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THE CHLOROPHYLL-CAROTENOID PROTEINS OF OXYGENIC ..

Basically this is the Chlorophyll containing plant or algae "moving" to respond to a positive light source to begin the process of photosynthesis (initial growth of plants, zooxanthellae, etc.).*Photosynthetic response; During this time, the molecules needed for photosynthesis gradually reach operating levels which begins when energy from light is absorbed by proteins called photosynthetic reaction centers that contain chlorophylls.

The chlorophyll-carotenoid proteins of oxygenic photosynthesis

N2 - In the light-harvesting chlorophyll pigment-proteins of photosynthesis, a carotenoid is typically positioned within a distance of ∼4 Å of individual chlorophylls or antenna arrays, allowing rapid triplet energy transfer from chlorophyll to the carotenoid. This triplet energy transfer prevents the formation of toxic singlet oxygen. In the cytochrome b6f complex of oxygenic photosynthesis that contains a single chlorophyll a molecule, this chlorophyll is distant (14 Å) from the single β-carotene, as defined by x-ray structures from both a cyanobacterium and a green alga. Despite this separation, rapid (

THE CHLOROPHYLL-CAROTENOID PROTEINS OF OXYGENIC PHOTOSYNTHESIS

Bode S, Quentmeier CC, Liao P‐N et al. (2009) On the regulation of photosynthesis by excitonic interactions between carotenoids and chlorophylls. Proceedings of the National Academy of Sciences of the USA 106: 12311–12316.

AB - In the light-harvesting chlorophyll pigment-proteins of photosynthesis, a carotenoid is typically positioned within a distance of ∼4 Å of individual chlorophylls or antenna arrays, allowing rapid triplet energy transfer from chlorophyll to the carotenoid. This triplet energy transfer prevents the formation of toxic singlet oxygen. In the cytochrome b6f complex of oxygenic photosynthesis that contains a single chlorophyll a molecule, this chlorophyll is distant (14 Å) from the single β-carotene, as defined by x-ray structures from both a cyanobacterium and a green alga. Despite this separation, rapid (

proteins of oxygenic photosynthesis.

In the light-harvesting chlorophyll pigment-proteins of photosynthesis, a carotenoid is typically positioned within a distance of ∼4 Å of individual chlorophylls or antenna arrays, allowing rapid triplet energy transfer from chlorophyll to the carotenoid. This triplet energy transfer prevents the formation of toxic singlet oxygen. In the cytochrome b6f complex of oxygenic photosynthesis that contains a single chlorophyll a molecule, this chlorophyll is distant (14 Å) from the single β-carotene, as defined by x-ray structures from both a cyanobacterium and a green alga. Despite this separation, rapid (6f complex.

Chlorophylls and bacteriochlorophylls serve – noncovalently bound to specific proteins – as principal energy‐transforming cofactors in photosynthesis.

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proteins of photosynthesis, a carotenoid is ..

Photosynthetic pigments absorb in the visible range of the electromagnetic spectrum. (a) Spectra of chlorophylls and (in acetone), 1 (in diethyl ether), and (in acetone). (b) Spectra of phycobiliproteins B‐PE (phycoerythrin), PC (phycocyanin) and APC (allophycocyanin) (in 0.1 mol L–1 phosphate buffer). These water‐soluble pigments are present in many rhodophytes and cyanobacteria. Lutein (in acetone) is a common carotenoid in green plants.

6 x The chlorophyll-carotenoid proteins of oxygenic photosynthesis

Molecular structures of chlorophylls and photosynthetically important carotenoids. Portions highlighted in red indicate the specific side‐chains of the individual chlorophylls, and the differences between lutein, peridinin and fucoxanthin.

The chlorophyll-carotenoid proteins of oxygenic ..

We measure PAR via µMolm which is a unit of measure (more about measurement later).
PAR is the abbreviation for Photosynthetically Active Radiation which is the spectral range of solar light from 400 to 700 nanometers that is generally accepted as needed by plants & symbiotic zooanthellic algae for photosynthesis (Zooxanthellae are single-celled algae that live in the tissues of animals such as corals, clams, & anemones).
It is also noteworthy that while outside of the accepted PAR, a study using infrared (IR) LEDs of 880 nm & 935 nm on etiolated oat seedlings showed leaf emergence, so these parameters may someday need better defining (See at the end of article).UVA to 550 nm contains the absorption bandwidth of chlorophylls a, c², and peridinin (the light-harvesting carotenoid, a pigment related to chlorophyll).

Abstract The chlorophyll-carotenoid binding proteins ..

A variety of chlorophyll/carotenoid‐binding LHCs and phycobilisomes are associated with reaction centres of photosystem I (RC1) and II (RC2): in cyanophytes (e.g. ) phycobilisomes transfer energy initially to RC2, and LHCs are lacking; rhodophytes (e.g. ) have Chl /car LHCs associated only with RC1, and phycobilisomes only with RC2. In chlorophytes (e.g. ) distinct Chl //car LHCs are associated with each RC. In chromophytes (e.g. ) distinct Chl /‐car LHCs occur with RC1 and RC2. In cryptophytes (e.g. ) phycobiliproteins in the lumen transfer energy to Chl , but not to Chl . Both Chl types are associated with RC1 and RC2. Dinophytes (e.g. ) have a luminal peridinin–Chl complex and an integral Chl / complex in thylakoids.

05/11/2010 · Acta Scientiarum

In the present study the rate of triplet transfer from chlorophyll to carotenoids in solubilized LHCII was investigated by flash spectroscopy using laser pulses of approximately 2 ns for both pump and probe. Special attention has been paid to calibration of the experimental setup and to avoid saturation effects. Carotenoid triplets were identified by the pronounced positive peak at approximately 507 nm in the triplet-singlet difference spectra. DeltaOD (507 nm) exhibits a monoexponential relaxation kinetics with characteristic lifetimes of 2-9 micros (depending on the oxygen content) that was found to be independent of the pump pulse intensity. The rise of DeltaOD (507 nm) was resolved via a pump probe technique where an optical delay of up to 20 ns was used. A thorough analysis of these experimental data leads to the conclusion that the kinetics of carotenoid triplet formation in solubilized LHCII is almost entirely limited by the lifetime of the excited singlet state of chlorophyll but neither by the pulse width nor by the rate constant of triplet-triplet transfer. Within the experimental error the rate constant of triplet-triplet transfer from chlorophyll to carotenoids was estimated to be kTT > (0.5 ns)-1. This value exceeds all data reported so far by at least one order of magnitude. The implications of this finding are briefly discussed.

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