In the mutant CC-1047 of Chlamydomonas reinhardtii, LDS-PAGE showed that the chlorophyll-protein complex I (CPI) is almost absent. The mutant could not grow in a culture medium without organic carbon source while the wild type (WT) C. reinhardtii grew quickly. When an organic carbon source was added into the culture medium, the mutant grew almost as well as WT. The rate of photosystem 1 (PS1) electron transport (DCPIP→MV) and the rate of whole chain electron transport (H2O→MV) of chloroplasts of the CC-1047 mutant were both lower than those of WT. The photophosphorylation activity, photosynthetic O2 evolution rate, and rate of NADP+ photoreduction of CC-1047 were also much lower than the activities of WT. There were some differences in ATPase activity between the mutant and WT. Two different activation ways were used to activate the latent ATPase using methanol and dithiothreitol (DTT) as activation substrate. More methanol and DTT were required for the mutant than WT to obtain the maximum activity. Thus the photosynthetic apparatus could not operate normally when CPI was absent because of the abnormal PS1 electron transport. Meanwhile, the other adjacent complexes of the thylakoid membrane, for example, ATP synthase complex, were slightly affected. and Qing-Xiu Tang, Zhang-Lin Ni, Jia-Mian Wei.
The protein secondary structure and pigments' microenvironment in photosystem 1 (PS1) complexes were studied in the temperature range of 25-80 °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 °C. However, apparent conformational changes occurred at 60 °C and further continued at 70 and 80 °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 °C). When temperature reached 70 and 80 °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 °C and was lost completely at 80 °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. and Z.-H. Hu ... [et al.].
Net photosynthetic rate (PN), transpiration rate (E), water use efficiency (WUE), stomatal conductance (gs), and stomatal limitation (Ls) were investigated in two Syringa species. The saturation irradiance (SI) was 400 µmol m-2s-1 for S. pinnatifolia and 1 700 µmol m-2s-1 for S. oblata. Compared with S. oblata, S. pinnatifolia had extremely low gs. Unlike S. oblata, the maximal photosynthetic rate (Pmax) in S. pinnatifoliaoccurred around 08:00 and then fell down, indicating this species was sensitive to higher temperature and high photosynthetic photon flux density. However, such phenomenon was interrupted by the leaf development rhythms before summer. A relatively lower PN together with a lower leaf area and shoot growth showed the capacity for carbon assimilation was poorer in S. pinnatifolia. and H. X. Cui ... [et al.].