Spectroscopic properties of the reaction center and of the 47 kDa chlorophyll protein of Photosystem II

Dorssen, R.J. van; Breton, Jacques; Plijter, Johan J.; Satoh, Kimiyuki; Gorkom, Hans J. van; Amesz, J.

doi:10.1016/0005-2728(87)90048-x

Cited by 169 publications

(175 citation statements)

References 24 publications

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“…This is consistent with the environment deduced by analysis of x-ray crystallographic structures (30,31,37). In PSII-RCs, Cars are mainly surrounded by amino acids and are quite distant from other cofactors; they exhibit only low rates of energy transfer to the bound Chl molecules (27,33,34). On the other hand, the luteins in LHCII are in very close contact with the LHCII-bound Chl molecules, both at the levels of their end cycles and of the conjugated CϭC chain (37).…”

Section: Lutein Molecules In Lhcii-supporting

confidence: 88%

“…3). Linear dichroism experiments showed that these peaks correspond to distinct Car molecules, with different orientations relative to the membrane plane (27), and considering their position, they must be attributed to the 0 -0 sublevel of the absorption transition of each molecule. Although the resolution between these peaks becomes much lower at room temperature, the overall position of the Car absorption transition appears not to shift by more than a few nanometers between low temperature and room temperature (see Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The PSII-RC binds two ␤-carotene molecules, which at low temperature have their main absorption transition at 489 and 507 nm (27)(28)(29), the former being perpendicular and the latter parallel to the membrane plane (27,30,31). These Car molecules exhibit only limited singlet-singlet energy transfer to Chls and essentially no quenching of Chl triplets, but are both able to transfer an electron to the oxidized primary electron donor, albeit with very low efficiency (27,(32)(33)(34)(35). LHCII is assembled into a trimeric form in the photosynthetic membrane, with each monomer containing two lutein molecules whose binding sites are related by pseudo-symmetry.…”

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confidence: 99%

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Mechanisms Underlying Carotenoid Absorption in Oxygenic Photosynthetic Proteins

Mendes-Pinto

Galzerano

Telfer

et al. 2013

Journal of Biological Chemistry

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Background: Tuning of carotenoid function, through modulation of their electronic properties, is seen throughout Nature. Results: Two photosynthetic proteins are able to modulate the effective conjugation length of bound carotenoid cofactors. Conclusion: Altering the conformation of conjugated end cycles via steric hindrance provides a means of tuning the electronic properties of carotenoids. Significance: A novel mechanism tuning the functional properties of carotenoids is revealed.

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Section: Lutein Molecules In Lhcii-supporting

confidence: 88%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

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Mechanisms Underlying Carotenoid Absorption in Oxygenic Photosynthetic Proteins

Mendes-Pinto

Galzerano

Telfer

et al. 2013

Journal of Biological Chemistry

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“…Therefore, destabilization of either chlorophyll-binding protein due to a lack of appropriate pigment binding may have long-distance effects on PS I1 properties. Indeed, a loss of CP43 leads to a loss of oxygen evolution activity and to a great decrease in the amount of PS I1 present in thylakoids [13, 141. As possibly expected, the similarity between CP47 and CP43 does not hold for His114 of CP47 versus His119 of CP43: His114 of CP47 appears to be associated with the 695 nm fluorescence emission peak observed at low temperature that is thought to originate from a very small number (possibly just one) of chlorophyll molecules in CP47 [31]. Mutation of His114 in CP47 to glutamine or asparagine was found to shift the emission maximum of the 695 nm peak to lower wavelengths, and mutation of His114 to tyrosine led to a large decrease in the amount of PS I1 that could be detected [22].…”

Section: Discussionmentioning

confidence: 71%

Mutational Studies on Conserved Histidine Residues in the Chlorophyll‐Binding Protein CP43 of Photosystem II

Manna

Vermaas

1997

European Journal of Biochemistry

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Two chlorophyll-binding antenna proteins in the photosystem I1 core, CP43 and CP47, are structurally similar and are thought to have evolved from a common ancestor. Several conserved histidine residues in hydrophobic regions of CP47 have been shown to be important for photosystem I1 structure, function, and energy transfer. The purpose of this study was to determine whether similarly located histidine residues in CP43 function in a similar way. Three conserved histidine residues in presumed membranespanning regions of CP43, His40, HislO.5, and Hisll9, were mutated to glutamine (Q) and tyrosine (Y). The strains H105Q, H119Q, and H119Y were photoautotrophs whereas H40Q, H40Y, and H105Y were obligate photoheterotrophs. The H40Y and H105Y strains lacked detectable amounts of photosystem I1 reaction centers and hence could not evolve oxygen whereas H40Q retained a significant amount of photosystem I1 and oxygen evolution capacity. The observation that mutation of histidine residues to tyrosine has more drastic effects than mutation of these residues to glutamine is in agreement with results obtained for CP47 and suggests the involvement of these residues in chlorophyll binding. The drastic functional changes observed upon mutating His40 and His105 of CP43 are similar to those observed when mutating the corresponding histidine residues in CP47, thus suggesting that the similarity between CP43 and CP47 extends to the relative importance of functionally relevant residues. Interestingly, the His40+Gln mutation in CP43 had significant effects on photosystem I1 electron transfer in that it affected the thermodynamics of Qi oxidation by QB and increased the charge recombination rate between Q i and donor side components. This indicates that relatively minor changes in CP43 can significantly impact the properties of the photosystem I1 reaction center. The implications of this finding are discussed.Keywords: thylakoid ; photosynthesis ; photosystem 11; cyanobacteria; chlorophyll-binding protein Photosystem I1 (PS 11 A possibly significant difference between the CP47 and CP43 polypeptides is that CP43 can be removed easily from the , 3-(3,4-dichlorophenyi)-l ,I-dimethylurea; LHC 11: light-harvesting complex 11; PS, photosystem. PS I1 core either by mild chaotropic agents such as potassium thiocyanate [8] or by additional detergent treatment [9, 101 indicating a relatively loose association with PS 11. However, under these conditions the CP47 protein remains associated with the D1, D2, and cytochrome b,,, complex, suggesting that CP47 is closer to the PS I1 reaction center than CP43. This is in agreement with the conclusion drawn from comparisons of electron micrographs of isolated PS I1 reaction centers with and without CP43 11 11.Nonetheless, CP43 appears to be important for various as- short deletions in the long lumenal hydrophilic loop between membrane spanning helices V and VI showed that the integrity of this loop is an important factor for oxygen evolution and PS I1 stability [15]. In addition, introduction of parts of...

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“…The peak at 648 nm and the two shoulders at 665 nm and 685 nm were due to PC, APC, and the terminal emitter of the PBS, respectively (2). The peak at 725 nm was due to PS I, and we have assigned the shoulder at 695 nm to PS II (21,22). The spectrum of dark-grown cells still retained the uorescence emissions (648, 665, and 685 nm) from PC, APC, and the terminal emitter of the PBS.…”

Section: Spectroscopic Characteristics Of Chll ¡ Cells Grown In Darknmentioning

confidence: 83%

Effects of Chlorophyll Availability on Phycobilisomes in Synechocystis sp. PCC 6803

Mao

et al. 1999

IUBMB Life

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SummaryInactivation of the chlL gene in Synechocystis sp. PCC 6803 resulted in negligible chlorophyll content when the mutant was grown in darkness. Upon phycocyanin excitation at 580 nm, the 77K uorescence spectrum of dark-grown cells showed three peaks at 648 nm, 665 nm, and 685 nm, this last being the largest. This re ects the functional presence of major components of phycobilisomes, including phycocyanin, allophycocyanin, and the terminal emitter, and ef cient energy transfer between these components. As expected, no uorescence emission peaks corresponding to chlorophyll in the photosystems were observed. Intact phycobilisomes could be isolated from the dark-grown chlL-deletion mutant. However, the phycobilisomes had a lower ef ciency of energy transfer than did those isolated from the light-grown mutant, probably because of a decreased phycobilisome stability in the absence of chlorophyll. Exposing the dark-grown chlL-deletion mutant to light triggered the biosynthesis of chlorophyll. For the rst 6 h in the light, upon phycocyanin excitation at 580 nm, the 77K uorescence emission spectrum of greening cells was identical to that of dark-grown cells that lacked signi cant amounts of chlorophyll. With increased chlorophyll synthesis, gradual energy transfer from phycobilisomes to the two photosystems can be demonstrated. IUBMB Life, 48: 625-630, 1999

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Spectroscopic properties of the reaction center and of the 47 kDa chlorophyll protein of Photosystem II

Cited by 169 publications

References 24 publications

Mechanisms Underlying Carotenoid Absorption in Oxygenic Photosynthetic Proteins

Mechanisms Underlying Carotenoid Absorption in Oxygenic Photosynthetic Proteins

Mutational Studies on Conserved Histidine Residues in the Chlorophyll‐Binding Protein CP43 of Photosystem II

Effects of Chlorophyll Availability on Phycobilisomes in Synechocystis sp. PCC 6803

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