Phycocyanin

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Phycobilisome protein
Phycocyanin assembly.png
Allophycocyanin 12-mer PDB 1all
Identifiers
Symbol Phycobilisome
Pfam PF00502
InterPro IPR001659
SCOP2 1cpc / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary
Phycocyanobilin Phycocyanobilin2.svg
Phycocyanobilin

Phycocyanin is a pigment-protein complex from the light-harvesting phycobiliprotein family, along with allophycocyanin and phycoerythrin. [1] It is an accessory pigment to chlorophyll. All phycobiliproteins are water-soluble, so they cannot exist within the membrane like carotenoids can. Instead, phycobiliproteins aggregate to form clusters that adhere to the membrane called phycobilisomes. Phycocyanin is a characteristic light blue color, absorbing orange and red light, particularly near 620 nm (depending on which specific type it is), and emits fluorescence at about 650 nm (also depending on which type it is). Allophycocyanin absorbs and emits at longer wavelengths than phycocyanin C or phycocyanin R. Phycocyanins are found in cyanobacteria (also called blue-green algae). [2] Phycobiliproteins have fluorescent properties that are used in immunoassay kits. Phycocyanin is from the Greek phyco meaning “algae” and cyanin is from the English word “cyan", which conventionally means a shade of blue-green (close to "aqua") and is derived from the Greek “kyanos" which means a somewhat different color: "dark blue". The product phycocyanin, produced by Aphanizomenon flos-aquae and Spirulina, is for example used in the food and beverage industry as the natural coloring agent 'Lina Blue' or 'EXBERRY Shade Blue' and is found in sweets and ice cream. In addition, fluorescence detection of phycocyanin pigments in water samples is a useful method to monitor cyanobacteria biomass. [3]

Contents

The phycobiliproteins are made of two subunits (alpha and beta) having a protein backbone to which 1–2 linear tetrapyrrole chromophores are covalently bound.

C-phycocyanin is often found in cyanobacteria which thrive around hot springs, as it can be stable up to around 70 °C, with identical spectroscopic (light absorbing) behaviours at 20 and 70 °C. Thermophiles contain slightly different amino acid sequences making it stable under these higher conditions. Molecular weight is around 30,000 Da. Stability of this protein in vitro at these temperatures has been shown to be substantially lower. Photo-spectral analysis of the protein after 1 min exposure to 65 °C conditions in a purified state demonstrated a 50% loss of tertiary structure.

Phycocyanin pigment extracted from Microcystis aeruginosa cyanobacteria Extracted phycocyanin.jpg
Phycocyanin pigment extracted from Microcystis aeruginosa cyanobacteria

Structure

Phycocyanin (ab) monomer Phycocyanin monomer 5mjm.png
Phycocyanin (αβ) monomer
Phycocyanin (ab)6 hexamer Phycocyanin hexamer 5mjm.png
Phycocyanin (αβ)6 hexamer

Phycocyanin shares a common structural theme with all phycobiliproteins. [4] The structure begins with the assembly of phycobiliprotein monomers, which are heterodimers composed of α and β subunits, and their respective chromophores linked via thioether bond.

Each subunit is typically composed of eight α-helices. Monomers spontaneously aggregate to form ring-shaped trimers (αβ)3, which have rotational symmetry and a central channel. Trimers aggregate in pairs to form hexamers (αβ)6, sometimes assisted with additional linker proteins. Each phycobilisome rod generally has two or more phycocyanin hexamers. Despite the overall similarity in structure and assembly of phycobiliproteins, there is a large diversity in hexamer and rod conformations, even when only considering phycocyanins. On a larger scale phycocyanins also vary in crystal structure, although the biological relevance of this is debatable.

As an example, the structure of C-phycocyanin from Synechococcus vulcanus has been refined to 1.6 Angstrom resolution. [5] The (αβ) monomer consists of 332 amino acids and 3 thio-linked phycocyanobilin (PCB) cofactor molecules. Both the α- and β-subunits have a PCB at amino acid 84, but the β-subunit has an additional PCB at position 155 as well. This additional PCB faces the exterior of the trimeric ring and is therefore implicated in inter-rod energy transfer in the phycobilisome complex. In addition to cofactors, there are many predictable non-covalent interactions with the surrounding solvent (water) that are hypothesized to contribute to structural stability.

R-phycocyanin II (R-PC II) is found in some Synechococcus species. [6] R-PC II is said to be the first PEB containing phycocyanin that originates in cyanobacteria. [6] Its purified protein is composed of alpha and beta subunits in equal quantities. [6] R-PC II has PCB at beta-84 and the phycoerythrobillin (PEB) at alpha-84 and beta-155. [6]

As of March 21, 2023, there are 310 crystal structures of phycocyanin deposited in the Protein Data Bank. [7]

Spectral characteristics

C-phycocyanin has a single absorption peak at ~621 nm, [8] [9] varying slightly depending on the organism and conditions such as temperature, pH, and protein concentration in vitro. [10] [11] Its emission maximum is ~642 nm. [8] [9] This means that the pigment absorbs orange light, and emits reddish light. R-phycocyanin has an absorption maxima at 533 and 544 nm. [6] The fluorescence emission maximum of R-phycocyanin is 646 nm. [6]

PropertyC-PhycocyaninR-Phycocyanin
Absorption maximum (nm)621533, 544
Emission maximum (nm)642646
Extinction Coefficient (ε)1.54x106 M−1cm−1-
Quantum Yield0.81-

Ecological relevance

Phycocyanin is produced by many photoautotrophic cyanobacteria. [12] Even if cyanobacteria have large concentrations of phycocyanin, productivity in the ocean is still limited due to light conditions. [12]

Phycocyanin has ecological significance in indicating cyanobacteria bloom. Normally chlorophyll a is used to indicate cyanobacteria numbers, however since it is present in a large number of phytoplankton groups, it is not an ideal measure. [13] For instance a study in the Baltic Sea used phycocyanin as a marker for filamentous cyanobacteria during toxic summer blooms. [13] Some filamentous organisms in the Baltic Sea include Nodularia spumigena and Aphanizomenon flosaquae.

An important cyanobacteria named spirulina ( Arthrospira platensis ) is a micro algae that produces C-PC. [14]

There are many different methods of phycocyanin production including photoautotrophic, mixotrophic and heterotrophic and recombinant production. [15] Photoautotrophic production of phycocyanin is where cultures of cyanobacteria are grown in open ponds in either subtropical or tropical regions. [15] Mixotrophic production of algae is where the algae are grown on cultures that have an organic carbon source like glucose. [15] Using mixotrophic production produces higher growth rates and higher biomass compared to simply using a photoautotrophic culture. [15] In the mixotrophic culture, the sum of heterotrophic and autotrophic growth separately was equal to the mixotrophic growth. [16] Heterotrophic production of phycocyanin is not light limited, as per its definition. [15] Galdieria sulphuraria is a unicellular rhodophyte that contains a large amount of C-PC and a small amount of allophycocyanin. [15] G. sulphuraria is an example of the heterotrophic production of C-PC because its habitat is hot, acidic springs and uses a number of carbon sources for growth. [15] Recombinant production of C-PC is another heterotrophic method and involves gene engineering. [15]

Lichen-forming fungi and cyanobacteria often have a symbiotic relationship and thus phycocyanin markers can be used to show the ecological distribution of fungi-associated cyanobacteria. As shown in the highly specific association between Lichina species and Rivularia strains, phycocyanin has enough phylogenetic resolution to resolve the evolutionary history of the group across the northwestern Atlantic Ocean coastal margin. [17]

Biosynthesis

The two genes cpcA and cpcB, located in the cpc operon and translated from the same mRNA transcript, encode for the C-PC α- and β-chains respectively. [18] Additional elements such as linker proteins, and enzymes involved in phycobilin synthesis and the phycobiliproteins are often encoded by genes in adjacent gene clusters, and the cpc operon of Arthrospira platensis also encodes a linker protein assisting in the assembly of C-PC complexes. [19] In red algae, the phycobiliprotein and linker protein genes are located on the plastid genome. [20]

Phycocyanobilin is synthesized from heme and inserted into the C-PC apo-protein by three enzymatic steps. [21] Cyclic heme is oxidised to linear biliverdin IXα by heme oxygenase and further converted to 3Z-phycocyanobilin, the dominant phycocyanobilin isomer, by 3Z-phycocyanobilin:ferredoxin oxidoreductase. Insertion of 3Z-phycocyanobilin into the C-PC apo-protein via thioether bond formation is catalysed by phycocyanobilin lyase. [22]

The promoter for the cpc operon is located within the 427-bp upstream region of the cpcB gene. In A. platensis , six putative promoter sequences have been identified in the region, with four of them showing expression of green fluorescent protein when transformed into E. coli. [23] The presence of other positive elements such as light-response elements in the same region have also been demonstrated. [24]

The multiple promoter and response element sequences in the cpc operon enable cyanobacteria and red algae to adjust its expression in response to multiple environmental conditions. Expression of the cpcA and cpcB genes is regulated by light. Low light intensities stimulate synthesis of CPC and other pigments, while pigment synthesis is repressed at high light intensities. [25] Temperature has also been shown to affect synthesis, with specific pigment concentrations showing a clear maximum at 36 °C in Arthronema africanum, a cyanobacterium with particular high C-PC and APC contents. [26]

Nitrogen and also iron limitation induce phycobiliprotein degradation. Organic carbon sources stimulate C-PC synthesis in Anabaena spp., but seem to have almost no effector negative effect in A. platensis. [27] [28] In the rhodophytes Cyanidium caldarium and Galdieria sulphuraria, C-PC production is repressed by glucose but stimulated by heme. [29]

Biotechnology

Pure phycocyanin extractions can be isolated from algae. The basic segregation order is as follows. The rupturing of the cell wall, with mechanical forces (freeze thawing) or chemical agents (enzymes). Then, C-PC is isolated with centrifugation and purified with ammonium sulfate precipitation or chromatography -either ion or gel-filtration. After, the sample gets frozen and dried. [15]

Applications

Phycocyanin can be used in many practices, it is particularly used medicine and foods applications. It can also be used in genetics, where it acts a tracer due to its natural fluorescence. [30]

Medicine

Anti-oxidation and anti-inflammation

Phycocyanin has both anti-oxidant and anti-inflammation properties. [31] [32] [33] Peroxyl, hydroxyl, and alkoxyl radicals are all oxidants scavenged by C-PC. C-PC, however, has a greater effect on peroxyl radicals. C-PC is a metal binding antioxidant as it prevents lipid peroxidation from occurring. [34] The peroxyl radicals are stabilized by the chromophore (a subunit of C-PC). [35] For hydroxyl radicals to be scavenged, it must be done in low light and with high C-PC levels. [36] Hydroxyl radicals are found at inflamed parts of the body. [34] C-PC, being an anti-oxidant, scavenges these damage-inducing radicals, hence being an anti-inflammation agent.

Neuroprotection

Excess oxygen in the brain generates Reactive Oxygen Species (ROS). ROS cause damage to brain neurons, leading to decreased neurological function. C-phycocyanin scavenges hydrogen peroxide, a type of ROS species, from the inside of astrocyte, reducing oxidative stress. [37] Astrocytes also increase the production of growth factors like BDNF and NDF, therefore, enhance nerve regeneration. C-PC also prevents astrogliosis and glial inflammation. [37] [38]

Hepatoprotection

C-phycocyanin is found to have hepatotoxicity protection. [31] [39] Vadiraja et al. (1998) found an increase in the serum glutamic pyruvic transaminase (SGPT) when C-PC is treated against heptatoxins such as Carbon tetrachloride (CCl4) or R-(+)-pulegone. C-PC protects the liver by the means of the Cytochrome-P450 system. [39] It can either disturb the production of menthofuran or disturb formation of α, β-unsaturated- γ-ketoaldehyde. Both of which are key components of the cytochrome P-450 system that produced a reactive metabolite that produce toxins when it binds to liver tissues. Another possible protection mechanism by C-PC can be the scavenging of reactive metabolites (or free radicals if the cause is CCl4).

Anti-cancer

C-phycocyanin (C-PC) has anti-cancer effects. Cancer happens when cells continue to grow uncontrollably. C-PC has been found to prevent cell growth. [40] C-PC stops the formation of tumour before the S phase. DNA synthesis is not performed due to the tumour cell entering G0, resulting in no tumour proliferation. [41] Furthermore, C-PC induces apoptosis. When cells are treated with C-PC, ROS (Radical Oxygen Species) are made. These molecules decrease BCl-2 (regulator of apoptosis) production. Here, BCl-2 inhibits proteins called caspases. Caspases are part of the apoptosis pathway. When BCl-2 decreases, the expression of caspases increases. As a result, apoptosis occurs. [42] [41] C-PC alone is not enough to treat cancer, it needs to work other drugs to overcome the persistence nature of tumour cells.

Food

C-phycocyanin (C-PC) can be used as a natural blue food colouring. [43] This food colourant can only be used for low temperature prepared goods because of its inability to maintaining its blue colouring in high heats unless there is an addition of preservatives or sugars. [43] [44] The type of sugar is irrelevant, C-PC is stable when there is high sugar content. Knowing so, C-PC can be used for numerous types of foods, one of which being syrups. C-PC can be used for syrups ranging from green to blue colours. It can have different green tints by adding yellow food colourings.

Related Research Articles

<span class="mw-page-title-main">Spirulina (dietary supplement)</span> Blue-green algal genus (cyanobacteria) used in food

Spirulina is a biomass of cyanobacteria that can be consumed by humans and animals. The three species are Arthrospira platensis, A. fusiformis, and A. maxima.

Phycobilins are light-capturing bilins found in cyanobacteria and in the chloroplasts of red algae, glaucophytes and some cryptomonads. Most of their molecules consist of a chromophore which makes them coloured. They are unique among the photosynthetic pigments in that they are bonded to certain water-soluble proteins, known as phycobiliproteins. Phycobiliproteins then pass the light energy to chlorophylls for photosynthesis.

Phycoerythrin (PE) is a red protein-pigment complex from the light-harvesting phycobiliprotein family, present in cyanobacteria, red algae and cryptophytes, accessory to the main chlorophyll pigments responsible for photosynthesis.The red pigment is due to the prosthetic group, phycoerythrobilin, which gives phycoerythrin its red color.

Accessory pigments are light-absorbing compounds, found in photosynthetic organisms, that work in conjunction with chlorophyll a. They include other forms of this pigment, such as chlorophyll b in green algal and vascular ("higher") plant antennae, while other algae may contain chlorophyll c or d. In addition, there are many non-chlorophyll accessory pigments, such as carotenoids or phycobiliproteins, which also absorb light and transfer that light energy to photosystem chlorophyll. Some of these accessory pigments, in particular the carotenoids, also serve to absorb and dissipate excess light energy, or work as antioxidants. The large, physically associated group of chlorophylls and other accessory pigments is sometimes referred to as a pigment bed.

<span class="mw-page-title-main">Phycobilisome</span> Light-energy harvesting structure in cyanobacteria and red algae

Phycobilisomes are light-harvesting antennae that transmit the energy of harvested photons to photosystem II and photosystem I in cyanobacteria and in the chloroplasts of red algae and glaucophytes. They were lost during the evolution of the chloroplasts of green algae and plants.

<span class="mw-page-title-main">Allophycocyanin</span>

Allophycocyanin is a protein from the light-harvesting phycobiliprotein family, along with phycocyanin, phycoerythrin and phycoerythrocyanin. It is an accessory pigment to chlorophyll. All phycobiliproteins are water-soluble and therefore cannot exist within the membrane like carotenoids, but aggregate, forming clusters that adhere to the membrane called phycobilisomes. Allophycocyanin absorbs and emits red light, and is readily found in Cyanobacteria, and red algae. Phycobilin pigments have fluorescent properties that are used in immunoassay kits. In flow cytometry, it is often abbreviated APC. To be effectively used in applications such as FACS, High-Throughput Screening (HTS) and microscopy, APC needs to be chemically cross-linked.

<span class="mw-page-title-main">Phycobiliprotein</span>

Phycobiliproteins are water-soluble proteins present in cyanobacteria and certain algae. They capture light energy, which is then passed on to chlorophylls during photosynthesis. Phycobiliproteins are formed of a complex between proteins and covalently bound phycobilins that act as chromophores. They are most important constituents of the phycobilisomes.

<span class="mw-page-title-main">Biological pigment</span> Substances produced by living organisms

Biological pigments, also known simply as pigments or biochromes, are substances produced by living organisms that have a color resulting from selective color absorption. Biological pigments include plant pigments and flower pigments. Many biological structures, such as skin, eyes, feathers, fur and hair contain pigments such as melanin in specialized cells called chromatophores. In some species, pigments accrue over very long periods during an individual's lifespan.

<span class="mw-page-title-main">Bilin (biochemistry)</span> Class of chemical compound

Bilins, bilanes or bile pigments are biological pigments formed in many organisms as a metabolic product of certain porphyrins. Bilin was named as a bile pigment of mammals, but can also be found in lower vertebrates, invertebrates, as well as red algae, green plants and cyanobacteria. Bilins can range in color from red, orange, yellow or brown to blue or green.

Phycoerythrocyanin is a kind of phycobiliprotein, magenta chromoprotein involved in photosynthesis of some Cyanobacteria. This chromoprotein consists of alpha- and beta-subunits, generally aggregated as hexamer. Alpha-phycoerythrocyanin contains a phycoviolobilin, a violet bilin, that covalently attached at Cys-84, and beta-phycoerythrocyanin contains two phycocyanobilins, a blue bilin, that covalently attached at Cys-84 and -155, respectively. Phycoerythrocyanin is similar to phycocyanin, an important component of the light-harvesting complex (phycobilisome) of cyanobacteria and red algae.

<span class="mw-page-title-main">Phycocyanobilin</span> Chemical compound

Phycocyanobilin is a blue phycobilin, i.e., a tetrapyrrole chromophore found in cyanobacteria and in the chloroplasts of red algae, glaucophytes, and some cryptomonads. Phycocyanobilin is present only in the phycobiliproteins allophycocyanin and phycocyanin, of which it is the terminal acceptor of energy. It is covalently linked to these phycobiliproteins by a thioether bond.

<span class="mw-page-title-main">Photosynthetic reaction centre protein family</span>

Photosynthetic reaction centre proteins are main protein components of photosynthetic reaction centres (RCs) of bacteria and plants. They are transmembrane proteins embedded in the chloroplast thylakoid or bacterial cell membrane.

<i>Arthrospira</i> Genus of Cyanobacteria

Arthrospira is a genus of free-floating filamentous cyanobacteria characterized by cylindrical, multicellular trichomes in an open left-hand helix. A dietary supplement is made from A. platensis and A. maxima, known as spirulina. The A. maxima and A. platensis species were once classified in the genus Spirulina. Although the introduction of the two separate genera Arthrospira and Spirulina is now generally accepted, there has been much dispute in the past and the resulting taxonomical confusion is tremendous.

<span class="mw-page-title-main">Culture of microalgae in hatcheries</span>

Microalgae or microscopic algae grow in either marine or freshwater systems. They are primary producers in the oceans that convert water and carbon dioxide to biomass and oxygen in the presence of sunlight.

<span class="mw-page-title-main">Picozoa</span> Phylum of marine unicellular heterotrophic eukaryotes

Picozoa, Picobiliphyta, Picobiliphytes, or Biliphytes are protists of a phylum of marine unicellular heterotrophic eukaryotes with a size of less than about 3 micrometers. They were formerly treated as eukaryotic algae and the smallest member of photosynthetic picoplankton before it was discovered they do not perform photosynthesis. The first species identified therein is Picomonas judraskeda. They probably belong in the Archaeplastida as sister of the Rhodophyta.

<i>Arthrospira platensis</i> Species of bacterium

Arthrospira platensis is a filamentous, gram-negative cyanobacterium. This bacterium is non-nitrogen-fixing photoautotroph. It has been isolated in Chenghai Lake, China, soda lakes of East Africa, and subtropical, alkaline lakes.

<span class="mw-page-title-main">Avigad Vonshak</span>

Avigad Vonshak is a Professor Emeritus at the French Associates Institute for Agriculture and Biotechnology of Drylands at the Jacob Blaustein Institutes for Desert Research at Ben-Gurion University of the Negev, Israel.

Sammy Boussiba is a professor emeritus at the French Associates Institute for Agriculture and Biotechnology of Drylands at the Jacob Blaustein Institutes for Desert Research at Ben-Gurion University of the Negev, Israel.

<span class="mw-page-title-main">Biliprotein</span> Class of pigment proteins in photosynthesising organisms

Biliproteins are pigment protein compounds that are located in photosynthesising organisms such as algae, and sometimes also in certain insects. They refer to any protein that contains a bilin chromophore. In plants and algae, the main function of biliproteins is to make the process of light accumulation required for photosynthesis more efficient; while in insects they play a role in growth and development. Some of their properties: including light-receptivity, light-harvesting and fluorescence have made them suitable for applications in bioimaging and as indicators; while other properties such as anti-oxidation, anti-aging and anti-inflammation in phycobiliproteins have given them potential for use in medicine, cosmetics and food technology. While research on biliproteins dates back as far as 1950, it was hindered due to issues regarding biliprotein structure, lack of methods available for isolating individual biliprotein components, as well as limited information on lyase reactions . Research on biliproteins has also been primarily focused on phycobiliproteins; but advances in technology and methodology, along with the discovery of different types of lyases, has renewed interest in biliprotein research, allowing new opportunities for investigating biliprotein processes such as assembly/disassembly and protein folding.

Alexander Glazer was a professor of the Graduate School in the Department of Molecular and Cell Biology at the University of California, Berkeley. He had a passion for protein chemistry and structure function relationships. He also had a longstanding interest in light-harvesting complexes in cyanobacteria and red algae called phycobilisomes. He had also spent more than 10 years working on the human genome project where he has investigated methods for DNA detection and sequencing which most notably includes the development of fluorescent reagents involved in cell labeling. Most recently, he had focused his studies on issues in environmental sciences. He died on July 18, 2021, in Orinda, California

References

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