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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Kuzminov, F. I. Bolychevtseva, Yu V. Elanskaya, I. V. Karapetyan, N. V. |
| Description | Author Affiliation: Kuzminov FI ( A.N. Bach Institute of Biochemistry RAS, 119071 Moscow, Russia); Bolychevtseva YV ( A.N. Bach Institute of Biochemistry RAS, 119071 Moscow, Russia.); Elanskaya IV ( Faculty of Biology, M.V. Lomonosov Moscow State University, 119991 Moscow, Russia.); Karapetyan NV ( A.N. Bach Institute of Biochemistry RAS, 119071 Moscow, Russia.) |
| Abstract | Long-wavelength allophycocyanin (APC) subunits in cyanobacteria (APCD, APCE, and APCF) are required for phycobilisome (PBS) assembly, stability, and energy transfer to photosystems. Here we studied fluorescence properties of PBS in vivo, using Synechocystis PCC 6803 mutant cells deficient in both photosystems and/or long-wavelength APC subunits. At room temperature, an absence of APCD and APCF subunits resulted in â¼2-fold decrease of long-wavelength APC (APC680) fluorescence. In 77K fluorescence spectra, we observed only a slight shift of long-wavelength emission. However, 77K fluorescence of a PSI/PSII/APCF-less mutant was also characterized by increased emission from short-wavelength APC, which suggested the importance of this subunit in energy transfer from APC660 to APC680. Under blue-green actinic light, all mutants showed significant non-photochemical fluorescence quenching of up to 80% of the initial dark fluorescence level. Based on the mutants' quenching spectra, we determined quenching to originate from the pool of short-wavelength APC, while the spectral data alone was not sufficient to make unambiguous conclusion on the involvement of long-wavelength APC in non-photochemical quenching. Using a model of quenching center formation, we determined interaction rates between PBS and orange carotenoid protein (OCP) in vivo. Absence of APCD or APCF subunits had no effect on the rates of quenching center formation confirming the data obtained for isolated OCP-PBS complexes. Thus, although APCD and APCF subunits were required for energy transfer in PBS in vivo, their absence did not affect rates of OCP-PBS binding. |
| File Format | HTM / HTML |
| ISSN | 10111344 |
| Volume Number | 133 |
| e-ISSN | 18732682 |
| Journal | Journal of Photochemistry and Photobiology B: Biology |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2014-04-05 |
| Publisher Place | Switzerland |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Biology Bacterial Proteins Chemistry Phycobilisomes Phycocyanin Synechocystis Metabolism Genetics Kinetics Light Mutation Photosystem I Protein Complex Photosystem Ii Protein Complex Spectrometry, Fluorescence Temperature Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Radiology, Nuclear Medicine and Imaging Biophysics Radiological and Ultrasound Technology Radiation |
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