Photosynthetic energy conservation investigated by thermoluminescence. Activation energies and half-lives of thermoluminescence bands of chloroplasts determined by mathematical resolution of glow curves

Vass, Imre; Horváth, Gábor; Herczeg, T.; Demeter, S.

doi:10.1016/0005-2728(81)90134-1

Cited by 127 publications

(59 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This value is comparable to the t1 ͞2 in vivo as assayed in spinach leaf disks (Fig. 2) as well as to values reported before for spinach thylakoids assayed by both TL and the oxygen flash yield techniques (24,25).…”

Section: Resultssupporting

confidence: 90%

“…Following single turnover excitation after dark adaptation most of RCII are in the S 2 state (22,25). Under the conditions used in these experiments we did not resolve the rates of Q B…”

Section: Resultsmentioning

confidence: 77%

“…•Ϫ ͞S 2,3 states (25). Following single turnover excitation after dark adaptation most of RCII are in the S 2 state (22,25).…”

Section: Resultsmentioning

confidence: 99%

“…•Ϫ or Q A •Ϫ ͞S 2,3 states generated by single turnover flashes that decay by charge recombination (25), and (ii) to determine the relationship between the number of flashes delivered at a given rate and the resulting PSII inactivation and degradation of the D1 protein.…”

Section: Resultsmentioning

confidence: 99%

See 3 more Smart Citations

Mechanism of photosystem II photoinactivation and D1 protein degradation at low light: The role of back electron flow

Keren

Berg

Kan

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

280

196

View full text Add to dashboard Cite

Light intensities that limit electron f low induce rapid degradation of the photosystem II (PSII) reaction center D1 protein. The mechanism of this phenomenon is not known. We propose that at low excitation rates back electron f low and charge recombination between the Q B• Following the discovery of the light dependent turnover of reaction center II (RCII) D1 protein (1), the process of excess light-induced photoinactivation and the related degradation of photosystem II (PSII) proteins (photoinhibition) were studied intensively. Significant progress toward understanding the mechanism(s) involved was achieved (reviewed in refs. [2][3][4]

show abstract

Section: Resultssupporting

confidence: 90%

“…Following single turnover excitation after dark adaptation most of RCII are in the S 2 state (22,25). Under the conditions used in these experiments we did not resolve the rates of Q B…”

Section: Resultsmentioning

confidence: 77%

“…•Ϫ ͞S 2,3 states (25). Following single turnover excitation after dark adaptation most of RCII are in the S 2 state (22,25).…”

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 2 more Smart Citations

Mechanism of photosystem II photoinactivation and D1 protein degradation at low light: The role of back electron flow

Keren

Berg

Kan

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

280

196

View full text Add to dashboard Cite

show abstract

“…We have suggested earlier [6], that the reactions resulting in ultraweak light emission of chloroplasts are, at some level, associated with a hypothesized slow back flow of electrons from NADPH to oxygen via, the plastoquinone pool: chlororespiration [20,21]. Supporting this assumption, the estimated 98 kJ/mol activation energy of ultraweak light emission is similar to the previously reported activation energies of other thylakoid membrane related electron-transport backreactions (80-90 k J/tool, in [22]). …”

Section: Discussionsupporting

confidence: 80%

Ultraweak photoemission from dark‐adapted leaves and isolated chloroplasts

Hideg¹,

Kobayashi²,

Inaba

1990

FEBS Letters

View full text Add to dashboard Cite

Dark‐adapted isolated spinach chloroplasts and leaves, unlike sub‐chloroplast fractions, are capable of emitting ultraweak light spontaneously (50–125 counts per cm2). The emission of leaves is due to two processes with activation energies of 97 and 25 kJ/mol while in isolated chloroplasts, it is the result of a single process (98 kJ/mol), as indicated by the Arrhenius plots of the intensity. Emission spectra demonstrate that the terminal step of these reactions is the excitation of chlorophyll in both samples. We suggest that the additional component in the ultraweak light emission of leaves may be related to mitochondria

show abstract

Environmental pH and a Glu364 to Gln mutation in the chlorophyll‐binding CP47 protein affect redox‐active TyrD and charge recombination in Photosystem II

et al. 2018

View full text Add to dashboard Cite

In Photosystem II, loop E of the chlorophyll‐binding CP47 protein is located near a redox‐active tyrosine, YD, forming a symmetrical analog to loop E in CP43, which provides a ligand to the oxygen‐evolving complex (OEC). A Glu364 to Gln substitution in CP47, near YD, does not affect growth in the cyanobacterium Synechocystis sp. PCC 6803; however, deletion of the extrinsic protein PsbV in this mutant leads to a strain displaying a pH‐sensitive phenotype. Using thermoluminescence, chlorophyll fluorescence, and flash‐induced oxygen evolution analyses, we demonstrate that Glu364 influences the stability of YD and the redox state of the OEC, and highlight the effects of external pH on photosynthetic electron transfer in intact cyanobacterial cells.

show abstract

Photosynthetic energy conservation investigated by thermoluminescence. Activation energies and half-lives of thermoluminescence bands of chloroplasts determined by mathematical resolution of glow curves

Cited by 127 publications

References 23 publications

Mechanism of photosystem II photoinactivation and D1 protein degradation at low light: The role of back electron flow

Mechanism of photosystem II photoinactivation and D1 protein degradation at low light: The role of back electron flow

Ultraweak photoemission from dark‐adapted leaves and isolated chloroplasts

Environmental pH and a Glu364 to Gln mutation in the chlorophyll‐binding CP47 protein affect redox‐active TyrD and charge recombination in Photosystem II

Contact Info

Product

Resources

About