15-Cis-?-carotene found in the reaction center of spinach Photosystem I

Bialek-Bylka, Grazyna E.; Hiyama, Tetsuo; Yumoto, Kenji; Koyama, Yasushi

doi:10.1007/bf00034785

Cited by 34 publications

(31 citation statements)

References 24 publications

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“…Previously, it was thought that, unlike the carotenoids bound in the reaction centers of the photosynthetic bacteria, p-carotene adopted an all-trans configuration (19). A new study by Bialek-Bylka et al (18) employing solvent extraction of p-carotene from spinach PSI1 reaction centers in complete darkness and subsequent HPLC analyses indicates that the carotenoid adopts a 15-cis configuration consistent with the central, mono-cis structure observed for carotenoids in all of the bacterial reaction centers.…”

Section: Structures Of Carotenoids In Photosynthetic Systemsmentioning

confidence: 99%

Carotenoids in Photosynthesis

Frank

Cogdell

1996

Photochem & Photobiology

892

644

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Section: Structures Of Carotenoids In Photosynthetic Systemsmentioning

confidence: 99%

Carotenoids in Photosynthesis

Frank

Cogdell

1996

Photochem & Photobiology

892

644

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“…The 15-cis b-carotene (Fig. 1b) was purified and analysed using HPLC method [1,17] prior to the measurements.…”

Section: Methodsmentioning

confidence: 99%

“…One of the most studied carotenoids is b-carotene. It can be found in mono-cis configuration in photosynthetic reaction centres, where is it responsible for the photo-protection of the photosynthetic apparatus [1][2][3]. b-carotene is present in all-trans configuration in the photosynthetic antenna complexes where it participates in the light harvesting together with chlorophylls [4][5][6].…”

Section: Introductionmentioning

confidence: 99%

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The thermal deactivation of all-trans and 15-cis beta-carotene-excited states in the ionic liquids without and with methylenoxy group

Pawlak

Szurkowski

Skrzypczak

et al. 2014

J Therm Anal Calorim

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Photoacoustic spectroscopy was used to study thermal (dark) paths of excited state deactivation of bcarotene in ionic liquids. The dark paths of excited state deactivation of all-trans and 15-cis b-carotene isomers are very important in photosynthesis and medicine. The photoacoustic measurements of b-carotene in traditional solvents are difficult due to fast evaporation of the solvent which leads to concentration fluctuation. Room temperature ionic liquids are good medium for temperature study due to their high thermal stability and low volatility. Dark deactivation of both b-carotene isomers in ionic liquids occurs in a similar way except for an additional path of deactivation of excited state 1 1 A g ? ('cis' peak). The thermal-excited state deactivation of all-trans and 15-cis bcarotene isomers is not sensitive to the ionic liquid structure, in contrast to the radiative path.

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“…2) (8). Carotenoids are essential for the normal development of photosynthetic membranes, for dissipation of light energy, and for protecting plants from excess light (3)(4)(5)15). Carotenoids quench singlet oxygen, and their absence is lethal in plants and oxygenic photosynthetic bacteria such as Synechocystis sp.…”

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confidence: 99%

Type II Isopentenyl Diphosphate Isomerase fromSynechocystissp. Strain PCC 6803

2004

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Open reading frame sll1556 in the cyanobacterium Synechocystis sp. strain 6803 encodes a putative type II isopentenyl diphosphate (IPP) isomerase. The His 6 -tagged protein was produced in Escherichia coli and purified by Ni 2؉ chromatography. The homotetrameric enzyme required NADPH, flavin mononucleotide, and Mg 2؉for activity; K m IPP was 52 M, and k cat IPP was 0.23 s ؊1 .The isomerization of isopentenyl diphosphate (IPP) to dimethylallyl diphosphate (DMAPP) is an essential reaction in the mevalonate (MVA) pathway to isoprenoids (13) and, although not essential, probably serves to balance the IPP and DMAPP pools in the methylerythritol phosphate (MEP) route (9). Two types of IPP isomerase are known. The type I enzyme, found in Eucarya and some of the Bacteria, is well characterized (16). Type II IPP isomerase, found in Archaea and some of the Bacteria, was discovered much more recently (10), and only a few studies of the protein have been reported. Analysis of the genome of Synechocystis sp. strain PCC 6803 indicated that the cyanobacterium synthesizes isoprenoid compounds by the MEP route. Although it was reported elsewhere that the bacterium does not have detectable IPP isomerase activity under phototrophic growth conditions (6, 7), open reading frame (ORF) sll1556 encodes a protein that is substantially similar to other type II IPP isomerases. We now report that purified ORF sll1556 protein is an active type II IPP isomerase.Evidence that Synechocystis sp. strain PCC 6803 ORF sll1556 encodes a functional type II IPP isomerase was obtained by complementation studies with Salmonella enterica serovar Typhimurium strain RMC29 (Table 1) (2). The chromosomal copy of idi (IPP isomerase) in RMC29 was disrupted with a chloramphenicol (CAM) marker, and dxs (deoxyxylulose synthase) was disrupted with a minioperon that includes the yeast genes required for biosynthesis of IPP from MVA and an ampicillin (AMP) marker. Thus, RMC29 is viable when supplemented with methylerythritol (ME) but does not grow on MVA unless idi activity is restored. RMC29 was transformed with plasmid pJMSB02278-8 bearing a copy of ORF sll1556 from Synechocystis sp. strain PCC 6803 and the expression plasmid without ORF sll1556. Both strains were resistant to AMP and expressed the plasmid-carried genes when induced with arabinose. As shown in Fig. 1, strains JMSB02278-8, JMSB0354, and RMC29 grew on LB broth-CAM-ME, demonstrating that they can utilize the MEP pathway to synthesize IPP and DMAPP without a functional IPP isomerase. Strains JMSB02278-8 and JMSB0354 contain plasmids conferring resistance to AMP and grew on LB-AMP-CAM-ME, while RMC29 did not. Only JMSB02278-8 grew on LB-AMP-CAM-MEV-arabinose by utilizing the IPP isomerase encoded by ORF sll1556 from Synechocystis sp. strain PCC 6803 to convert IPP synthesized from MVA to DMAPP.Nickel-nitrilotriacetic acid affinity chromatography of the supernatant from a cell extract of Escherichia coli strain JMSB0373a yielded a protein that gave a single band upon sodium dodecyl sulfate-polyacrylami...

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15-Cis-?-carotene found in the reaction center of spinach Photosystem I

Cited by 34 publications

References 24 publications

Carotenoids in Photosynthesis

Carotenoids in Photosynthesis

The thermal deactivation of all-trans and 15-cis beta-carotene-excited states in the ionic liquids without and with methylenoxy group

Type II Isopentenyl Diphosphate Isomerase fromSynechocystissp. Strain PCC 6803

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