Results 151 to 160 of about 2,381 (181)
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The CP47 and CP43 Core Antenna Components
2005The CP47 and CP43 subunits of Photosystem II bind chlorophyll a and belong to a family of (bacterio)chlorophyll-binding proteins that serve as core antenna polypeptides in both anoxygenic and oxygenic photosynthesis. Uniquely, both of these proteins possess extended hydrophilic domains that contribute to the environment of the oxygen-evolving complex ...
Julian J. Eaton-Rye, Cindy Putnam-Evans
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Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1993
Mutants of the cyanobacterium Synechocystis sp. PCC 6803 have been generated in which parts of psbC (the gene encoding the Photosystem II chlorophyll-protein CP43) have been replaced with the homologous gene fragment from spinach. Upon the replacement of all but the 3' 84 bp of the cyanobacterial psbC gene with the homologous fragment from spinach, an ...
S D, Carpenter, I, Ohad, W F, Vermaas
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Mutants of the cyanobacterium Synechocystis sp. PCC 6803 have been generated in which parts of psbC (the gene encoding the Photosystem II chlorophyll-protein CP43) have been replaced with the homologous gene fragment from spinach. Upon the replacement of all but the 3' 84 bp of the cyanobacterial psbC gene with the homologous fragment from spinach, an ...
S D, Carpenter, I, Ohad, W F, Vermaas
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Heat-Induced Unfolding of Apo-CP43 Studied by Fluorescence Spectroscopy and CD Spectroscopy
Photosynthesis Research, 2015CP43 is a chlorophyll-binding protein, which acts as a conduit for the excitation energy transfer. The thermal stability of apo-CP43 was studied by intrinsic fluorescence, exogenous ANS fluorescence, and circular dichroism spectroscopy. Under heat treatment, the structure of apo-CP43 changed and existed transition state occurred between 56 and 62 °C by
Linfang Du, Lei Xi
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Spectral densities and absorption spectra of the core antenna complex CP43 from photosystem II
The Journal of Chemical Physics, 2022Besides absorbing light, the core antenna complex CP43 of photosystem II is of great importance in transferring excitation energy from the antenna complexes to the reaction center. Excitation energies, spectral densities, and linear absorption spectra of the complex have been evaluated by a multiscale approach.
Pooja Sarngadharan +2 more
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Investigating the Role of CP43 Phosphorylation During Environmental Stress
1998The product of the photosystem two (PSII) psbC gene is usually called CP43 since it is a chlorophyll binding protein (CP) with an apparent molecular mass of 43kDa as judged by SDS-PAGE (1). It is reasonably easy to remove biochemically CP43 from PSII to leave a subcore complex composed of CP47 and the D1 and D2 proteins (2).
Katia Georgieva +2 more
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Degradation of Antenna Chlorophyll-Binding Protein CP43 during Photoinhibition of Photosystem II
Biochemistry, 1995When photosystem II (PS II) membranes from spinach were treated with Tris (0.8 M, pH 9.0) and illuminated with white light (5000 microE m-2 s-1) under aerobic conditions at 25 degrees C, not only were the reaction center-forming D1 and D2 proteins degraded but the antenna chlorophyll-binding protein CP43 was also degraded.
Y, Yamamoto, T, Akasaka
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Journal of Structural Biology, 2000
Microcrystals of the chlorophyll binding protein, CP43, isolated from spinach thylakoid membranes have been studied by electron microscopy both in negative stain and in vitreous ice. Image analyses of three characteristic views show that the crystals are built of five different layers perpendicular to the c-axis.
Claudia Büchel +2 more
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Microcrystals of the chlorophyll binding protein, CP43, isolated from spinach thylakoid membranes have been studied by electron microscopy both in negative stain and in vitreous ice. Image analyses of three characteristic views show that the crystals are built of five different layers perpendicular to the c-axis.
Claudia Büchel +2 more
exaly +3 more sources
Structure-based simulation of linear optical spectra of the CP43 core antenna of photosystem II
Photosynthesis Research, 2011The linear optical spectra (absorbance, linear dichroism, circular dichroism, fluorescence) of the CP43 (PsbC) antenna of the photosystem II core complex (PSIIcc) pertaining to the S(0) → S(1) (Q(Y)) transitions of the chlorophyll (Chl) a pigments are simulated by applying a combined quantum chemical/electrostatic method to obtain excitonic couplings ...
Mueh, F., Madjet, M. E. -A., Renger, T.
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Science in China Series C: Life Sciences, 2007
Terahertz time-domain spectroscopy (THz-TDS) is a new technique in studying the conformational state of a molecule in recent years. In this work, we reported the first use of THz-TDS to examine the denaturation of two photosynthesis membrane proteins: CP43 and CP47.
YuanGang, Qu +5 more
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Terahertz time-domain spectroscopy (THz-TDS) is a new technique in studying the conformational state of a molecule in recent years. In this work, we reported the first use of THz-TDS to examine the denaturation of two photosynthesis membrane proteins: CP43 and CP47.
YuanGang, Qu +5 more
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European Journal of Biochemistry, 1997
Two chlorophyll‐binding antenna proteins in the photosystem II core, CP43 and CP47, are structurally similar and are thought to have evolved from a common ancestor. Several conserved histidine residues in hydrophobic regions of CP47 have been shown to be important for photosystem I1 structure, function, and energy transfer.
P, Manna, W, Vermaas
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Two chlorophyll‐binding antenna proteins in the photosystem II core, CP43 and CP47, are structurally similar and are thought to have evolved from a common ancestor. Several conserved histidine residues in hydrophobic regions of CP47 have been shown to be important for photosystem I1 structure, function, and energy transfer.
P, Manna, W, Vermaas
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