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Effects of lipids on the rate-limiting steps in the dark-to-light transition of Photosystem II core complex of Thermostichus vulcanus.


ABSTRACT: In our earlier works, we have shown that the rate-limiting steps, associated with the dark-to-light transition of Photosystem II (PSII), reflecting the photochemical activity and structural dynamics of the reaction center complex, depend largely on the lipidic environment of the protein matrix. Using chlorophyll-a fluorescence transients (ChlF) elicited by single-turnover saturating flashes, it was shown that the half-waiting time (Δτ 1/2) between consecutive excitations, at which 50% of the fluorescence increment was reached, was considerably larger in isolated PSII complexes of Thermostichus (T.) vulcanus than in the native thylakoid membrane (TM). Further, it was shown that the addition of a TM lipid extract shortened Δτ 1/2 of isolated PSII, indicating that at least a fraction of the 'missing' lipid molecules, replaced by detergent molecules, caused the elongation of Δτ 1/2. Here, we performed systematic experiments to obtain information on the nature of TM lipids that are capable of decreasing Δτ 1/2. Our data show that while all lipid species shorten Δτ 1/2, the negatively charged lipid phosphatidylglycerol appears to be the most efficient species - suggesting its prominent role in determining the structural dynamics of PSII reaction center.

SUBMITTER: Magyar M 

PROVIDER: S-EPMC10991767 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature

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Effects of lipids on the rate-limiting steps in the dark-to-light transition of Photosystem II core complex of <i>Thermostichus vulcanus</i>.

Magyar Melinda M   Akhtar Parveen P   Sipka Gábor G   Domonkos Ildikó I   Han Wenhui W   Li Xingyue X   Han Guangye G   Shen Jian-Ren JR   Lambrev Petar H PH   Garab Győző G  

Frontiers in plant science 20240321


In our earlier works, we have shown that the rate-limiting steps, associated with the dark-to-light transition of Photosystem II (PSII), reflecting the photochemical activity and structural dynamics of the reaction center complex, depend largely on the lipidic environment of the protein matrix. Using chlorophyll-<i>a</i> fluorescence transients (ChlF) elicited by single-turnover saturating flashes, it was shown that the half-waiting time (Δ<i>τ</i> <sub>1/2</sub>) between consecutive excitations  ...[more]

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