The PsbQ′ protein affects the redox potential of the QA in photosystem II

M. Yamada; R. Nagao; M. Iwai; Y. Arai; A. Makita; H. Ohta; T. Tomo

doi:10.1007/s11099-018-0778-8

The PsbQ′ protein affects the redox potential of the Q_A in photosystem II

M. Yamada, R. Nagao, M. Iwai, Y. Arai, A. Makita, H. Ohta, T. Tomo

Research Institute for Interdisciplinary Science

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

Abstract

Red alga contains four extrinsic proteins in photosystem II (PSII), which are PsbO, PsbV, PsbU, and PsbQ′. Except for the PsbQ′, the composition is the same in cyanobacterial PSII. Reconstitution analysis of cyanobacterial PSII has shown that oxygen-evolving activity does not depend on the presence of PsbQ′. Recently, the structure of red algal PSII was elucidated. However, the role of PsbQ′ remains unknown. In this study, the function of the acceptor side of PSII was analyzed in PsbQ′-reconstituted PSII by redox titration of Q_A and thermoluminescence. The redox potential of Q_A was positively shifted when PsbQ′ was attached to the PSII. The positive shift of Q_A is thought to cause a decrease in the amount of triplet chlorophyll in PSII. On the basis of these results, we propose that PsbQ′ has a photoprotective function when irradiated with strong light.

Original language	English
Pages (from-to)	185-191
Number of pages	7
Journal	Photosynthetica
Volume	56
Issue number	1
DOIs	https://doi.org/10.1007/s11099-018-0778-8
Publication status	Published - Mar 1 2018

Keywords

diversity
evolution
photoinhibition
photosynthesis

ASJC Scopus subject areas

Physiology
Plant Science

Access to Document

10.1007/s11099-018-0778-8

Cite this

@article{0050c0f071f54d75aa62e941fbd62734,

title = "The PsbQ′ protein affects the redox potential of the QA in photosystem II",

abstract = "Red alga contains four extrinsic proteins in photosystem II (PSII), which are PsbO, PsbV, PsbU, and PsbQ′. Except for the PsbQ′, the composition is the same in cyanobacterial PSII. Reconstitution analysis of cyanobacterial PSII has shown that oxygen-evolving activity does not depend on the presence of PsbQ′. Recently, the structure of red algal PSII was elucidated. However, the role of PsbQ′ remains unknown. In this study, the function of the acceptor side of PSII was analyzed in PsbQ′-reconstituted PSII by redox titration of QA and thermoluminescence. The redox potential of QA was positively shifted when PsbQ′ was attached to the PSII. The positive shift of QA is thought to cause a decrease in the amount of triplet chlorophyll in PSII. On the basis of these results, we propose that PsbQ′ has a photoprotective function when irradiated with strong light.",

keywords = "diversity, evolution, photoinhibition, photosynthesis",

author = "M. Yamada and R. Nagao and M. Iwai and Y. Arai and A. Makita and H. Ohta and T. Tomo",

note = "Funding Information: Received 8 May 2017, accepted 16 August 2017 published as online-first 10 January 2018. +Corresponding author; e-mail: tomo@rs.tus.ac.jp Abbreviations: Chl – chlorophyll; CP43 – chlorophyll protein 43 kDa; CP47 – chlorophyll protein 47 kDa; DCMU – 3-(3,4-dichlorophenyl)-1,1-dimethylurea; IPTG – isopropyl β-D-1-thiogalactopyranoside; Ni-NTA – nickel-nitrilotriacetic acid. Acknowledgments: This study was supported by the Grants-in-Aids for Scientific Research from JSPS (No. 24370025, 26220801, 17K07453 to T.T.) and a grant from JST PRESTO (T.T.). The authors thank Professor Kintake Sonoike for his kind support. We express our heartfelt gratitude to Professor Govindjee for his numerous invaluable contributions to the research field of photosynthesis. Publisher Copyright: {\textcopyright} 2018, The Institute of Experimental Botany.",

year = "2018",

month = mar,

day = "1",

doi = "10.1007/s11099-018-0778-8",

language = "English",

volume = "56",

pages = "185--191",

journal = "Photosynthetica",

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T1 - The PsbQ′ protein affects the redox potential of the QA in photosystem II

AU - Yamada, M.

AU - Nagao, R.

AU - Iwai, M.

AU - Arai, Y.

AU - Makita, A.

AU - Ohta, H.

AU - Tomo, T.

N1 - Funding Information: Received 8 May 2017, accepted 16 August 2017 published as online-first 10 January 2018. +Corresponding author; e-mail: tomo@rs.tus.ac.jp Abbreviations: Chl – chlorophyll; CP43 – chlorophyll protein 43 kDa; CP47 – chlorophyll protein 47 kDa; DCMU – 3-(3,4-dichlorophenyl)-1,1-dimethylurea; IPTG – isopropyl β-D-1-thiogalactopyranoside; Ni-NTA – nickel-nitrilotriacetic acid. Acknowledgments: This study was supported by the Grants-in-Aids for Scientific Research from JSPS (No. 24370025, 26220801, 17K07453 to T.T.) and a grant from JST PRESTO (T.T.). The authors thank Professor Kintake Sonoike for his kind support. We express our heartfelt gratitude to Professor Govindjee for his numerous invaluable contributions to the research field of photosynthesis. Publisher Copyright: © 2018, The Institute of Experimental Botany.

PY - 2018/3/1

Y1 - 2018/3/1

N2 - Red alga contains four extrinsic proteins in photosystem II (PSII), which are PsbO, PsbV, PsbU, and PsbQ′. Except for the PsbQ′, the composition is the same in cyanobacterial PSII. Reconstitution analysis of cyanobacterial PSII has shown that oxygen-evolving activity does not depend on the presence of PsbQ′. Recently, the structure of red algal PSII was elucidated. However, the role of PsbQ′ remains unknown. In this study, the function of the acceptor side of PSII was analyzed in PsbQ′-reconstituted PSII by redox titration of QA and thermoluminescence. The redox potential of QA was positively shifted when PsbQ′ was attached to the PSII. The positive shift of QA is thought to cause a decrease in the amount of triplet chlorophyll in PSII. On the basis of these results, we propose that PsbQ′ has a photoprotective function when irradiated with strong light.

AB - Red alga contains four extrinsic proteins in photosystem II (PSII), which are PsbO, PsbV, PsbU, and PsbQ′. Except for the PsbQ′, the composition is the same in cyanobacterial PSII. Reconstitution analysis of cyanobacterial PSII has shown that oxygen-evolving activity does not depend on the presence of PsbQ′. Recently, the structure of red algal PSII was elucidated. However, the role of PsbQ′ remains unknown. In this study, the function of the acceptor side of PSII was analyzed in PsbQ′-reconstituted PSII by redox titration of QA and thermoluminescence. The redox potential of QA was positively shifted when PsbQ′ was attached to the PSII. The positive shift of QA is thought to cause a decrease in the amount of triplet chlorophyll in PSII. On the basis of these results, we propose that PsbQ′ has a photoprotective function when irradiated with strong light.

KW - diversity

KW - evolution

KW - photoinhibition

KW - photosynthesis

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