Regulation of the Distribution of Chlorophyll and Phycobilin-Absorbed Excitation Energy in Cyanobacteria. A Structure-Based Model for the Light State Transition

• Published in: Plant physiology (Bethesda) 2002-11, Vol.130 (3), p.1201-1212
• Main Authors: Michael D. Mc Connell, Randy Koop, Sergej Vasil'ev, Bruce, Doug
• Format: Article
• Language: English
• Subjects: Bioenergetics and Photosynthesis; Chlorophyll; Chlorophyll - metabolism; Chlorophyll - radiation effects; Chromophores; Cyanobacteria; Cyanobacteria - genetics; Cyanobacteria - metabolism; Cyanobacteria - radiation effects; Cyanophyta; Emission spectra; Emission spectroscopy; Energy; Energy transfer; Environmental conditions; Fluorescence; Light; Models, Biological; Mutation; Photosynthesis; Photosynthesis - physiology; Photosynthesis - radiation effects; Photosynthetic Reaction Center Complex Proteins - metabolism; Photosynthetic Reaction Center Complex Proteins - radiation effects; Phycobilins; Phycocyanin - metabolism; Phycocyanin - radiation effects; Pigments; Pyrroles - metabolism; Pyrroles - radiation effects; Room temperature; Spectrometry, Fluorescence; Synechococcus; Synechocystis; Tetrapyrroles; Thylakoids; Visible spectrum; Wavelengths
• ISSN: 0032-0889; 1532-2548
• DOI: 10.1104/pp.009845

The light state transition regulates the distribution of absorbed excitation energy between the two photosystems (PSs) of photosynthesis under varying environmental conditions and/or metabolic demands. In cyanobacteria, there is evidence for the redistribution of energy absorbed by both chlorophyll (Chl) and by phycobilin pigments, and proposed mechanisms differ in the relative involvement of the two pigment types. We assayed changes in the distribution of excitation energy with 77K fluorescence emission spectroscopy determined for excitation of Chl and phycobilin pigments, in both wild-type and state transition-impaired mutant strains of Synechococcus sp. PCC 7002 and Synechocystis sp. PCC 6803. Action spectra for the redistribution of both Chl and phycobilin pigments were very similar in both wild-type cyanobacteria. Both state transition-impaired mutants showed no redistribution of phycobilin-absorbed excitation energy, but retained changes in Chl-absorbed excitation. Action spectra for the Chl-absorbed changes in excitation in the two mutants were similar to each other and to those observed in the two wild types. Our data show that the redistribution of excitation energy absorbed by Chl is independent of the redistribution of excitation energy absorbed by phycobilin pigments and that both changes are triggered by the same environmental light conditions. We present a model for the state transition in cyanobacteria based on the x-ray structures of PSII, PSI, and allophycocyanin consistent with these results.