phycocyanin

Phycocyanin adalah kompleks pigmen -protein dari keluarga phycobiliprotein pemanen cahaya , bersama dengan
allophycocyanin dan phycoerythrin . [1] Ini adalah pigmen aksesori untuk klorofil . Semua fikobiliprotein larut dalam
air, sehingga mereka tidak dapat berada di dalam membran seperti halnya karotenoid . Sebaliknya, fikobiliprotein
berkumpul untuk membentuk kelompok yang melekat pada membran yang disebut fikobilisom. Phycocyanin adalah
warna biru muda yang khas, menyerap cahaya oranye dan merah, terutama di dekat 620 nm (tergantung pada
jenis spesifiknya), dan memancarkan fluoresensi sekitar 650 nm (juga tergantung pada jenisnya). Allophycocyanin
menyerap dan memancarkan pada panjang gelombang yang lebih panjang daripada phycocyanin C atau
phycocyanin R. Phycocyanin ditemukan di cyanobacteria (juga disebut ganggang biru-hijau ). [2 ] Phycobiliproteins
memiliki sifat fluoresen yang digunakan dalam kit immunoassay . Phycocyanin berasal dari bahasa Yunani phyco
yang berarti " alga " dan cyanin dari kata bahasa Inggris " cyan ".", yang secara konvensional berarti warna biru-
hijau (dekat dengan "aqua") dan berasal dari bahasa Yunani " kyanos " yang berarti warna yang agak berbeda:
"biru tua". Produk phycocyanin, yang diproduksi oleh Aphanizomenon flos-aquae dan Spirulina , misalnya
digunakan dalam industri makanan dan minuman sebagai pewarna alami 'Lina Blue' atau 'EXBERRY Shade Blue' dan
ditemukan dalam permen dan es krim. Selain itu, deteksi fluoresensi pigmen phycocyanin dalam sampel air adalah
metode yang berguna untuk memantau biomassa cyanobacteria. [3]
 Protein fiko biliso m

Allo phyco cyanin 12-mer PDB 1all

pengenal

Simbo l fiko biliso m

Pfam PF00502 (http://pfam.xfam.o rg/family?acc=PF00502)

InterPro IPR001659 (https://www.ebi.ac.uk/interpro/entry/IPR0016

59)

SCOP2 1cpc (http://sco p2.mrc-lmb.cam.ac.uk/search?t=txt;q=1cp

c) / CAKUPAN (https://sco p.berkeley.edu/pdb/co de=1
cpc) / SUPFAM (http://supfam.o rg/SUPERFAMILY/cgi-bi
n/search.cgi?search_field=1cpc)

Struktur protein yang tersedia:

Pfam
  struktur (http://pfam.xfam.org/family/PF00502?tab=pdbBl
ock) / ECOD (http://prodata.swmed.edu/ecod/complete/s
earch?kw=PF00502)
 

PDB RCSB PDB (https://www.rcsb.org/search?q=rcsb_polymer_e

ntity_annotation.annotation_id:PF00502%20AND%20rcsb_
polymer_entity_annotation.type:Pfam) ; PDBe (https://ww
w.ebi.ac.uk/pdbe/entry/search/index?pfam_accession:PF
00502) ; PDBj (https://pdbj.org/searchFor?query=PF0050
2)

PDBsum ringkasan struktur (https://www.ebi.ac.uk/thornton-srv/data

bases/cgi-bin/pdbsum/GetPfamStr.pl?pfam_id=PF00502)
Phycocyanobilin

Fikobiliprotein terbuat dari dua subunit (alfa dan beta) yang memiliki tulang punggung protein yang terikat secara
kovalen dengan 1-2 kromofor tetrapirol linier.

C-phycocyanin sering ditemukan pada cyanobacteria yang tumbuh subur di sekitar sumber air panas, karena
dapat stabil hingga sekitar 70 °C, dengan perilaku spektroskopi (penyerapan cahaya) yang identik pada 20 dan
70 °C. Termofil mengandung urutan asam amino yang sedikit berbeda sehingga stabil di bawah kondisi yang lebih
tinggi ini. Berat molekul sekitar 30.000 Da. Stabilitas protein invitro ini pada suhu ini telah terbukti jauh lebih
rendah. Analisis foto-spektral protein setelah 1 menit terpapar pada kondisi 65 °C dalam keadaan murni
menunjukkan hilangnya 50% struktur tersier.

Pigmen phycocyanin diekstrak dari Microcystis aeruginosa cyanobacteria.

Struktur
Phycocyanin (αβ) monomer

Phycocyanin (αβ) heksamer

6

[4]
Phycocyanin berbagi tema struktural umum dengan semua phycobiliproteins . Strukturnya dimulai dengan
perakitan monomer fikobiliprotein, yang merupakan heterodimer yang terdiri dari subunit dan , dan masing-masing
kromofor dihubungkan melalui ikatan
tioeter .

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 7, 2018, there are 44 crystal structures of phycocyanin deposited in the Protein Data Bank. [7]

Karakteristik spektral

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]

Property C-Phycocyanin R-Phycocyanin

Absorption maximum (nm) 621 533, 544

Emission maximum (nm) 642 646

Extinction Coefficient (ε) 1.54x10 6 M−1cm−1 -

Quantum Yield 0.81 -

Relevansi ekologis

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 plantensis) 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]

Biosintesis

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 synthesised from heme and inserted into the C-PC apo-protein by three enzymatic steps. [2 1]
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. [2 2 ]

The promoter for the cpc operon is located within the 427-bp upstream region of the cpcB gene. In A. platensis, 6
putative promoter sequences have been identified in the region, with four of them showing expression of green
fluorescent protein when transformed into E. coli. [2 3] 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. [2 9]

Bioteknologi

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 causes damages to brain neurons,
leading to strokes. 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) (https://www.medicinenet.com/script/main/art.asp?articlekey=631
6) 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.

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Bacaan lebih lanjut

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