Journal
PHOTOSYNTHESIS RESEARCH
Volume 137, Issue 2, Pages 307-320Publisher
SPRINGER
DOI: 10.1007/s11120-018-0505-0
Keywords
Cyanobacteria; Spectrally resolved fluorometry; Singular value decomposition; Time-resolved spectroscopy; Plastoquinone pool; Cyclic electron flow
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Funding
- Dutch Ministry of Economic Affairs
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Photosynthetic activity and respiration share the thylakoid membrane in cyanobacteria. We present a series of spectrally resolved fluorescence experiments where whole cells of the cyanobacterium Synechocystis sp. PCC 6803 and mutants thereof underwent a dark-to-light transition after different dark-adaptation (DA) periods. Two mutants were used: (i) a PSI-lacking mutant (Delta PSI) and (ii) M55, a mutant without NAD(P)H dehydrogenase type-1 (NDH-1). For comparison, measurements of the wild-type were also carried out. We recorded spectrally resolved fluorescence traces over several minutes with 100 ms time resolution. The excitation light was at 590 nm so as to specifically excite the phycobilisomes. In Delta PSI, DA time has no influence, and in dichlorophenyl-dimethylurea (DCMU)-treated samples we identify three main fluorescent components: PB-PSII complexes with closed (saturated) RCs, a quenched or open PB-PSII complex, and a PB-PSII 'not fully closed.' For the PSI-containing organisms without DCMU, we conclude that mainly three species contribute to the signal: a PB-PSII-PSI megacomplex with closed PSII RCs and (i) slow PB -> PSI energy transfer, or (ii) fast PB -> PSI energy transfer and (iii) complexes with open (photochemically quenched) PSII RCs. Furthermore, their time profiles reveal an adaptive response that we identify as a state transition. Our results suggest that deceleration of the PB -> PSI energy transfer rate is the molecular mechanism underlying a state 2 to state 1 transition.
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