosynechococcus elongatus Strain BP-1

Crystal structure analysis of photosystem II from Thermosynechococcus vulcanus

Kamiya N, Shen J.-R

PS2001 Proceedings, 12th International Congress on Photosynthesis 2002

Cross-reconstitution of cytochrome c550 and 12 kDa protein between cyanobacterial and red algal PSII.

Enami I, Iwai M, Akiyama A, Nakata Y, Ohta H, Shen J.-R

PS2001 Proceedings, 12th International Congress on Photosynthesis 2002

Distribution of extrinsic proteins among various organisms as an index of evolution of oxygen-evolving PSII.

Nakata Y, Satoh A, Nakamura K, Okumura A, Ohta H, Shen J.-R, Enami I

PS2001 Proceedings, 12th International Congress on Photosynthesis 2002

Reconstitution of the 23 and 17 kDa proteins with spinach PSII which had been exchanged for the 33 kDa protein from different plant species.

Suzuki T, Akiyama A, Iwai M, Tohri A, Tomo T, Ohta H, Shen J.-R, Enami I

PS2001 Proceedings, 12th International Congress on Photosynthesis 2002

Evolution of oxygen-evolving PSII in view of extrinsic proteins among various organisms. II

Y Nakada, H Ohta, Shen, JR, Enami, I

PLANT AND CELL PHYSIOLOGY 43 S63 - S63 2002

KATOH Hiroshi, ITOH Suwako, SHEN Jian-ren, IKEUCHI Masahiko

Plant and Cell Physiology 42 ( 6 ) 599 - 607 2001.6

紅藻チアニジウムの酸素発生標品に存在する表在性20kDa蛋白のクローニングと発現

太田尚孝, 上野匡司, 沈建仁, 加茂政晴, 榎並勲

日本植物生理学会年会要旨集 40th 218 2000.3

Crystallization and the crystal properties of the oxygen-evolving photosystem II from Synechococcus vulcanus.

Shen J.-R, Kamiya N

Biochemistry 2000

27aN-1 Spherical assembly of the Light Harvesting Chlorophyll a/b protein complex in the octahedral crystal

HINO T, KANAMORI E, GOTO T, TAKEDA K, SATO H, SHEN J.R, INOUE Y, KOUYAMA T

Meeting abstracts of the Physical Society of Japan 54 ( 2 ) 318 - 318 1999.9

CLONING OF THE GENES FOR CYTOCHROME C550 AND A C550-LIKE PROTEIN FROM THE THERMOPHILIC CYANOBACTERIUM Synechococcus elongatus.

KATOH Hiroshi, ITOH Suwako, SHEN Jian-Ren, IKEUCHI Masahiko

40 s34 - s34 1999.3

COMPARISON OF BINDING AND FUNCTIONAL PROPERTIES OF Cyt c550 FROM CYANOBCTERIAL PSII WITH THOSE OF Cyt c550 FROM RED ALGAL PSII

IWAI Masako, AKIYAMA Ai, OHTA Hisataka, SHEN Jian-Ren, ENAMI Isao

40 s33 - s33 1999.3

CLONING OF THE GENE ENCODING THE PSII EXTRINSIC 33 kDa PROTEIN FROM A RED ALGA

OKUYAMA Satoshi, OHTA Hisataka, SHEN Jian-Ren, ENAMI Isao

40 s30 - s30 1999.3

THE STRUCTURE OF PHOTOSYSTEM II IN THYLAKOID MEMBRANES IMPLICATED FROM THE FUNCTIONAL DIFFERENCES OF ISOLATED PSII MONOMER AND DIMER

SHEN Jian-Ren

40 s33 - s33 1999.3

COMPARISON OF PSII CRYSTALS BETWEEN HIGHER PLANTS AND CYANOBACTERIA

SHEN Jian-Ren, AOYAMA Hiroshi, INOUE Yorinao, NOBUO Kamiya

40 s33 - s33 1999.3

CROSS-RECONSTITUTION OF FOUR EXTRINSIC PROTEINS FROM A RED ALGA WITH HIGHER PLANT AND CYANOBACTERIAL PSII

Isao Enami, Shizue Yoshihara, Hisataka Ohta, Jian-Ren Shen

Photosynthesis:Mechanisms and Effects Vol 2 1435 - 1438 1999

好熱性シアノバクテリアSynechococcuselongatusのチトクロムc550およびc550類似タンパク質の遺伝子のクローニング

加藤浩, 伊藤須和子, 沈建仁, 池内昌彦

日本植物生理学会年会要旨集 39th 1999

X-ray crystallographic study of ligh-harvesting chlorophyll a/b protein complex

Hino T., Sato H., Iwanaga S., Shen J-R., Inoue Y., Kouyama T.

Biophysics 38 ( 2 ) S15 1998.9

高等植物, 紅藻, ラン色細菌の系II表在性蛋白のCross-Reconstitution

榎並勲, 吉原静恵, 岩井雅子, 秋山愛, 太田尚孝, 沈建仁

日本植物学会大会研究発表記録 = Proceedings of the annual meeting of the Botanical Society of Japan 62 118 - 118 1998.9

紅藻チアニジウムの酸素発生標品に存在する表在性蛋白チトクロームc‐550のクローニングと発現

太田尚孝, 加藤宝, 奥村彰槻, 沈建仁, 加茂政晴, 榎並勲

日本植物生理学会年会要旨集 38th(1998) 75 1998.5

CROSS-RECONSTITUTION OF FOUR EXTRINSIC PROTEINS FROMA RED ALGA TO HIGHER PLANT PSII

YOSHIHARA Shizue, OHTA Hisataka, SHEN Jian-Ren, ENAMI Isao

39 S15 - S15 1998.5

CONSTRUCTION OF MONOCLONAL ANTIBODIES AGAINST PSII REACTION CENTER PROTEINS AND THE USE OF THEM TO ANALYZE THE TOPOLOGY OF PSII REACTION CENTER

TOMO Tatsuya, SHEN Jian-Ren, OGAWA Kenji, INOUE Yorinao

39 S12 - S12 1998.5

Vesicular Assembly of Membrane Proteins

HINO T., TAKEDA K., SATO H., SAKURAI I., SHEN Jr, INOUE Y., OKADA T., KOUYAMA T.

Meeting abstracts of the Physical Society of Japan 53 ( 1 ) 731 - 731 1998.3

Comparative studies of three-dimensional crystals of light-harvesting chlorophyll a/b proteincomplex and bacteriorhodopsin

HINO T., TAKEDA K., SHEN J-R., INOUE Y., SAKURAI I., OKADA T., KOUYAMA T.

Biophysics 37 S126 1997.10

CLONING AND EXPRESSION OF A cDNA ENCODING THE EXTRINSIC 12 KDA PROTEIN INVOLVED IN OXYGEN-EVOLVING PS II COMPLEX FROM A RED ALGA Cyanidium caldarium

OKUMURA Akinori, OHTA Hisataka, SHEN Jian-Ren, KAMO Masaharu, ENAMI Isao

38 s25 1997.3

CRYSTALLIZATION OF OXYGEN-EVOLVING PSII COMPLEX : EFFECTS OF DETERGENTS

SHEN Jian-Ren, AOYAMA Hiroshi, INOUE Yorinao, KAMIYA Nobuo

38 s22 1997.3

IDENTIFICATION OF LYS RESIDUES ON THE EXTRINSIC 33KDA PROTEIN INVOLVED IN ELECTROSTATIC INTERACTION WITH PSII COMPLEX BY CHEMICAL MODIFICATION WITH NSP

KAMEI Ayako, SHEN Jian-Ren, OHTA Hisataka, DOMAE Naoshi, TAKIO Koji, INOUE Yorinao, ENAMI Isao

38 s25 1997.3

RECONSTITUTION OF THREE EXTRINSIC PROTEINS, THE 20KDA-, 12KDA- PROTEINS AND CYTC-550, IN OXYGEN-EVOLVING PSII COMPLEX FROM A RED ALGA, Cyanidium caldarium

KIKUCHI Sanae, FUKUDA Tetuya, OHTA Hisataka, SHEN Jian-Ren, ENAMI Isao

38 s25 1997.3

Analysis of the psbU gene encoding the 12-kDa extrinsic protein of Photosystem II and studies on its role by deletion mutagenesis in Synechocystis sp. PCC 6803

SHEN J.-R.

J. Biol. Chem. 272 17821 - 17826 1997

CLONING AND DIRECTED MUTAGENESIS OF THE GENE CODING FOR A 12 kDa PHOTOSYSTEM II EXTRINSIC PROTEIN FROM Synechocystis sp. PCC 6803

SHEN Jian-Ren, INOUE Yorinao

37 36 - 36 1996.3

Chemical crosslinking studies ofextrinsic proteins in cyanobacterial photosystem II

HAN Kab-Cho, SHEN Jian-Ren, IKEUCHI Masahiko, INOUE Yorinao

36 S92 1995.3

The role of cytochrome c-550 as studied through reverse genetics and mutant characterization in Synechocystis sp. PCC 6803

SHEN J. R.

J. Biol. Chem. 270 6901 - 6907 1995

Binding and functional properties of two new extrinsic components, cytchrome c-550 and 12 kDa protein, in cyanobacterial photosystem II

SHEN J. -R.

Biochemistry 32 1925 - 1932 1993

Cellular localization of cytochrome c550. Its specific_association with cyanobacterial photosystem II

SHEN J. -R.

J. Biol. Chem. 268 20408 - 20413 1993

Stoichiometric association of extrinsic cytochrome c_<550> and 12 kDa protein with a highly purified oxygen-evolving photosystem II core complex from Synechococcus vulcanus

SHEN J. -R.

FEBS Lett. 301 145 - 149 1992

Low pH-Induced Dissociation of Three Extrinsic Proteins from O_2-Evolving Photosystem II :

Shen Jian-Ren, Inoue Yorinao

Plant and cell physiology 32 ( 3 ) 453 - 457 1991

Language：English Publisher：Japanese Society of Plant Physiologists

Three extrinsic proteins involved in oxygen evolution reversibly dissociated from Photo-system II (PS II) membranes at acidic pHS showing distinctly different pH dependencies. The pHS for half dissociation of 17, 23 and 33 kDa extrinsic proteins were determined to be 5.0, 4.1 and 3.6, respectively. The half dissociation pHS Of 17 and 23 kDa proteins were much lower than their respective isoelectric points, while that for 33 kDa protein was close to its isoelectric point. It was suggested that protonation of the negatively charged binding domain on membrane proteins causes dissociation of the former two extrinsic proteins, whereas protonation of the extrinsic protein itself is responsible for the dissociation of 33 kDa protein. Based on these, features of low pH-induced dissociation of extrinsic proteins and Mn from PS II were discussed.

Inactivation and Calcium-Dependent Reactivation of Oxygen Evolution in Photosystem II Preparations Treated at pH 3.0 or with High Concentrations of NaCl :

Other Link： https://projects.repo.nii.ac.jp/?action=repository_uri&item_id=181397

Shen Jian-Ren, Katoh Sakae

Plant and cell physiology 32 ( 3 ) 439 - 446 1991

Language：English Publisher：Japanese Society of Plant Physiologists

A brief treatment at pH 3.0 of Photosystem II (PS II) membranes containing two bound Ca^<2+> from rice resulted in strong suppression of oxygen evolution concomiiant with extraction of one Ca^<2+> and the lost activity was restored on addition of 50 mM Ca^<2+>. However, inactivation of oxygen evolution by low pH-treatment of oxygen-evolving PS II complexes containing only one Ca^<2+> from a rice chlorophyll b-deficient mutant was not associated with extraction of the bound Ca^<2+>, although oxygen evolution was markedly enhanced by the addition of Ca^<2+> to the treated complexes. Thus, the acid-inactivation of oxygen evolution cannot be related to extraction of Ca^<2+>. On the other hand, low pH-treatment was found to share the following common features with NaCl-treatment which also causes a Ca^<2+>-reversible inactivation of oxygen evolution. (1) Exposure of PS II membranes to pH 3.0 resulted in solubilization of the 23 and 17 kDa extrinsic proteins, although the released proteins rebound to the membranes when pH was raised to 6.5. (2) There was an apparent heterogeneity in the binding affinity of Ca^<2+> effective in restoration of the oxygen-evolving activity. (3) Low pH-treated preparations required a higher concentration of Ca^<2+> for the maximum reactivation of oxygen evolution than did NaCl-washed preparations. This was also the case with Sr^<2+>, which stimulated oxygen evolution of both low pH-treated and NaCl-washed PS II membranes to smaller extents. When the extrinsic 23 and 17 kDa proteins had been removed, however, Ca^<2+> concentration dependence of oxygen evolution in low pH-treated membranes became similar to that in NaCl-washed PS 11 preparations and the changes were largely reversed by rebinding of the two proteins. These results strongly suggest that low pH-treatment and NaCl-wash involve similar mechanisms of Ca^<2+>-dependent reactivation.

Other Link： https://projects.repo.nii.ac.jp/?action=repository_uri&item_id=181395

Isolation and characterization of Photosystem II complexes which lack light-harvesting chlorophyll a/b proteins but retain three extrinsic proteins related to oxygen evolution from spinach

Isao Enami, Kei Kamino, Jian-Ren Shen, Kazuhiko Satoh, Sakae Katoh

BBA - Bioenergetics 977 ( 1 ) 33 - 39 1989.10

Language：English

Oxygen-evolving Photosystem II (PS II) complexes, which were largely deprived of major light-harvesting chlorophyll a/b proteins (LHC II) but still associated with the 33 kDa, 23 kDa and 17 kDa extrinsic proteins related to oxygen evolution, were isolated from spinach oxygen-evolving PS II membranes with a non-ionic detergent, n-heptyl thioglucoside. A minor antenna chlorophyll-protein (CP 29) was present but in reducted amounts. The complexes contained all the constituent subunits of PS II reaction center core complexes, the 47 kDa and 43 kDa chlorophyll-carrying proteins, the D1 and D2 proteins and cytochrome b-559. In addition, three hydrophobic proteins of 29 kDa (CP 29 apoprotein), 20 kDa and 10 kDa were present. The antenna size was 80 chlorophyll a per QA, or 76 chlorophyll a per 4 Mn, and the complexes contained about 1 Ca2+ per PS II. With phenyl- or dichloro-p-benzoquinone as electron acceptor, the complexes showed high rates of oxygen evolution in the absence of exogenously added Ca2+. The activity became, however, strongly Ca2+-dependent when the 23 kDa and 17 kDa proteins, but not the bound Ca2+, had been removed with 1.5 M NaCl. The Ca2+ requirement disappeared on reconstitution of the complexes with the two proteins. The complexes were compared with other oxygen-evolving preparations having different polypeptide compositions and functions of several subunit proteins and Ca2+ in PS II electron transport are discussed. © 1989 Elsevier Science Publishers.

DOI： 10.1016/S0005-2728(89)80006-4

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Nearest neighbor relationships among constituent proteins of oxygen-evolving Photosystem II membranes: binding and function of the extrinsic 33 kDa protein

Isao Enami, Takeshi Miyaoka, Yasuki Mochizuki, Jian-Ren Shen, Kazuhiko Satoh, Sakae Katoh

BBA - Bioenergetics 973 ( 1 ) 35 - 40 1989

Language：English

Nearest neighbor relationships among constituent proteins of oxygen-evolving Photosystem II (PS II) membrane preparations from spinach were investigated by means of crosslinking with a cleavable bifunctional crosslinker, dithiobis(succinimidylpropionate) (DSP). (1) Diagonal gel electrophoresis revealed crosslinking between two extrinsic proteins of 17 and 23 kDa, between the extrinsic 33 kDa protein and the 47 kDa chlorophyll-carrying protein and between the 26 and 27 kDa apoproteins of light-harvesting chlorophyll a/b protein. In addition, a product which involved a protein of 29 kDa was detected. (2) Amounts of the extrinsic proteins crosslinked were determined by washing DSP-treated membranes with high concentrations of urea and NaCl, or CaCl2. Neither of the two extrinsic proteins of 17 and 23 kDa was crosslinked with intrinsic membrane proteins, whereas 15 to 20% of the 33 kDa protein was immobilized by treatment with 0.1% DSP. Oxygen evolution became resistant to the urea/NaCl-wash proportionally to the amount of the 33 kDa protein crosslinked, indicating that the 33 kDa protein covalently bound to the 47 kDa protein is still fully functional. (3) The crosslinking of the 33 kDa protein accompanied by parallel increases in the amount of Mn remained unextracted, and the rate of oxygen evolution survived after 30-min treatment of PS IImembranes at pH 9.0. Thus the 33 kDa protein has a protective effect on the Mn cluster at the alkaline pH. In contrast, Mn was mostly extracted with a high concentration of Tris, irrespective of the crosslinking of the 33 kDa protein. © 1989 Elsevier Science Publishers B.V. (Biomedical Division) All rights reserved.

DOI： 10.1016/S0005-2728(89)80399-8

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