Characterization of red-shifted phycobilisomes isolated from the chlorophyll f-containing cyanobacterium Halomicronema hongdechloris
2016 (English)In: Biochimica et Biophysica Acta - Bioenergetics, ISSN 0005-2728, E-ISSN 1879-2650, Vol. 1857, no 1, 107-114 p.Article in journal (Refereed) PublishedText
Phycobilisomes are the main light-harvesting protein complexes in cyanobacteria and some algae. It is commonly accepted that these complexes only absorb green and orange light, complementing chlorophyll absorbance. Here, we present a new phycobilisome derived complex that consists only of allophycocyanin core subunits, having red-shifted absorption peaks of 653 and 712 nm. These red-shifted phycobiliprotein complexes were isolated from the chlorophyll f-containing cyanobacterium, Halomicronema hongdechloris, grown under monochromatic 730 nm-wavelength (far-red) light. The 3D model obtained from single particle analysis reveals a double disk assembly of 120-145 angstrom with two alpha/beta allophycocyanin trimers fitting into the two separated disks. They are significantly smaller than typical phycobilisomes formed from allophycocyanin subunits and core-membrane linker proteins, which fit well with a reduced distance between thylakoid membranes observed from cells grown under far-red light. Spectral analysis of the dissociated and denatured phycobiliprotein complexes grown under both these light conditions shows that the same bilin chromophore, phycocyanobilin, is exclusively used. Our findings show that red-shifted phycobilisomes are required for assisting efficient far-red light harvesting. Their discovery provides new insights into the molecular mechanisms of light harvesting under extreme conditions for photosynthesis, as well as the strategies involved in flexible chromatic acclimation to diverse light conditions.
Place, publisher, year, edition, pages
Elsevier, 2016. Vol. 1857, no 1, 107-114 p.
Phycobilisome, Complementary chromatic acclimation, Far-red light, Small angle neutron scattering, Photosynthesis, Cyanobacteria
Biochemistry and Molecular Biology Biophysics
IdentifiersURN: urn:nbn:se:kth:diva-180482DOI: 10.1016/j.bbabio.2015.10.009ISI: 000366771700012ScopusID: 2-s2.0-84947053021OAI: oai:DiVA.org:kth-180482DiVA: diva2:895275
QC 201601182016-01-182016-01-142016-01-18Bibliographically approved