Interaction of trivalent Al and Ga cations with proteins of PSII. Cation binding mode and protein conformation by FTIR spectroscopy

Nahar, S.; Carpentier, Robert; Tajmir-Riahi, H.A.

doi:10.1016/s0162-0134(96)00138-9

Cited by 20 publications

(8 citation statements)

References 22 publications

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“…6). The observed structural changes were probably related to the electrostatic Al 3+ -proteins interaction [66]. The interaction of cations with PSI proteins was also reported in the presence of Pb 2+ and spermine, a heavy metal and an organic cation, respectively [28,57].…”

Section: Discussionmentioning

confidence: 57%

Characterization of the structural changes and photochemical activity of photosystem I under Al3+ effect

Hasni

Msilini

Hamdani

et al. 2015

Journal of Photochemistry and Photobiology B: Biology

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Section: Discussionmentioning

confidence: 57%

Characterization of the structural changes and photochemical activity of photosystem I under Al3+ effect

Hasni

Msilini

Hamdani

et al. 2015

Journal of Photochemistry and Photobiology B: Biology

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“…Furthermore, Li et al (2012) [ 48 ] have suggested that the inhibition of PSII activity in tobacco leaves subjected to aluminum stress may be due to the reaction of Al 3+ with the non-heme iron located between Q A and Q B . Nahar et al (1997) [ 57 ] have reported that the interaction of Ga 3+ and Al 3+ , at high concentrations, with proteins of PSII causes a major conformational change of protein secondary structure. However, in spite of these studies, to our knowledge little information is available regarding the mechanisms of interaction of Al 3+ with PSII complex and its effects on the structural change of proteins, proteins composition, and functionality of PSII complex.…”

Section: Introductionmentioning

confidence: 99%

Mechanism of Interaction of Al3+ with the Proteins Composition of Photosystem II

et al. 2015

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The inhibitory effect of Al3+on photosystem II (PSII) electron transport was investigated using several biophysical and biochemical techniques such as oxygen evolution, chlorophyll fluorescence induction and emission, SDS-polyacrylamide and native green gel electrophoresis, and FTIR spectroscopy. In order to understand the mechanism of its inhibitory action, we have analyzed the interaction of this toxic cation with proteins subunits of PSII submembrane fractions isolated from spinach. Our results show that Al 3+, especially above 3 mM, strongly inhibits oxygen evolution and affects the advancement of the S states of the Mn4O5Ca cluster. This inhibition was due to the release of the extrinsic polypeptides and the disorganization of the Mn4O5Ca cluster associated with the oxygen evolving complex (OEC) of PSII. This fact was accompanied by a significant decline of maximum quantum yield of PSII (Fv/Fm) together with a strong damping of the chlorophyll a fluorescence induction. The energy transfer from light harvesting antenna to reaction centers of PSII was impaired following the alteration of the light harvesting complex of photosystem II (LHCII). The latter result was revealed by the drop of chlorophyll fluorescence emission spectra at low temperature (77 K), increase of F0 and confirmed by the native green gel electrophoresis. FTIR measurements indicated that the interaction of Al 3+ with the intrinsic and extrinsic polypeptides of PSII induces major alterations of the protein secondary structure leading to conformational changes. This was reflected by a major reduction of α-helix with an increase of β-sheet and random coil structures in Al 3+-PSII complexes. These structural changes are closely related with the functional alteration of PSII activity revealed by the inhibition of the electron transport chain of PSII.

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“…It has an exceptional binding capacity for a wide range of endogenous and exogenous ligands, and its abundance makes it an important determinant of physiological behavior of many molecules [14]. In recent years, several spectrophotometric methods mainly including fluorescence, UV-vis, CD, FT-IR, NMR have been used to study the interaction of small molecule substances and protein and clarify the conformational change of protein [15][16][17][18]. Some techniques such as electrochemical technique [19], capillary electrophoresis [20], high-performance liquid chromatography [21], have also been applied to the evaluation of binding mode and binding constants.…”

Section: Introductionmentioning

confidence: 99%

Interaction between titanium dioxide nanoparticles and human serum albumin revealed by fluorescence spectroscopy in the absence of photoactivation

Sun

Chen

et al. 2009

Journal of Luminescence

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Interaction of trivalent Al and Ga cations with proteins of PSII. Cation binding mode and protein conformation by FTIR spectroscopy

Cited by 20 publications

References 22 publications

Characterization of the structural changes and photochemical activity of photosystem I under Al3+ effect

Characterization of the structural changes and photochemical activity of photosystem I under Al3+ effect

Mechanism of Interaction of Al3+ with the Proteins Composition of Photosystem II

Interaction between titanium dioxide nanoparticles and human serum albumin revealed by fluorescence spectroscopy in the absence of photoactivation

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