Characterization of low-energy chlorophylls in the PSI-LHCI supercomplex from Chlamydomonas reinhardtii. A site-selective fluorescence study.
نویسندگان
چکیده
Almost all photosystem I (PSI) complexes from oxygenic photosynthetic organisms contain chlorophylls that absorb at longer wavelength than that of the primary electron donor P700. We demonstrate here that the low-energy pool of chlorophylls in the PSI-LHCI complex from the green alga Chlamydomonas reinhardtii, containing five to six pigments, is significantly blue-shifted (A(max) at 700 nm at 4 K) compared to that in the PSI core preparations from several species of cyanobacteria and in PSI-LHCI particles from higher plants. This makes them almost isoenergetic with the primary donor. However, they keep the other characteristic features of "red" chlorophylls: clear spectral separation from the bulk chlorophylls, big Stokes shift revealing pronounced electron-phonon coupling, and large homogeneous and inhomogeneous broadening of approximately 170 and approximately 310 cm(-1), respectively.
منابع مشابه
The High Efficiency of Photosystem I in the Green Alga Chlamydomonas reinhardtii Is Maintained after the Antenna Size Is Substantially Increased by the Association of Light-harvesting Complexes II.
Photosystems (PS) I and II activities depend on their light-harvesting capacity and trapping efficiency, which vary in different environmental conditions. For optimal functioning, these activities need to be balanced. This is achieved by redistribution of excitation energy between the two photosystems via the association and disassociation of light-harvesting complexes (LHC) II, in a process kn...
متن کاملPSI–LHCI of Chlamydomonas reinhardtii: Increasing the absorption cross section without losing efficiency
Photosystem I (PSI) is an essential component of photosynthetic membranes. Despite the high sequence and structural homologies, its absorption properties differ substantially in algae, plants and cyanobacteria. In particular it is characterized by the presence of low-energy chlorophylls (red forms), the number and the energy of which vary in different organisms. The PSI-LHCI (PSI-light harvesti...
متن کاملCP29, a monomeric light-harvesting complex II protein, is essential for state transitions in Chlamydomonas reinhardtii.
In oxygen-evolving photosynthesis, the two photosystems, photosystem I (PSI) and photosystem II (PSII), function in parallel, and their excitation levels must be balanced to maintain an optimal photosynthetic rate under various light conditions. State transitions balance excitation energy between the two photosystems by redistributing light-harvesting complex II (LHCII) proteins. Here we descri...
متن کاملPhotosystem I of Chlamydomonas reinhardtii contains nine light-harvesting complexes (Lhca) located on one side of the core.
In this work we have purified the Photosystem I (PSI) complex of Chlamydomonas reinhardtii to homogeneity. Biochemical, proteomic, spectroscopic, and structural analyses reveal the main properties of this PSI-LHCI supercomplex. The data show that the largest purified complex is composed of one core complex and nine Lhca antennas and that it contains all Lhca gene products. A projection map at 1...
متن کاملThe light-harvesting complex of photosystem I in Chlamydomonas reinhardtii: protein composition, gene structures and phylogenic implications.
Light-harvesting chlorophyll a/b-binding proteins (LHCI) associated with photosystem I (PSI) and the genes encoding these proteins have been characterized in the unicellular green alga Chlamydomonas reinhardtii, extending previous studies of the PSII-LHCII [Teramoto et al. (2001) Plant Cell Physiol. 42: 849]. In order to assign LHCI proteins in the thylakoid membranes, the PSI-LHCI supercomplex...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The journal of physical chemistry. B
دوره 109 44 شماره
صفحات -
تاریخ انتشار 2005