Topic:

Functions of Carotenoids in Light Harvesting

Complexes

Submitted to: Dr. Barizah

Submitted by:

Juraira Zafar (BS-BC19-F23)

Umer Farooq (BS-BC10-F23)

Azka Fatima (BS-BC08-F23)

Semester: V

Subject: Bioenergetics

Program: BS Biochemistry

School of Biochemistry and Biotechnology

University of the Punjab, Lahore

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 Contents
1 Abstract
2 Introduction
3 Structure of LHCs
4 Chemical composition of carotenoids
5 Binding sites of carotenoids in LHCs
6 Functional role of carotenoids in Plants
7 Functional role of carotenoids in Cyanobacteria
8 Conclusion

FUNCTIONS OF CAROTINOIDS IN LIGHT HARVESTING COMPLEXES

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 Abstract

Carotenoids are commonly generated in photosynthetic organisms, including

plants, fungi, algae, and bacteria. They are thought to be the most abundant lipid-
soluble pigments. All photosynthetic organisms contain carotenoids, which are
tetraterpenoids molecules that improve photosynthesis's capacity to absorb light
and dissipate energy. The primary photosynthetic pigments that enable effective
light absorption in plants, algae, and cyanobacteria are chlorophyll, carotenoids,
and phycobilins. Carotenoids are essential antioxidants that lower photodamage
and photoinhibition, among their many other functions in photosynthesis. Due to
phycobilins' ability to absorb a broad range of light in the marine environment,
cyanobacteria and red algae have been able to settle in deep waters where other
light frequencies are suppressed by the water column.

INTRODUCTION
The most abundant lipid-soluble pigments in nature are called carotenoids. They are widely
distributed and mostly biosynthesized in a variety of photosynthetic species, including higher
plants, fungi, algae, and bacteria. This is how they give these creatures their distinct colors,
tones, and tints [1].. A sequence of physical and chemical reactions known as photosynthesis
transform solar energy into chemical energy, which is then stored in organic materials. The
process of oxygen-forming photosynthesis allows water molecules to split, producing oxygen,
which is indispensable for maintaining aerobic life on earth [2]. The two types of photosystems
found in oxygen-dependent photosynthetic organisms, cyanobacteria, eukaryotic algae, and
plants, are called photosystem II (PSII) and photosystem I (PSI), and they are in charge of the
light-driven electron transport. While PSI is found in the lamella of stroma of the thylakoid and
aids in NADP+ to NADPH reduction, PSII is found in the stacked membranes grana in plants
and is responsible for catalyzing a reaction of water-splitting and oxygen-evolving [3]. Protein
complexes of multisubunit proteins that bind a variety of carotenoids (Cars), chlorophylls (Chls),
and other cofactors make up both photosystems. Because of their involvement in light
harvesting, stability of protein, light and photoprotection in plants, carotenoids are considered to
be the crucial components of light-harvesting complexes (LHCs) in plants. A core complex and
a peripheral antenna system, which gathers light energy and sends it to the reaction center, make
up each photosystem. Although the antenna systems of PSI and PSII vary greatly between
species, their basic complexes are mostly maintained from cyanobacteria to higher plants [4].
Typically, photosystem II from various species forms a homodimer inside the membranes of
thylakoids. While plants and green algae contain a variety of transmembrane Chl- and Car-
binding proteins that are members of the light-harvesting complex (LHC) superfamily and form
the PSII-LHCII supercomplex with the PSII core, cyanobacteria and red algae use soluble

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phycobiliproteins as their antennae. The PSI of cyanobacterial core primarily resides as a trimer,
sometimes using phyco biliproteins for light harvesting or existing without directly connected
antennae [5]. The membrane-intrinsic LHCs, or LHCIs, encircle the monomeric PSI core of
eukaryotic algae and plants to create the PSI-LHCI supercomplex [6]. Various creatures have
different antenna sizes and compositions in their photosystems. LHCs perform energy capture
and transfer tasks in addition to non-photochemical quenching, which is the process of releasing
excess excitation energy as heat in order to prevent or lessen photooxidative damage caused by
intense light or other stressful situations [7].

STRUCTURE OF LHCs
Chl a, Chl b, and carotenoids are bound by the light-harvesting complexes (LHCs), a superfamily
of nuclear-encoded 21–29 kDa membrane apoproteins found in plants and green algae [8]. LHCs
effectively act as antennae to power photochemistry by capturing light energy in the form of
pigment excitation and sending it to the photosynthetic reaction centers. The extremely
conserved structure of LHCs consists of two short amphipathic helices (D and E) and three
transmembrane alpha-helices (A–C) that are exposed to the thylakoid lumen. (Fig .1) [9]. The
stroma and lumen, respectively, are exposed to the N-terminal and C-terminal domains of the
protein. The C- and N-terminal sections, as well as the stromal and luminal loops between the
helices, are more flexible, but the central helices are more stiff and bind the majority of pigments
[10]. Trimeric LHCII is the most prevalent LHC. Up to 15 Chls can be bound by LHCs, and
their binding sites are well conserved. Chls are made up of a tetrapyrrole ring, which uses its four
nitrogen atoms to coordinate a core Mg2+ ion, an isocyclic ring, and a lengthy hydrophobic
phytol tail. Most Chls are directly linked to the protein through coordination of their core Mg by
side chains of nucleophilic residues (e.g., His, Glu, Gln, or Asn), whereas other Chls are
coordinated by water molecules, the protein backbone, or a lipid molecule. The membrane plane
is roughly parallel to the formation of two layers of the Chls, one closer to the lumen and the
other to the stroma. (Fig. 1)[11].

Ff

Fig.1 Structrural composition of LHCs

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CHEMISTRY OF CAROTENOIDS
Carotenoids are isoprenoid polyenes in terms of chemistry. Since the units in their structure are
linked isoprene (C5) units that can be classified in to C30 (6 units, apocarotenoids), C40 (8
units), C45 (9 units), and C50 (10 units). Tetraterpenoids, or carotenoids containing 40 C atoms,
are the most prevalent types of carotenoids found in nature. With the exception of the
midsection, where the arrangement is tail-to-tail, their molecule is found to be symmetrical, with
the isoprenes placed head-to-tail. Furthermore, carotenoids found in a range of marine species
can be identified by their acetylenic (C C) and allenic (C = C = C) groups. [12,13]. Xanthophylls
and carotenes are the two classes into which carotenoids are usually divided. the oxygenated
derivatives possessing one or more functional groups that contain oxygen. Rhodovibrin and
spirilloxanthin are examples of these derivatives; hydroxy-, criptoxanthin, zeaxanthin, and lutein;
keto-, taxanthin, and canthaxanthin; epoxy-, violaxanthin, neoxanthin, and fucoxanthin;
carboxy-, bixin, and crocetin; oxo-, capsanthin, and rhodoxanthin; and ester, which is the
xanthophyll esterified with fatty acids, are some examples of these derivatives. While
xanthophylls are thought to be products of processes including hydrogenation, dehydrogenation,
cyclization, and oxidation are usually responsible for the creation of xanthophylls from their
basic structure, enzymatic carotenes are hydrocarbons (C40H56). The presence of oxygen-
containing functional groups in xanthophyll structures influences their solubility and biological
characteristics, rendering them more polar than carotenes [14]. Acyclic, monocyclic, and bicyclic
compounds can also be categorized according to the quantity of molecular terminal rings [15].
Because carotene molecules include double bonds, they frequently show signs of cis-trans
isomerization. Carotenoids, however, are mostly found in trans form in nature. They are also
vulnerable to oxidation (autooxidation, photooxidation, and enzymatic oxidation) as a result of
this structural characteristic [16].

BINDING SITES OF CAROTENOIDS IN LHCs

Carotenoids are auxiliary pigments made up of a conjugated chain of polyene with two rings that
usually terminate it. The length of the chain varies (Fig.2). They fall into two categories:
xanthophylls, which also contain oxygen, and carotenes, which solely contain carbon and
hydrogen. While b-carotene, the most significant form of carotene, is primarily present in the
photosystem core units, xanthophylls are typically located in the LHCs [17]. Three carotenoid
binding sites (designated L1, L2, and N1; Fig. 1) are present in all LHCs. The two key locations,
L1 and L2, form a transmembrane cross next to the two core helices. L1 always binds
xanthophyll lutein, but L2's occupancy changes with the LHC; violaxanthin is found in some
minor antennae, and LHCII contains a second lutein. N1 position is occupied by neoxanthin (as
in LHCII) or, in some cases, b-carotene [18,19]. The N1 carotenoid partially protrudes into the
membrane and is severely bent. In LHCII trimers, a fourth carotenoid is present at the interface

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between monomers at V1 site. [20]. In monomeric LHCs [21], V1 is usually empty and is
inhabited by violaxanthin or lutein, that can be exchanged for other xanthophyll cycle
carotenoids in high light. Carotenoids have an important function in photoprotection and are
engaged in light harvesting in all binding sites except V1 [22, 23].

Fig.2 Chemical structure of carotinoids

FUNCTIONAL ROLE OF CAROTENOIDS IN PHOTOPROTECTION

AND LIGHT HARVESTING
Regarding species, distribution, and location, the carotenoid profile of algae is comparable to that
of higher plants [24]. Carotenoids are 400–550 nm light-absorbing chromophores with a yellow-
orange color (Fig. 1). All photosynthetic organisms have them [25]. They perform a variety of
vital biological tasks there, such as (i) stabilizing lipid membranes and assembling lipid protein
structures [26, 27]. (for example, filaments); (ii) photosynthetic light harvesting; and (iii)
preventing the oxidative damage of photosystems caused by photoradiation, which is frequently
linked to reactive oxygen species (ROS) [28]. Carotenoids play an important role in regulation of
both photosynthetic and non-photosynthetic species, in addition to their protective function [29].
For instance, carotenoids are broken down by enzymes called NCEDs (9-cis-epoxy carotenoid
dioxygenases) and CCDs (carotenoid cleavage dioxygenases). The resulting products, found in
fruit pericarp, flowers, and seeds, serve as precursors for the production of essential primary and
secondary metabolites, such as the phytohormones strigolactones [30,31] and abscisic acid [29]
as well as significant favors and aroma compounds.

Products with these carotenoid-derived flavor and fragrance components are valued in the food,
floral, wine, bourbon, cosmetic, and spice sectors [34–36]. Because of their many uses,
carotenoids are essential for light absorption in blue-green zone [37, 38]. They also transfer
energy to Chl (see Fig.2), which broadens the light spectrum that the light harvesting complex
can gather. By assembling photosystems that improve the functioning of the photosynthetic
equipment, carotenoids also have a role in controlling gene expression through the products of
oxidation [39]. When light absorption exceeds what the photosystems can use, carotenoids help
quench the surplus energy , which may otherwise lead to the creation of harmful Chl triplets (see

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the Xanthophyll (ZAV) and Lutein (LxL) cycles below) [40]. Any blockage in the manufacture
of carotenoids is fatal to all photosynthetic organisms because of the protective role that these
compounds have in relation to thelight harvesting complex and the RC. The generation of ROS is
increased under high light (HL) stress [41,42], which can be harmful to proteins and other
organic molecules . The polyunsaturated fatty acids that are prevalent in the lipids of the
thylakoid membrane are very susceptible to oxidation by reactive oxygen species (ROS). This
can lead to the formation of lipid hydroperoxides, which can set off a series of events that can
ultimately destroy the chloroplast membrane [43]. When a plant absorbs more light than it can
utilize for photosynthetic processes, it must dissipate the surplus energy or it may harm the
photosystems, especially the D1 protein, which lowers photosynthetic capability. This is referred
to as photoinhibition (Fig. 3). If PSII photo damage occurs at a rate higher than its repair rate,
then under extreme stress, the photoinhibition rate increases [44] (see Fig. 3). In addition to
directly quenching triplet Chl, a significant source of singlet oxygen, certain carotenoids are also
involved in quenching reactive oxygen species (ROS). For instance, it has been observed that β-
carotene (β-car) quenches singlet oxygen and triplet chloride in photosystem’s core complex
[45]. The xanthophyll pigment zeaxanthin (Z) is present in thylakoids free or attached to the
antenna proteins in light harvesting complexes. It has been shown that this free pool of Z has the
ability to quench excited Chl molecules [46], and that when it binds to proteins found in the light
harvesting center [47]. It increases its antioxidant capability. Additionally, the free pool of Z
exhibits its photoprotective characteristic Photosynthesis Research in the lipids of the thylakoid
membrane by eliminating singlet oxygen species and functions as an antioxidant in concert with
tocopherol [48, 49]. Another xanthophyll carotenoid called lutein is considered to be the most
significant xanthophyll stabilizing the light harvesting complexes [50]. Lutein also actively
functions as a photoprotectant.

THE XANTHOPHYLL (ZEAXANTHIN) CYCLE AND NON PHOTO-

CHEMICAL QUENCHING
A lot of photosynthetic organisms use mechanisms to dissipate absorbed light energy that is
greater than can be used for photosynthesis because, as was previously mentioned,
photosynthetic organisms can modify the size of the light harvesting antennae as a moderate to
long-term acclimation to growth light environment. However, irradiance also changes on much
shorter time scales, seconds to hours. Singlet-excited chlorophylls are quenched through a
process called non-photochemical quenching (NPQ), in which the energy is released as heat The
primary form of NPQ is the pH or energy dependent component (fig4 ) [51] which depends on
the protein PsbS as well as the xanthophyll cycle (VAZ cycle) . This primary quenching factor is
caused by the thylakoid lumen becoming acidic [52], which happens as a result of electron
transport and results in the activation of violaxanthin de-epoxidase catalysing the conversion of
violaxanthin (V) [via antherax anthin (A) to zeaxanthin (Z). Fast variations in the VAZ cycle are
necessary for plastids to adapt to changing light levels because they control light energy
conversion, safeguarding the photosynthetic apparatus [53].

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Manufacturing of Z is induced by environmental stressors such as intense light, injury, cold,
dehydration, and salt stress, which can promote the creation of reactive oxygen species (ROS) by
saturating photosynthetic electron transport.. Variations in transmembrane pH cause NPQ to be
activated by the protonation of the PSII antennae protein PsbS's carboxylic acid residues and the
enzymatic conversion of violaxanthin to zeaxanthin [54]. Stress-sensing proteins, such as PsbS
and Light Harvesting Complex Stress Related 3 (LhcSR3), are essential for the start of NPQ
[55]. It was shown that NPQ in C. reinhardtii was triggered by high light-induced PsbS and
LhcSR3 accumulation. These authors also suggested that PsbS plays a critical role in NPQ
activation by promoting conformational changes necessary to activate LHCSR3-dependent
quenching in the photosystem II antenna. LhcSR3, a pigment binding protein, binds xanthophylls
V, Z, and L in addition to Chl a and Chl b, unlike PsbS. It builds up at times of intense light and
quenches Chl molecules in the excited state, and it is necessary for C. reinhardtii energy
quenching (qE)[56]. Additionally, this protein promotes the synthesis of lutein radical cations,
which helps to further aid in the process of expelling excess energy. Recent research has
confirmed that over-expression of VDE and ZEP to increase xanthophyll cycle kinetics and
increased levels of PsbS protein to sense pH in the lumen have a direct impact on the speed at
which CO2 fixation is recovered and NPQ relaxes following a high-light period. These results
indicated areas for improvement in terms of CO2 fixation, maximal carboxylation capacity
(Vcmax), and ribulose bisphosphate regeneration capacity (Jmax). Accelerating plant recovery to
changing circumstances in the field also increased biomass by 14–20%. These findings suggest
that it is possible to increase plant productivity and yield potential by taking advantage of NPQ's
quicker activation and relaxation. Increased PsbS expression was shown to decrease stomatal
opening in yet another study with transgenic tobacco plants, resulting in a 25% reduction in
water loss per assimilated carbon dioxide [57]. Recent findings in Arabidopsis thaliana have
demonstrated that, in contrast to the findings in tobacco, the overexpression of Instead of causing
a rise in productivity, VDE, ZEP, and PsbS proteins hindered the accumulation of
biomass .These inconsistent results between tobacco and Arabidopsis provide more evidence that
the constraints and management of NPQ may vary depending on the species. To achieve
consistent results that increase yield consistently in a variety of growing environments, it is
necessary to identify specific targeted manipulations for various crop plants. Nevertheless, these
data offer a way to manipulations for various crop plants [58].

THE LUTEIN EPOXIDE AMD NON-PHOTOCHEMICAL QUENCHING

Lutein has crucial role in functioning of plants ranging from enhancing the antenna proteins
stability, light harvesting through excitation energy transfer to Chl and Chl triplet state
quenching in LHCII and superfluous energy dissipation (NPQ), accumulation of L (by
conversion of lutein epoxide (Lx) to L) in the light harvesting complex converts this highly
efficient light harvesting system into a system for energy dissipation [59]. Similar to the other
protective carotenoids, such as VAZ, the induction of NPQ by L is caused by a drop in lumen
pH. Recent research proved that this is typically caused by photosynthetic electron transport at

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high light intensities. It can also be caused by increased cyclic electron flow or a decrease in
chloroplast ATPase proton conductance as a result of decreased ATP utilization, such as
decreased calvin cycle activity [60]. The LxL cycle was originally described in green tomato
fruit and was identified later in photosynthetic stems of Cuscuta reflexa. In terms of quenching
the triple states of Chl, L is more effective than V. Because the higher canopy shields the older,
shaded leaves from bright light, Lx frequently accumulates in these leaves. The Lx cycle is
active at low temperatures, and lutein concentration is raised as a result of lutein binding to Early
Light-Induced Protein that builds up in stressed plants. It has also been demonstrated that Lx and
V co-localize in Inga's shadow leaves. According to earlier suggestions, this co-localization
suggests that Lx is likely to be physically and functionally identical to V [61]. Under intense
light, the VDE enzyme not only de-epoxylates V in the VAZ cycle but also the Lx β-ring ( Fig
4). Converting Lx to L again, The enzyme ZEP is most likely responsible for the epoxidation of
L's β-ring, which converts L to Lx It should be mentioned that because ZEP has a poor affinity
for L, the epoxidation of L proceeds very slowly. The potential to create plants with a higher
functional LxL cycle, which enhances and supplements the VAZ cycle and increases the
efficiency of NPQ, is provided by the identification of ZEP and VDE variations with a stronger
affinity for L and Lx. Given that VAZ and LxL are two kinetically separate cycles, this technique
would work. After being exposed to intense light, L (created by converting Lx to L) takes the
place of Lx in the light-harvesting complexes, replacing A + Z; to “lock in” a potential for higher
NPQ in the dark thereby reducing PSII photochemical efficiency. α-car, the precursor for the
synthesis of L, has been observed to accumulate in the leaves and green fruit of several plant
species, including carrots and coffee at the expense of β-car [62]. It has been proposed
previously that in some circumstances, α-car molecules could take the place of β-car molecules
needed for the assembly of photosystem II complex. In plants where the Lx cycle may be more
significant, this extra α-car accumulation might be necessary to stabilize the pool of L.
Enhancing the Lx cycle in plants where the VAZ cycle predominates may provide plants
exposed to intense light with increased protection or increased flexibility, depending on the
amount of carotenoids that are available [63].

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Fig.3 Defence mechanisms of photosynthetic pigments as stress busters. The figure illustrates the
pathways initiated by pigments as photo protectants in response to environmental stress thereby
reduc ing photoinhibition which curtails photosynthetic efficiency

Fig. 4 The Lutein (LxL) cycles and xanthophyll (ZAV) production pathways are represented by
these pathways. β-carotene is created when Lycopene β-cyclase (β/βcyclase) adds two β-rings to
the ends of the Lycopene carbon chain. Lycopene β-cyclase and Lycopene ε-cyclase
subsequently add a β- and β-ring to lycopene, respectively, to create α-carotene. Oxygenated
carotenoids are produced when the β and ε-rings of beta- and alpha-carotene are hydroxylated. β-
carotene hydroxylase converts β-carotene to zeaxanthin, whereas βCHY hydroxylates the β-rings
of α-carotene, and ε-carotene hydroxylase hydroxylates the ε-rings to generate lutein. The two
hydroxylated β-rings of zeaxanthin are epoxidized in two processes by zeaxanthin epoxidase
(ZEP), producing violaxanthin and antheraxanthin. The enzyme violaxanthin de-epoxidase
(VDE) is responsible for converting violaxanthin back to zeaxanthin in strong light.
Additionally, these two enzymes can create Lutein epoxide by epoxidizing and de-epoxidizing
the β-rings of lutein.

FUNCTIONAL ROLE OF CAROTENOIDS IN CYANOBACTERIA

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Cyanobacteria are photosynthetic organisms with a light-harvesting complex that makes it easier
for light energy to be absorbed for photosynthesis. Carotenoids, phycobiliproteins, and
chlorophylls are the three chemical groups that comprise the pigments that comprise this
harvesting complex [64]. In the thylakoid membrane, these materials are organized parallel to the
cell membrane. Specifically, the majority of carotenoids and chlorophyll are present in a
transmembrane protein complex inside the photosystem, while cyanobacteria have an outer
membrane-bound phycobilisome that contains phycobili proteins and orange carotenoid proteins
(OCP), which includes hydroxyechinenone [65]. Carotenoids have a significant effect on non-
photochemical quenching (NPQ) as protective agents against saturating light and as a quencher
of reactive oxygen species (ROS) in cyanobacteria, where phycobiliproteins are the primary
pigments for light absorption [66].Regarding carotenoids, these terpenoids pigments are thought
to be transverse through photosynthetic organisms and are necessary for their existence. About
600 pigments are classified as carotenoids, and they can be further classified into two main
classes: xanthophylls, which are oxygenized derivatives of carotenes and include zeaxanthin and
echinenone, and carotenes, which include α- and β-carotene [67,68].

Carotenoids are polymers mostly composed of a C40 hydrocarbon chain with multiple double-bound
conjugations and eight isoprenoids. They can be further separated into two groups: carotenes, which
are linear or cyclized molecules lacking oxygen atoms and having one or two rings at their extremities,
and xanthophylls, which are oxygenated derivatives of carotenes. Moreover, modifications to carotenes
may lead to the production of glycosylated carotenoids such as myxoxanthophyll or even
apocarotenoids, which are carotenoids with shorter chains [58]. Carotenogenesis is a complex but well-
characterized biochemical route that allows cyanobacteria to manufacture a broad range of terpenoids
(Figure 6). Geranylgeranyl pyrophosphate precursor is the starting point for the synthesis of these
chemicals [69]. The synthases, desaturases, hydroxylases, and cyclases involved in the production of
carotenoids are encoded by a number of genes [60]. Many cyanobacterial species were used to assess
the presence of the specified genes. It was discovered that while certain genes can be identified as
redundant or as a replacement for other genes, the majority of the genes are transversal. [70].

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Fig.6 Carotenoids biosynthetic cycle in Cyanobacteria.

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BIOSYNTHESIS OF CAROTENOIDS IN CYANOBACTERIA

Using phytoene synthase (CrtB), two molecules of geranylgeranyl pyrophosphate are first
condensed into phytoene. Phytoene desaturase (CrtP) can then convert phytoene to ζ-carotene,
and carotene desaturase (CrtQ) can finally convert phytoene to lycopene. Certain species, like
Anabaena and Nostoc, can convert phytoene straight to lycopene by means of a phytoene
desaturase (CrtI), even if they also produce the typical phytoene desaturase (CrtP) [71]. The two
main primary carotenoids, α- and β-carotene, are produced from lycopene. Lycopene cyclase
(CrtL or CruA) converts α-carotene directly, but β-carotene is produced by lycopene cyclase
(CrtL or CruA) in two steps from γ-carotene [72]. Several xanthophylls can be generated from
the three carotenoids in the following ways.Myxoxanthophyll is created from γ-carotene by
hydroxylation by γ-carotene hydroxylase (CruF) and glycoside group addition by
glycosyltransferase (CruG). The formation of myxoxanthophyll, a yellow glycoside terpenoid
unique to cyanobacteria, is necessary for the organization of thylakoids and the structure of cell
walls [73].α-carotene can be converted to lutein by a hydroxylase (CrtR) [66]. β-carotene can be
converted to zeaxanthin by a hydroxylase (CrtR) or to an echinenone by a ketolase (CrtO or
CrtW). Moreover, hydroxylase (CrtR) may produce hydroxyechinenone from echinenone, the
main ketocarotenoid in the OCP, and ketolase (CrtO or CrtW) can form canthaxanthin from
echinenone. The violaxanthin cycle is the mechanism by which zeaxanthin is transformed into
both antheraxanthin and violaxanthin by the reversible activity of epoxidase and de-epoxidase.
While neoxanthin synthase (NSY) may make neoxanthin from violaxanthin, hydroxylase (CrtG)
can also produce nostoxanthin from zeaxanthin [74]. Moreover, astaxanthin can be produced by
inserting a CrtR or CrtW gene into transgenic cyanobacteria. Astaxanthin can be generated by
hydroxylase from canthaxanthin. [75].

ORANGE CAROTENOID PROTEIN

Cyanobacteria primarily use phycobilisomes. These are the protein component of the antenna
pigments of extramembrane known as phycobiliproteins which absorb light and transfer energy
to the core of photosystem. [76]. Conversely, the primary roles of carotenoids in cyanobacteria
are dissipation of energy and defense against oxidative damage. In order for the photosystem
core to be reached, extra light energy must be reduced by the NPQ. The photoprotective enzyme
OCP requires carotenoids, which are located in cyanobacteria's reaction center with chlorophyll
molecules or in protein complexes containing a single carotenoid molecule [77]. The OCP is a 35
kDa protein that dissolves in water and contains a single hydroxyechinenone molecule. This
molecule is present in an inactive form (orange) and is activated (red) in response to blue-green
light (Figure 7). Despite being essential for cell defense, the OCP typically makes up only 1% of
all carotenoids [78].

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Fig.7 Energy dissipation of Orange carotenoid protein (OCP) under saturation of light.

The OCP is composed of two domains joined by a flexible linker. A cyanobacteria-specific all-
helical N-terminal domain is the first, and a C-terminal α/β-fold domain that is found in all
kingdoms is the second [79]. The constitutively expressed slr1963 gene [80] encodes the OCP,
and stressors like as prolonged exposure to light or salt stress can temporarily acclimate cells to
the environment and boost the transcription of the gene. To sum up, the phycobilisome only
attaches to the OCP when it is red, or active, as shown in Fig.7. In total darkness or low light, the
phycobilisome can absorb all available light and transfer it to the photosystem. In saturation light
(strong blue-green or white), OCP takes on an active form. It binds to the phycobilisome to aid in
energy dissipation and enable non-saturating absorption by the photosystem. Phycobiliproteins
and OCP are not the only proteins engaged in the process; other proteins, such as the
fluorescence recovery protein (FRP), are responsible for deactivating OCP during the NPQ
process [81].

CONCLUSION

From the explanation above, it can be inferred that carotenoids enhance photosynthesis
efficiency, which is a provital role for them in light harvesting complexes. These pigments shield
the photosynthetic machinery from oxidative damage and excessive light, in addition to
broadening the absorption spectrum and enabling the uptake of a wider variety of wavevelengths
of light. As we continue to understand the complexities of these light-harvesting complexes, the
importance of carotenoids in maintaining life through photosynthesis becomes more and more
clear, highlighting their critical role in light conversion in chloroplasts. The complex interactions

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between carotenoids and chlorophyll molecules optimize energy transfer, contributing to overall
robustness and adaptability of photosynthetic organisms.

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