Light-harvesting complexes of green plants

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Chlorophyll A-B binding protein
2bhw.png
Light-Harvesting Complex II (LHCB)
Identifiers
SymbolChloroa_b-bind
Pfam PF00504
InterPro IPR022796
SCOP2 1rwt / SCOPe / SUPFAM
OPM superfamily 2
OPM protein 1rwt
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

The light-harvesting complex (or antenna complex; LH or LHC) is an array of protein and chlorophyll molecules embedded in the thylakoid membrane of plants and cyanobacteria, which transfer light energy to one chlorophyll a molecule at the reaction center of a photosystem.

Contents

The antenna pigments are predominantly chlorophyll b, xanthophylls, and carotenes. Chlorophyll a is known as the core pigment. Their absorption spectra are non-overlapping and broaden the range of light that can be absorbed in photosynthesis. The carotenoids have another role as an antioxidant to prevent photo-oxidative damage of chlorophyll molecules. Each antenna complex has between 250 and 400 pigment molecules and the energy they absorb is shuttled by resonance energy transfer to a specialized chlorophyll-protein complex known as the reaction center of each photosystem. [1] The reaction center initiates a complex series of chemical reactions that capture energy in the form of chemical bonds.

For photosystem II, when either of the two chlorophyll a molecules at the reaction center absorb energy, an electron is excited and transferred to an electron acceptor molecule, pheophytin, leaving the chlorophyll a in an oxidized state. The oxidised chlorophyll a replaces the electrons by photolysis that involves the oxidation of water molecules to oxygen, protons and electrons.

The N-terminus of the chlorophyll a-b binding protein extends into the stroma where it is involved with adhesion of granal membranes and photo-regulated by reversible phosphorylation of its threonine residues. [2] Both these processes are believed to mediate the distribution of excitation energy between photosystems I and II.

This family also includes the photosystem II protein PsbS, which plays a role in energy-dependent quenching that increases thermal dissipation of excess absorbed light energy in the photosystem. [3]

LH 1

Light-harvesting complex I is permanently bound to photosystem I via the plant-specific subunit PsaG. It is made up of four proteins: Lhca1, Lhca2, Lhca3, and Lhca4, all of which belong to the LHC or chlorophyll a/b-binding family. The LHC wraps around the PS1 reaction core. [4]

LH 2

The LH 2 is usually bound to photosystem II, but it can undock and bind PS I instead depending on light conditions. [4] This behavior is controlled by reversible phosphorylation. This reaction represents a system for balancing the excitation energy between the two photosystems. [5]

Related Research Articles

<span class="mw-page-title-main">Chlorophyll</span> Green pigments found in plants, algae and bacteria

Chlorophyll is any of several related green pigments found in cyanobacteria and in the chloroplasts of algae and plants. Its name is derived from the Greek words χλωρός, khloros and φύλλον, phyllon ("leaf"). Chlorophyll allow plants to absorb energy from light.

<span class="mw-page-title-main">Photosynthesis</span> Biological process to convert light into chemical energy

Photosynthesis is a biological process used by many cellular organisms to convert light energy into chemical energy, which is stored in organic compounds that can later be metabolized through cellular respiration to fuel the organism's activities. The term usually refers to oxygenic photosynthesis, where oxygen is produced as a byproduct, and some of the chemical energy produced is stored in carbohydrate molecules such as sugars, starch and cellulose, which are synthesized from endergonic reaction of carbon dioxide with water. Most plants, algae and cyanobacteria perform photosynthesis; such organisms are called photoautotrophs. Photosynthesis is largely responsible for producing and maintaining the oxygen content of the Earth's atmosphere, and supplies most of the biological energy necessary for complex life on Earth.

<span class="mw-page-title-main">Thylakoid</span> Membrane enclosed compartments in chloroplasts and cyanobacteria

Thylakoids are membrane-bound compartments inside chloroplasts and cyanobacteria. They are the site of the light-dependent reactions of photosynthesis. Thylakoids consist of a thylakoid membrane surrounding a thylakoid lumen. Chloroplast thylakoids frequently form stacks of disks referred to as grana. Grana are connected by intergranal or stromal thylakoids, which join granum stacks together as a single functional compartment.

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

Chloroplasts contain several important membranes, vital for their function. Like mitochondria, chloroplasts have a double-membrane envelope, called the chloroplast envelope, but unlike mitochondria, chloroplasts also have internal membrane structures called thylakoids. Furthermore, one or two additional membranes may enclose chloroplasts in organisms that underwent secondary endosymbiosis, such as the euglenids and chlorarachniophytes.

<span class="mw-page-title-main">Photosystem</span> Structural units of protein involved in photosynthesis

Photosystems are functional and structural units of protein complexes involved in photosynthesis. Together they carry out the primary photochemistry of photosynthesis: the absorption of light and the transfer of energy and electrons. Photosystems are found in the thylakoid membranes of plants, algae, and cyanobacteria. These membranes are located inside the chloroplasts of plants and algae, and in the cytoplasmic membrane of photosynthetic bacteria. There are two kinds of photosystems: PSI and PSII.

<span class="mw-page-title-main">Photosystem II</span> First protein complex in light-dependent reactions of oxygenic photosynthesis

Photosystem II is the first protein complex in the light-dependent reactions of oxygenic photosynthesis. It is located in the thylakoid membrane of plants, algae, and cyanobacteria. Within the photosystem, enzymes capture photons of light to energize electrons that are then transferred through a variety of coenzymes and cofactors to reduce plastoquinone to plastoquinol. The energized electrons are replaced by oxidizing water to form hydrogen ions and molecular oxygen.

<span class="mw-page-title-main">Photosystem I</span> Second protein complex in photosynthetic light reactions

Photosystem I is one of two photosystems in the photosynthetic light reactions of algae, plants, and cyanobacteria. Photosystem I is an integral membrane protein complex that uses light energy to catalyze the transfer of electrons across the thylakoid membrane from plastocyanin to ferredoxin. Ultimately, the electrons that are transferred by Photosystem I are used to produce the moderate-energy hydrogen carrier NADPH. The photon energy absorbed by Photosystem I also produces a proton-motive force that is used to generate ATP. PSI is composed of more than 110 cofactors, significantly more than Photosystem II.

Chlorophyll <i>a</i> Chemical compound

Chlorophyll a is a specific form of chlorophyll used in oxygenic photosynthesis. It absorbs most energy from wavelengths of violet-blue and orange-red light, and it is a poor absorber of green and near-green portions of the spectrum. Chlorophyll does not reflect light but chlorophyll-containing tissues appear green because green light is diffusively reflected by structures like cell walls. This photosynthetic pigment is essential for photosynthesis in eukaryotes, cyanobacteria and prochlorophytes because of its role as primary electron donor in the electron transport chain. Chlorophyll a also transfers resonance energy in the antenna complex, ending in the reaction center where specific chlorophylls P680 and P700 are located.

<span class="mw-page-title-main">Photophosphorylation</span> Biochemical process in photosynthesis

In the process of photosynthesis, the phosphorylation of ADP to form ATP using the energy of sunlight is called photophosphorylation. Cyclic photophosphorylation occurs in both aerobic and anaerobic conditions, driven by the main primary source of energy available to living organisms, which is sunlight. All organisms produce a phosphate compound, ATP, which is the universal energy currency of life. In photophosphorylation, light energy is used to pump protons across a biological membrane, mediated by flow of electrons through an electron transport chain. This stores energy in a proton gradient. As the protons flow back through an enzyme called ATP synthase, ATP is generated from ADP and inorganic phosphate. ATP is essential in the Calvin cycle to assist in the synthesis of carbohydrates from carbon dioxide and NADPH.

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

Phycobilisomes are light harvesting antennae of photosystem II in cyanobacteria, red algae and glaucophytes. It was lost in the plastids of green algae / plants (chloroplasts).

Photodissociation, photolysis, photodecomposition, or photofragmentation is a chemical reaction in which molecules of a chemical compound are broken down by photons. It is defined as the interaction of one or more photons with one target molecule.

<span class="mw-page-title-main">Photosynthetic reaction centre</span> Molecular unit responsible for absorbing light in photosynthesis

A photosynthetic reaction center is a complex of several proteins, pigments and other co-factors that together execute the primary energy conversion reactions of photosynthesis. Molecular excitations, either originating directly from sunlight or transferred as excitation energy via light-harvesting antenna systems, give rise to electron transfer reactions along the path of a series of protein-bound co-factors. These co-factors are light-absorbing molecules (also named chromophores or pigments) such as chlorophyll and pheophytin, as well as quinones. The energy of the photon is used to excite an electron of a pigment. The free energy created is then used, via a chain of nearby electron acceptors, for a transfer of hydrogen atoms (as protons and electrons) from H2O or hydrogen sulfide towards carbon dioxide, eventually producing glucose. These electron transfer steps ultimately result in the conversion of the energy of photons to chemical energy.

A light-harvesting complex consists of a number of chromophores which are complex subunit proteins that may be part of a larger super complex of a photosystem, the functional unit in photosynthesis. It is used by plants and photosynthetic bacteria to collect more of the incoming light than would be captured by the photosynthetic reaction center alone. The light which is captured by the chromophores is capable of exciting molecules from their ground state to a higher energy state, known as the excited state. This excited state does not last very long and is known to be short-lived.

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

Photoinhibition is light-induced reduction in the photosynthetic capacity of a plant, alga, or cyanobacterium. Photosystem II (PSII) is more sensitive to light than the rest of the photosynthetic machinery, and most researchers define the term as light-induced damage to PSII. In living organisms, photoinhibited PSII centres are continuously repaired via degradation and synthesis of the D1 protein of the photosynthetic reaction center of PSII. Photoinhibition is also used in a wider sense, as dynamic photoinhibition, to describe all reactions that decrease the efficiency of photosynthesis when plants are exposed to light.

<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.

<span class="mw-page-title-main">Cytochrome b559</span> Family of protein complexes

Cytochrome b559 is an important component of Photosystem II (PSII) is a multisubunit protein-pigment complex containing polypeptides both intrinsic and extrinsic to the photosynthetic membrane. Within the core of the complex, the chlorophyll and beta-carotene pigments are mainly bound to the antenna proteins CP43 (PsbC) and CP47 (PsbB), which pass the excitation energy on to chlorophylls in the reaction centre proteins D1 and D2 that bind all the redox-active cofactors involved in the energy conversion process. The PSII oxygen-evolving complex (OEC) provides electrons to re-reduce the PSII reaction center, and oxidizes 2 water molecules to recover its reduced initial state. It consists of OEE1 (PsbO), OEE2 (PsbP) and OEE3 (PsbQ). The remaining subunits in PSII are of low molecular weight, and are involved in PSII assembly, stabilisation, dimerization, and photoprotection.

<span class="mw-page-title-main">Photosystem II light-harvesting protein</span>

Photosystem II light-harvesting proteins are the intrinsic transmembrane proteins CP43 (PsbC) and CP47 (PsbB) occurring in the reaction centre of photosystem II (PSII). These polypeptides bind to chlorophyll a and β-Carotene and pass the excitation energy on to the reaction centre.

Non-photochemical quenching (NPQ) is a mechanism employed by plants and algae to protect themselves from the adverse effects of high light intensity. It involves the quenching of singlet excited state chlorophylls (Chl) via enhanced internal conversion to the ground state, thus harmlessly dissipating excess excitation energy as heat through molecular vibrations. NPQ occurs in almost all photosynthetic eukaryotes, and helps to regulate and protect photosynthesis in environments where light energy absorption exceeds the capacity for light utilization in photosynthesis.

<span class="mw-page-title-main">Light-dependent reactions</span> Photosynthetic reactions

Light-dependent reactions is jargon for certain photochemical reactions that are involved in photosynthesis, the main process by which plants acquire energy. There are two light dependent reactions, the first occurs at photosystem II (PSII) and the second occurs at photosystem I (PSI),

<span class="mw-page-title-main">Ycf9 protein domain</span> Plastid protein involved in photosynthesis

In molecular biology, the PsbZ (Ycf9) is a protein domain, which is low in molecular weight. It is a transmembrane protein and therefore is located in the thylakoid membrane of chloroplasts in cyanobacteria and plants. More specifically, it is located in Photosystem II (PSII) and in the light-harvesting complex II (LHCII). Ycf9 acts as a structural linker, that stabilises the PSII-LHCII supercomplexes. Moreover, the supercomplex fails to form in PsbZ-deficient mutants, providing further evidence to suggest Ycf9's role as a structural linker. This may be caused by a marked decrease in two LHCII antenna proteins, CP26 and CP29, found in PsbZ-deficient mutants, which result in structural changes, as well as functional modifications in PSII.

References

  1. Voet D, Voet JG (2011). Biochemistry 4th Ed . USA: Wiley. pp.  906. ISBN   978-0470-57095-1.
  2. Yang DH, Paulsen H, Andersson B (January 2000). "The N-terminal domain of the light-harvesting chlorophyll a/b-binding protein complex (LHCII) is essential for its acclimative proteolysis". FEBS Letters. 466 (2–3): 385–8. doi:10.1016/S0014-5793(00)01107-8. PMID   10682866. S2CID   19716587.
  3. Li XP, Gilmore AM, Caffarri S, Bassi R, Golan T, Kramer D, Niyogi KK (May 2004). "Regulation of photosynthetic light harvesting involves intrathylakoid lumen pH sensing by the PsbS protein". The Journal of Biological Chemistry. 279 (22): 22866–74. doi: 10.1074/jbc.M402461200 . PMID   15033974.
  4. 1 2 Grotjohann I, Fromme P (2013). "Photosystem I". Encyclopedia of biological chemistry (Second ed.). London. pp. 503–507. doi:10.1016/B978-0-12-378630-2.00287-5. ISBN   978-0-12-378630-2.{{cite book}}: CS1 maint: location missing publisher (link)
  5. Liu XD, Shen YG (July 2004). "NaCl-induced phosphorylation of light harvesting chlorophyll a/b proteins in thylakoid membranes from the halotolerant green alga, Dunaliella salina". FEBS Letters. 569 (1–3): 337–40. doi:10.1016/j.febslet.2004.05.065. PMID   15225658. S2CID   23367090.

See also