The most abundant chlorophyll-binding complex in plants is the intrinsic membrane protein light-harvesting complex II (LHC II). LHC II acts as a light-harvesting antenna and has an important role in the distribution of absorbed energy between the two photosystems of photosynthesis. We used spectroscopic techniques to study a synthetic peptide with identical sequence to the LHC IIb N terminus found in pea, with and without the phosphorylated Thr at the 5th amino acid residue, and to study both forms of the native full-length protein. Our results show that the N terminus of LHC II changes structure upon phosphorylation and that the structural change resembles that of rabbit glycogen phosphorylase, one of the few phosphoproteins where both phosphorylated and non-phosphorylated structures have been solved. Our results indicate that phosphorylation of membrane proteins may regulate their function through structural protein-protein interactions in surface-exposed domains. Light harvesting complex II (LHC II)1 is a major chlorophyllcontaining protein complex that accounts alone for half of the pigments involved in photosynthesis in plants. It is located mainly in appressed regions of the thylakoid membrane where it acts as the light-harvesting antenna for photosystem II (PS II). Reversible phosphorylation of LHC II is an established mechanism for redistribution of absorbed light energy between PS II and PS I. Phosphorylation of LHC II (giving LHC II(P)) is triggered by conditions where the plastoquinone pool of the photosynthetic electron transport chain becomes reduced (1). The kinase responsible for the phosphorylation of LHC II is not yet identified, although it is suggested that it is located in the core of photosystem II (2) or in contact with the cytochrome b 6 f complex (3, 4). LHC II(P) is found in the unappressed regions of the chloroplast thylakoid membrane and there acts as a lightharvesting antenna for photosystem I (PS I) (5-7). From electron crystallography of 2-dimensional crystals, a structure for the major part of non-phosphorylated LHC II has been described at 3.4-Å resolution (8). This structure reveals no information regarding the N-terminal domain that contains the phosphorylation site at position 5 (Thr); the protein backbone was traced only to residue 26 where it ends up close to the lipid membrane, consistent with the fact that the sequence between residues 21 and 29 (RVKYLGPF) (9) consists mainly of hydrophobic, aromatic, or charged amino acids. Aromatic residues are located at the membrane surface in structures of membrane proteins (10 -13), and residues Trp-16 and Tyr-17 of LHC II may also then form a point of contact with the membrane. LHC II has been shown to lose its ability to trimerize when more than the first 15 amino acids are removed from the apoprotein (14). At this site, specific lipid-protein interactions between the amino side chains and the lipid phosphatidylglycerol are involved in stabilization of the trimers (15), which implies that only the first 15 amino acid residues at the...
As a starting point for our calculation of 3-methyl-4-phenyl-5-(2-pyridyl)-1,2,4-triazole we used the XRD data obtained by C. Liu, Z. Wang, H. Xiao, Y. Lan, X. Li, S. Wang, Jie Tang, Z. Chen, J. Chem. Crystallogr., 2009 39 881. The structure was optimized by minimization of the forces acting on the atoms keeping the lattice parameters fixed with the experimental values. Using the relaxed geometry we have performed a comprehensive theoretical investigation of dispersion of the linear and nonlinear optical susceptibilities of 3-methyl-4-phenyl-5-(2-pyridyl)-1,2,4-triazole using the full potential linear augmented plane wave method. The local density approximation by Ceperley-Alder (CA) exchange-correlation potential was applied. The full potential calculations show that this material possesses a direct energy gap of 3.4 eV for the original experimental structure and 3.2 eV for the optimized structure. We have calculated the complex's dielectric susceptibility ε(ω) dispersion, its zero-frequency limit ε(1)(0) and the birefringence. We find that a 3-methyl-4-phenyl-5-(2-pyridyl)-1,2,4-triazole crystal possesses a negative birefringence at the low-frequency limit Δn(0) which is equal to about -0.182 (-0.192) and at λ = 1064 nm is -0.193 (-0.21) for the non-optimized structure (optimized one), respectively. We also report calculations of the complex second-order optical susceptibility dispersions for the principal tensor components: χ(ω), χ(ω) and χ(ω). The intra- and inter-band contributions to these susceptibilities are evaluated. The calculated total second order susceptibility tensor components at the low-frequency limit |χ(0)| and |χ(ω)| at λ = 1064 nm for all the three tensor components are evaluated. We established that the calculated microscopic second order hyperpolarizability, β(ijk), the vector component along the dipole moment direction, at the low-frequency limit and at λ = 1064 nm, for the dominant component |χ(ω)| is 4.99 × 10(-30) esu (3.4 × 10(-30) esu) and 7.72 × 10(-30) esu (5.1 × 10(-30) esu), respectively for the non-optimized structure (optimized structure).
Photosynthetic organisms exposed to a dynamic light environment exhibit complex transients of photosynthetic activities that are strongly dependent on the temporal pattern of the incident irradiance. In a harmonically modulated light of intensity I approximately const.+sin(omegat), chlorophyll fluorescence response consists of a steady-state component, a component modulated with the angular frequency of the irradiance omega and several upper harmonic components (2omega, 3omega and higher). Our earlier reverse engineering analysis suggests that the non-linear response can be caused by a negative feedback regulation of photosynthesis. Here, we present experimental evidence that the negative feedback regulation of the energetic coupling between phycobilisome and Photosystem II (PSII) in the cyanobacterium Synechocystis sp. PCC6803 indeed results in the appearance of upper harmonic modes in the chlorophyll fluorescence emission. Dynamic changes in the coupling of the phycobilisome to PSII are not accompanied by corresponding antiparallel changes in the Photosystem I (PSI) excitation, suggesting a regulation limited to PSII. Strong upper harmonic modes were also found in the kinetics of the non-photochemical quenching (NPQ) of chlorophyll fluorescence, of the P700 redox state and of the CO(2) assimilation in tobacco (Nicotiana tabaccum) exposed to harmonically modulated light. They are ascribed to negative feedback regulation of the reactions of the Calvin-Benson cycle limiting the photosynthetic electron transport. We propose that the observed non-linear response of photosynthesis may also be relevant in a natural light environment that is modulated, e.g., by ocean waves, moving canopy or by varying cloud cover. Under controlled laboratory conditions, the non-linear photosynthetic response provides a new insight into dynamics of the regulatory processes.
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