Publications by authors named "Chunhe Xu"

Most anurans are highly vocal but their vocalizations are stereotyped and simple with limited repertoire sizes compared with other vocal vertebrates, presumably because of the limited mechanisms for fine vocal motor control. We recently reported that the call of the concaveeared torrent frog (Amolops tormotus Fei) is an exception in its seemingly endless variety, musical warbling quality, extension of call frequency into the ultrasonic range and the prominence of subharmonics, chaos and other nonlinear features. We now show that the major spectral features of its calls, responsible for this frog's vocal diversity, can be generated by forcing pressurized air through the larynx of euthanized males.

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When manganese stabilizing protein (MSP) was treated with 0.5 mM N-succinimidyl propionate (NSP), the rebinding ability and oxygen-releasing capabilities of the modified MSP were not altered, in spite of changes of MSP surface Lys residues. Furthermore, far-ultraviolet circular dichroism and intrinsic fluorescence spectra analysis revealed that 0.

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The 1, 4, and 8 tyrosine (Tyr) residues on the PSII extrinsic 23 kDa protein were modified with 5, 10 or 40 mM N-acetylimidazole (NAI) respectively. The amount of rebound NAI-modified extrinsic 23 kDa protein was 98%, 80%, and 5% of that in the unmodified protein, respectively. These results indicate that the Tyr residues are absolutely essential to reconstitution ability.

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Among vertebrates, only microchiropteran bats, cetaceans and some rodents are known to produce and detect ultrasounds (frequencies greater than 20 kHz) for the purpose of communication and/or echolocation, suggesting that this capacity might be restricted to mammals. Amphibians, reptiles and most birds generally have limited hearing capacity, with the ability to detect and produce sounds below approximately 12 kHz. Here we report evidence of ultrasonic communication in an amphibian, the concave-eared torrent frog (Amolops tormotus) from Huangshan Hot Springs, China.

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Photodynamics of two kinds of peripheral antenna complexes (LH2 of Rhodobacter sphaeroides, native LH2 (RS601) and B800-released LH2 where B800-BChls were partially or completely removed with different pH treatments), were studied using femtosecond pump-probe technique at different laser wavelengths. The obtained results for these samples with different B800/B850 ratios demonstrated that under the excitation around B800 nm, the photoabsorption and photobleaching dynamics were caused by the direct excitation of upper excitonic levels of B850 and excited state of B800 pigments, respectively. Furthermore, the removal of B800 pigments had little effect on the energy transfer processes of B850 interband/intraband transfer.

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A novel photoelectrode (PE) consisting of the pigment-exchanged photosynthetic reaction center (RC) trapped on the mesoporous WO3-TiO2 film was fabricated to facilitate bio-photoelectric conversion by manipulating the excitation relaxation of the proteins.

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High hydrostatic pressure combined with various spectroscopies is a powerful technique to study protein folding. An ideal model system for protein folding studies should have the following characteristics. (1) The protein should be sensitive to pressure, so that the protein can be unfolded under mild pressure.

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The oxidation of bacteriochlorophylls (BChls) in peripheral light-harvesting complexes (LH2) from Rhodobacter sphaeroides was investigated by spectroelectrochemistry of absorption, fluorescence emission, and femtosecond (fs) pump-probe, with the aim obtaining information about the effect of in situ electrochemical oxidation on the pigment-protein arrangement and energy transfer within LH2. The experimental results revealed that: (a) the generation of the BChl radical cation in both B800 and B850 rings dramatically induced bleaching of the characteristic absorption in the NIR region and quenching of the fluorescence emission from the B850 ring for the electrochemical oxidized LH2; (b) the BChl-B850 radical cation might act as an additional channel to compete with the unoxidized BChl-B850 molecules for rapidly releasing the excitation energy, however the B800-B850 energy transfer rate remained almost unchanged during the oxidation process.

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This review describes the recent progress in understanding of light harvesting complexes and reaction centers from purple bacteria. Emphasis is paid on the structure of two light harvesting complexes, inner or outer, and the mechanism of the transfer of excited energy among relative pigments (Fig.1).

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To determine the contribution of charged amino acids to binding with the photosystem II complex (PSII), the amino or carboxyl groups of the extrinsic 18 kDa protein were modified with N-succinimidyl propionate (NSP) or glycine methyl ester (GME) in the presence of a water-soluble carbodiimide, respectively. Based on isoelectric point shift, 4-10 and 10-14 amino groups were modified in the presence of 2 and 4 mM NSP, respectively. Similarly, 3-4 carboxyl groups were modified by reaction with 100 mM GME.

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Direct EPR evidence of the photo-generation of superoxide radicals (O(2) (-.)) was obtained by using a novel spin trapping probe in spinach Photosystem II (PS II) membrane fragments. The production of O(2) (-.

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The first research paper on photosynthesis in China was published by T.T. Li(2) in 1929.

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In this paper an acetonitrile-induced unfolding of the manganese-stabilizing protein (MSP) of photosystem II was discovered. More distinct unfolding states of MSP were identified than previously by using mainly electrospray ionization mass spectrometry (ESI-MS), together with fluorescence spectra and far-UV circular dichroism (CD) at pH 2.0, 6.

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Novel three-dimensional wormlike mesoporous WO(3)-TiO(2) films with tailored pore size (approximately 7.1 nm) were applied to prepare the bio-photoelectrodes (Bio-PEs) through direct entrapping the bacteria photosynthetic reaction center (RC) proteins. These mesoporous WO(3)-TiO(2) films exhibited unique characteristics in the specific loading of RC with high activity retained.

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The primary mechanism of growth difference of cucumber (Cucumis sativus L.) seedlings cultured under sulfur lamp and xenon lamp in a phytotron was investigated. Compared with cucumber seedlings grown under xenon lamp, those under sulfur lamp were shorter, and the cell number in the middle hypocotyls epidermis and cortex of them were more (Fig.

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To study its contribution to the assembly of the green plant manganese stabilizing protein (MSP) into photosystem II (PSII), tyrosine residues were specifically acetylated using N-acetylimidazole (NAI). In soluble MSP, three groups of Tyr residues could be differentiated by NAI acetylation: approximately 5 (actually approximately 5.2) Tyr residues could be easily acetylated (superficial), 1-2 Tyr residues could be acetylated when the NAI concentration was sufficiently high (superficially buried), and 1-2 Tyr residues could only be acetylated in the presence of the denaturant, urea (deeply buried).

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Article Synopsis
  • The study examined how different light sources (xenon vs. sulfur lamps) affect the growth of cotton plants (Gossypium hirsutum cv. Xuzhou 142).
  • Utilization of sulfur lamps was found to reduce excessive elongation of the hypocotyl and enhance the growth of epidermis and cortex cells.
  • The results indicated that sulfur lamp illumination resulted in more branches, buds, and bolls, promoting better conditions for cotton yield production.
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Pressure-induced unfolding of 23-kDa protein from spinach photosystem II has been systematically investigated at various experimental conditions. Thermodynamic equilibrium studies indicate that the protein is very sensitive to pressure. At 20 degrees C and pH 5.

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Carotenoids in the peripheral light-harvesting complexes (LH2) of the green mutant (GM309) of Rhodobacter sphaeroides were identified as containing neurosporenes, which lack the polar CH(3)O group, compared to spheroidenes in native-LH2 of R. sphaeroides 601. After LH2 complexes were treated with 1-anilino-8-naphthalene sulfonate (ANS), new energy transfer pathways from ANS or tryptophan to carotenoids were discovered in both native- and GM309-LH2.

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A green mutant was obtained among the chemically induced mutants of Rhodobacter sphaeroides 601 (RS601) and named GM309. A blue shift of 20 nm of the carotenoid absorption spectrum was found in the light-harvesting complex II (LH2) of GM309. Different from LH2 of RS601, it was found that the carotenoids in GM309-LH2 changed to be neurosporene by mutation.

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In this paper, we analyzed the pH-induced changes in the conformational states of the manganese-stabilizing protein (MSP) of photosystem II. Distinct conformational states of MSP were identified using fluorescence spectra, far-UV circular dichroism, and pressure-induced unfolding at varying suspension pH values, and four different conformational states of MSP were clearly distinguished using the center of fluorescence spectra mass when suspension pH was altered from 2 to 12. MSP was completely unfolded at a suspension pH above 11 and partly unfolded below a pH of 3.

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Several groups of mammals such as bats, dolphins and whales are known to produce ultrasonic signals which are used for navigation and hunting by means of echolocation, as well as for communication. In contrast, frogs and birds produce sounds during night- and day-time hours that are audible to humans; their sounds are so pervasive that together with those of insects, they are considered the primary sounds of nature. Here we show that an Old World frog (Amolops tormotus) and an oscine songbird (Abroscopus albogularis) living near noisy streams reliably produce acoustic signals that contain prominent ultrasonic harmonics.

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A successful study on the secondary structure of the isolated photosystem II (PSII) particles with the Fourier transform infrared spectroscopy is reported in this paper. The beta condensation effect is obviously characterized by infrared absorption spectra. The infrared spectra of both living protein and beta condensed protein samples are measured at room temperature.

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The unfolding of 23kD (P23k) protein isolated from spinach photosystem II particle was studied by high pressure and fluorescence spectroscopy. The thermal equilibrium study indicated that the protein could be totally unfolded by 180 or 160 MPa at 20 degrees C and 3 degrees C, respectively. The standard free energy and standard volume change of the protein for unfolding at 20 degrees C is 23.

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We have studied the reaction native left arrow over right arrow denatured for the 33-kDa protein isolated from photosystem II. Sucrose and glycerol have profound effects on pressure-induced unfolding. The additives shift the equilibrium to the left; they also cause a significant decrease in the standard volume change (DeltaV).

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