Cyanobacterial light harvesting antenna and pigment organisation. (a) Cyanobacterial photosynthetic electron transport chain including the dynamic extrinsic antenna system consisting of phycoerythrin (PE), phycocyanin (PC), allophycocyanin (APC) is connected to the stromal surface of the PSI and PSII core complexes via the Core-Membrane Linker (L CM ). (b) Example of pigment coordination within the PSII monomer. (c) Four major chromophores in cyanobacteria. The chromophores Phycocyanobilin (PCB; C 33 H 40 N 4 O 6 ), Phycoerythrobilin (PEB; C 33 H 38 N 4 O 6 ), Phycourobilin (PUB; C 33 H 42 N 4 O 6 ) and Phycoviolobilin (PVB; C 33 H 34 N 4 O 6 ). (d) Typical phycobilisome (PBS) organisation: rod-shaped, bundle-shaped, hemi-discoidal and hemiellipsoidal. In most cyanobacteria the hemi-discoidal organisation occurs but the pigment composition within these rods is species-specific

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... health and environmental awareness has led to marketdriven expansion of the naturally derived pigment sector as part of an expanding circular bioeconomy [23,24]. In terms of industrial-scale pigment production it is important to note that pigments can be produced as isolated coloured chromophores such as chlorophylls, carotenoids and pheophytin (Fig. 1b), phycoerythrobilin (PEB) and phycocyanobilin (PCB; Fig. 1c), or as the coloured proteins that coordinate them (e.g. phycoerythrin, phycocyanin and allophycocyanin). To avoid confusion, isolated chromophores are here referred to as chromophores and chromophore binding proteins as coloured proteins. Collectively, along with other ...

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... expansion of the naturally derived pigment sector as part of an expanding circular bioeconomy [23,24]. In terms of industrial-scale pigment production it is important to note that pigments can be produced as isolated coloured chromophores such as chlorophylls, carotenoids and pheophytin (Fig. 1b), phycoerythrobilin (PEB) and phycocyanobilin (PCB; Fig. 1c), or as the coloured proteins that coordinate them (e.g. phycoerythrin, phycocyanin and allophycocyanin). To avoid confusion, isolated chromophores are here referred to as chromophores and chromophore binding proteins as coloured proteins. Collectively, along with other coloured molecules, they are referred to as ...

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... pigment-protein complexes located on and in the thylakoid 6 ). (d) Typical phycobilisome (PBS) organisation: rod-shaped, bundle-shaped, hemi-discoidal and hemiellipsoidal. In most cyanobacteria the hemi-discoidal organisation occurs but the pigment composition within these rods is species-specific membranes, which lie under the cell membrane (see Fig. 1), typically in a dense multilayered wrapping (Fig. 6, Sect. 5.2). The extrinsic and intrinsic antenna proteins have evolved to provide a dynamic scaffold that coordinates an intricate and excitonically coupled network of chromophores including phycoerythrobilin (PEB; Fig. 1c), phycocyanobilin (PCB; Fig. 1c), phycourobilin (PUB; Fig. ...

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... is species-specific membranes, which lie under the cell membrane (see Fig. 1), typically in a dense multilayered wrapping (Fig. 6, Sect. 5.2). The extrinsic and intrinsic antenna proteins have evolved to provide a dynamic scaffold that coordinates an intricate and excitonically coupled network of chromophores including phycoerythrobilin (PEB; Fig. 1c), phycocyanobilin (PCB; Fig. 1c), phycourobilin (PUB; Fig. 1c), phycoviolobilin (PVB; Fig. 1c), chlorophylls, pheophytins and carotenoids that collectively support the dual function of PSI and PSII light-driven charge separation and photoprotection. The extrinsic antenna systems include the light harvesting protein complexes ...

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... which lie under the cell membrane (see Fig. 1), typically in a dense multilayered wrapping (Fig. 6, Sect. 5.2). The extrinsic and intrinsic antenna proteins have evolved to provide a dynamic scaffold that coordinates an intricate and excitonically coupled network of chromophores including phycoerythrobilin (PEB; Fig. 1c), phycocyanobilin (PCB; Fig. 1c), phycourobilin (PUB; Fig. 1c), phycoviolobilin (PVB; Fig. 1c), chlorophylls, pheophytins and carotenoids that collectively support the dual function of PSI and PSII light-driven charge separation and photoprotection. The extrinsic antenna systems include the light harvesting protein complexes (phycoerythrin, phycocyanin and ...

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... (see Fig. 1), typically in a dense multilayered wrapping (Fig. 6, Sect. 5.2). The extrinsic and intrinsic antenna proteins have evolved to provide a dynamic scaffold that coordinates an intricate and excitonically coupled network of chromophores including phycoerythrobilin (PEB; Fig. 1c), phycocyanobilin (PCB; Fig. 1c), phycourobilin (PUB; Fig. 1c), phycoviolobilin (PVB; Fig. 1c), chlorophylls, pheophytins and carotenoids that collectively support the dual function of PSI and PSII light-driven charge separation and photoprotection. The extrinsic antenna systems include the light harvesting protein complexes (phycoerythrin, phycocyanin and allophycocyanin) which usually ...

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... a dense multilayered wrapping (Fig. 6, Sect. 5.2). The extrinsic and intrinsic antenna proteins have evolved to provide a dynamic scaffold that coordinates an intricate and excitonically coupled network of chromophores including phycoerythrobilin (PEB; Fig. 1c), phycocyanobilin (PCB; Fig. 1c), phycourobilin (PUB; Fig. 1c), phycoviolobilin (PVB; Fig. 1c), chlorophylls, pheophytins and carotenoids that collectively support the dual function of PSI and PSII light-driven charge separation and photoprotection. The extrinsic antenna systems include the light harvesting protein complexes (phycoerythrin, phycocyanin and allophycocyanin) which usually coordinate the chromophores ...

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... cyanobacterial PSII core complex is composed of around 20 subunits (Fig. 1a). In 2001 a 3.8 Å resolution PSII core complex structure from Synechococcus elongatus was described [32]. Each 350 kDa PSII monomer (Fig. 1b) is reported to contain 17 membrane spanning protein subunits as well, three extrinsic proteins, 99 cofactors, 35 chlorophyll a, 12 β-carotene, 2 pheophytin, 2 plastoquinone and 2 heme molecules, ...

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... cyanobacterial PSII core complex is composed of around 20 subunits (Fig. 1a). In 2001 a 3.8 Å resolution PSII core complex structure from Synechococcus elongatus was described [32]. Each 350 kDa PSII monomer (Fig. 1b) is reported to contain 17 membrane spanning protein subunits as well, three extrinsic proteins, 99 cofactors, 35 chlorophyll a, 12 β-carotene, 2 pheophytin, 2 plastoquinone and 2 heme molecules, the water splitting Mn 4 CaO 5 cluster and one non-heme Fe 2+ [33]. The electrons extracted from water by PSII are passed, via the cytochrome ...

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... Cyanobacterial phycobilisomes (PBS) (Fig. 1a) are large organised complexes of water-soluble phycobiliproteins (PBPs), phycoerythrin (PE), phycocyanin (PC), allophycocyanin (APC) and their chromophores [42,43]. Their chromophores (phycocyanobilin and phycoerythrobilin) are synthesised from glutamic acid, which is converted to aminolevulinic acid (ALA), two molecules of which form ...

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... & Properties: The PBS consist of water-soluble phycobiliproteins (PBPs) and hydrophobic linker peptides and are classified into 4 structural types which are both species and light-dependent: rod-shaped, hemi-ellipsoidal, hemidiscoidal and bundle-shaped (Fig. 1b). The most common and stable type of PBS organisation is reported to be the hemi-discoidal form (4.5-15 MDa) [48]. It is thought to accommodate a maximum of 800 chromophores per PSII dimer [49]. The bundle-shaped PBS was found in Gloeobacter violaceus and reported to support among the fastest energy transfer rates [49]. The rod-shaped ...

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... (17 kDa). They coordinate 2 PCB per αβ-APC monomer via thioether bonds [42,53]. These αβ PC monomers usually form trimeric APC ((αβ) 3 ). As for PC, the fluorescence of APC has been attributed to the covalent linkage of phycocyanobilin to cysteine-84 of the α-subunit as well as to cysteine-84 and cysteine-155 residues of β-subunit. The APC core (Fig. 1a) is formed by four APC trimers in Synechocystis sp. PCC6803 [54] and has a maximum fluorescence emission at ~660 nm, and the molar extinction coefficient at ε 650 is 0.7 × 10 6 M -1 cm -1 for the 104 kDa APC trimer ...

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... two subunits of PE named α-PE (20 kDa) and β-PE (22 kDa) are reported to coordinate from 2-6 chromophores via thioether bonds (i.e. 2-6. PEB, PUB or PVB or a combination thereof; Fig. 1) per αβ monomer (αβ) 1 [56]. These αβ-PE monomers are generally organised into disc-shaped trimers (αβ) 3 or hexamers (αβ) 6 . As an example, PE in Gloeobacter violaceus (PDB: 2VJH) is reported to form hexamers coordinating 4 PEB and 1 PUB per αβ monomer. The maximum fluorescence emission occurs at ~578 nm and the molar extinction ...

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... functions: Collectively chlorophylls have four major biological functions including light capture, excitation energy transfer, acting as electron donors, and energy dissipation (Fig. ...

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... document recent technical developments that have commercial potential [381]. A patent search on Patent Lens (Lens.org), a patent database with an integrated framework that serves nearly all the patent documents in the world, for the pigment 'Phycocyanin' showcases an example for current cyanobacterial pigments in the market and is represented in Fig. ...