Structural coupling of extrinsic proteins with the oxygen-evolving center in red algal photosystem II as revealed by light-induced FTIR difference spectroscopy

Chihiro Uno; Ryo Nagao; Hiroyuki Suzuki; Tatsuya Tomo; Takumi Noguchi

doi:10.1021/bi4009787

Structural coupling of extrinsic proteins with the oxygen-evolving center in red algal photosystem II as revealed by light-induced FTIR difference spectroscopy

Chihiro Uno, Ryo Nagao, Hiroyuki Suzuki, Tatsuya Tomo, Takumi Noguchi

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

13 Citations (Scopus)

Abstract

Effects of binding of extrinsic proteins (PsbO, PsbQ′, PsbV, and PsbU) on the structure of the oxygen-evolving center (OEC) in photosystem II core complexes from a red alga, Cyanidium caldarium, were studied using Fourier transform infrared (FTIR) spectroscopy. S₂-minus-S₁ FTIR difference spectra showed that the protein conformations of the OEC, revealed by the changes in amide I and II bands, were significantly altered upon depletion of all the extrinsic proteins, but mostly recovered when PsbV was rebound with the support of other extrinsic proteins. The recovery of protein conformations correlated well with O₂ evolution activity. This PsbV function of retaining a proper OEC conformation in red algae resembles that of PsbP in higher plants reported previously.

Original language	English
Pages (from-to)	5705-5707
Number of pages	3
Journal	Biochemistry
Volume	52
Issue number	34
DOIs	https://doi.org/10.1021/bi4009787
Publication status	Published - Aug 27 2013
Externally published	Yes

ASJC Scopus subject areas

Biochemistry

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title = "Structural coupling of extrinsic proteins with the oxygen-evolving center in red algal photosystem II as revealed by light-induced FTIR difference spectroscopy",

abstract = "Effects of binding of extrinsic proteins (PsbO, PsbQ′, PsbV, and PsbU) on the structure of the oxygen-evolving center (OEC) in photosystem II core complexes from a red alga, Cyanidium caldarium, were studied using Fourier transform infrared (FTIR) spectroscopy. S2-minus-S1 FTIR difference spectra showed that the protein conformations of the OEC, revealed by the changes in amide I and II bands, were significantly altered upon depletion of all the extrinsic proteins, but mostly recovered when PsbV was rebound with the support of other extrinsic proteins. The recovery of protein conformations correlated well with O2 evolution activity. This PsbV function of retaining a proper OEC conformation in red algae resembles that of PsbP in higher plants reported previously.",

author = "Chihiro Uno and Ryo Nagao and Hiroyuki Suzuki and Tatsuya Tomo and Takumi Noguchi",

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volume = "52",

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publisher = "American Chemical Society",

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TY - JOUR

T1 - Structural coupling of extrinsic proteins with the oxygen-evolving center in red algal photosystem II as revealed by light-induced FTIR difference spectroscopy

AU - Uno, Chihiro

AU - Nagao, Ryo

AU - Suzuki, Hiroyuki

AU - Tomo, Tatsuya

AU - Noguchi, Takumi

PY - 2013/8/27

Y1 - 2013/8/27

N2 - Effects of binding of extrinsic proteins (PsbO, PsbQ′, PsbV, and PsbU) on the structure of the oxygen-evolving center (OEC) in photosystem II core complexes from a red alga, Cyanidium caldarium, were studied using Fourier transform infrared (FTIR) spectroscopy. S2-minus-S1 FTIR difference spectra showed that the protein conformations of the OEC, revealed by the changes in amide I and II bands, were significantly altered upon depletion of all the extrinsic proteins, but mostly recovered when PsbV was rebound with the support of other extrinsic proteins. The recovery of protein conformations correlated well with O2 evolution activity. This PsbV function of retaining a proper OEC conformation in red algae resembles that of PsbP in higher plants reported previously.

AB - Effects of binding of extrinsic proteins (PsbO, PsbQ′, PsbV, and PsbU) on the structure of the oxygen-evolving center (OEC) in photosystem II core complexes from a red alga, Cyanidium caldarium, were studied using Fourier transform infrared (FTIR) spectroscopy. S2-minus-S1 FTIR difference spectra showed that the protein conformations of the OEC, revealed by the changes in amide I and II bands, were significantly altered upon depletion of all the extrinsic proteins, but mostly recovered when PsbV was rebound with the support of other extrinsic proteins. The recovery of protein conformations correlated well with O2 evolution activity. This PsbV function of retaining a proper OEC conformation in red algae resembles that of PsbP in higher plants reported previously.

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Structural coupling of extrinsic proteins with the oxygen-evolving center in red algal photosystem II as revealed by light-induced FTIR difference spectroscopy

Abstract

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