期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 117, 期 38, 页码 11000-11006出版社
AMER CHEMICAL SOC
DOI: 10.1021/jp309570u
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Cyanobacteria are oxygen-evolving photosynthetic organisms that harvest sunlight and convert excitation energy into chemical energy. Most of the light is absorbed by large light harvesting complexes called phycobilisomes (PBs). In high-light conditions, cyanobacteria switch on a photoprotective mechanism called non-photochemical quenching (NPQ): During this process, absorption of blue-green light transforms the inactive orange form of the orange carotenoid protein OCP (OCP degrees) into the red active form OCPt that subsequently binds to the PB, resulting in a substantial loss of excitation energy and corresponding decrease of the fluorescence. In wild-type cells, the quenching site is a bilin chomophore that fluoresces at 660 nm and which is called APC(Q)(66). In the present work, we studied NPQ in two different types of mutant cells (CB and CK) that possess significantly truncated PBs, using spectrally resolved picosecond fluorescence spectroscopy. The results are in very good agreement with earlier in vitro experiments on quenched and unquenched PBs, although the fraction of quenched PBs is far lower in vivo. It is also lower than the fraction of PBs that is quenched in wild-type cells, but the site, rate, and location of quenching appear to be very similar.
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