Protein secondary structure and conformational changes of photosystem II during heat denaturation studied by Fourier transform-infrared spectroscopy

Shi, Hua; Xiong, Ling; Yang, Kyu Hwan; Tang, Cui; Kuang, Tingyun; Zhao, Nanming

doi:10.1016/s0022-2860(98)00287-7

Cited by 17 publications

(8 citation statements)

References 28 publications

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“…Especially the structure of trans-membrane domain and extra-membrane domain altered greatly under heat stress. Shi et al (1998) already showed that great conformational changes in PS2 occur in the temperature range of 55-65 o C. However, the great changes of protein secondary structure in PS1 occurred at around 60-70 o C as shown in Figs. 1 and 3.…”

Section: Resultsmentioning

confidence: 93%

Effects of heat treatment on the protein secondary structure and pigment microenvironment in photosystem 1 complex

Gong³

et al. 2005

Photosynt.

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The protein secondary structure and pigments' microenvironment in photosystem 1 (PS1) complexes were studied in the temperature range of 25-80 o C using Fourier transform infrared (FT-IR) and circular dichroism (CD) spectroscopy, respectively. Quantitative analysis of the component bands of the amide I band (1 700-1 600 cm -1 ) showed no significant change below 50 o C. However, apparent conformational changes occurred at 60 o C and further continued at 70 and 80 o C accompanied with transitions of secondary structure mainly from α-helix to the β-sheet structures. CD analysis demonstrated that the regular arrangement, viz. protein microenvironment of pigments of PS1 complexes, was destroyed by heat treatment which might come from the changes of protein secondary structure of PS1. The CD signals at 645 nm contributed by chlorophyll (Chl) b of light-harvesting complex 1 (LHC1) were easily destroyed at the beginning of heat treatment (25-60 o C). When temperature reached 70 and 80 o C, the CD signals at 478 nm contributed mainly by Chl b of LHC1 and 498 nm contributed by carotenoids decreased most rapidly, indicating that LHC1 was more sensitive to high temperature than core complexes. In addition, the oxygen uptake rate decreased by 90.81 % at 70 o C and was lost completely at 80 o C showing that heat treatment damaged the regular function of PS1 complexes. This may be attributed to heat-induced changes of pigment microenvironment and protein secondary structure, especially transmembrane α-helix located in PsaA/B of PS1.

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Section: Resultsmentioning

confidence: 93%

Effects of heat treatment on the protein secondary structure and pigment microenvironment in photosystem 1 complex

Gong³

et al. 2005

Photosynt.

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“…Because of the long IR wavelength, light scattering problems are virtually non-existent and highly aggregated materials or large membrane fragments can be investigated. A unique advantage of infrared spec-troscopy is that it allows simultaneous study of the structure of lipids and proteins in intact biological membranes without introduction of foreign perturbing probes [4]. Some types of analysis of infrared data are claimed to provide highly accurate quantitative estimates of the content of secondary structures, with a standard deviation as low as 2% -3% with respect to the corresponding X-ray structures.…”

Section: Introductionmentioning

confidence: 99%

Secondary Structure Changes and Thermal Stability of Plasma Membrane Proteins of Wheat Roots in Heat Stress

Zhao¹,

Shi²,

Chen³

et al. 2011

AJPS

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“…Thermal denaturation is a valuable tool in studying the folding mechanism of proteins and has been conducted on PSII to investigate the thermal stability and conformational changes of protein subunits [6][7][8][9][10][11]. Thompson et al used differential scanning calorimetry (DSC) to study the heat denaturation of PSII and found four endothermic transitions [6]; the subunit contributions to these transitions were further identified by thermal gel analysis [7].…”

Section: Introductionmentioning

confidence: 99%

“…Thompson et al used differential scanning calorimetry (DSC) to study the heat denaturation of PSII and found four endothermic transitions [6]; the subunit contributions to these transitions were further identified by thermal gel analysis [7]. The thermal stability and the protein secondary structure changes of PSII during thermal denaturation were studied by Shi et al using FT-IR [8], and by Li et al using circular dichroism spectra [9]. Functional study showed that the oxygen evolving capacity of PSII membrane was more sensitive to high temperature than protein secondary structures [8,10].…”

Section: Introductionmentioning

confidence: 99%

“…The thermal stability and the protein secondary structure changes of PSII during thermal denaturation were studied by Shi et al using FT-IR [8], and by Li et al using circular dichroism spectra [9]. Functional study showed that the oxygen evolving capacity of PSII membrane was more sensitive to high temperature than protein secondary structures [8,10]. However, these studies focused on the denaturation of protein subunits and did not show how the pigment moiety changes during thermal denaturation.…”

Section: Introductionmentioning

confidence: 99%

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Global Changes of Chlorophyll Excitonic Interactions in Photosystem II During Thermal Denaturation

Xu¹,

Ding²,

Gong³

et al. 2005

PPL

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Photosystem II (PSII) is a multisubunit chlorophyll-binding enzyme that absorbs light to catalyze water oxidation and plastoquinone reduction. Chlorophyll excitonic interaction changes in PSII were studied by absorption and circular dichroism spectra from 25 degrees C to 80 degrees C, and protein subunit denaturation was monitored by differential scanning calorimetry. A four-stage process of chlorophyll excitonic interaction change was observed being correlated with the denaturation of protein subunits.

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Protein secondary structure and conformational changes of photosystem II during heat denaturation studied by Fourier transform-infrared spectroscopy

Cited by 17 publications

References 28 publications

Effects of heat treatment on the protein secondary structure and pigment microenvironment in photosystem 1 complex

Effects of heat treatment on the protein secondary structure and pigment microenvironment in photosystem 1 complex

Secondary Structure Changes and Thermal Stability of Plasma Membrane Proteins of Wheat Roots in Heat Stress

Global Changes of Chlorophyll Excitonic Interactions in Photosystem II During Thermal Denaturation

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