Structure
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Chlorophyll c refers to forms of chlorophyll found in certain marine algae, including the photosynthetic Chromista (e.g. diatoms and brown algae) and dinoflagellates. [1] [2] [3] These pigments are characterized by their unusual chemical structure, with a porphyrin as opposed to the chlorin (which has a reduced ring D) as the core; they also do not have an isoprenoid tail. Both these features stand out from the other chlorophylls commonly found in algae and plants. [2]
It has a blue-green color and is an accessory pigment, particularly significant in its absorption of light in the 447–520 nm wavelength region. [3] Like chlorophyll a and chlorophyll b, it helps the organism gather light and passes a quanta of excitation energy through the light harvesting antennae to the photosynthetic reaction centre. [2]
Chlorophyll c can be further divided into chlorophyll c1, chlorophyll c2, [3] and chlorophyll c3, [4] plus at least eight other more recently found subtypes. [5]
Chlorophyllc1 is a common form of chlorophyll c. It differs from chlorophyll c2 in its C8 group, having an ethyl group instead of vinyl group (C-C single bond instead of C=C double bond). Its absorption maxima are around 444, 577, 626 nm and 447, 579, 629 nm in diethyl ether and acetone respectively. [6]
Chlorophyllc2 is the most common form of chlorophyll c. [7] Its absorption maxima are around 447, 580, 627 nm and 450, 581, 629 nm in diethyl ether and acetone respectively. [6]
Chlorophyllc3 is a form of chlorophyll c found in microalga Emiliania huxleyi , identified in 1989. [4] Its absorption maxima are around 452, 585, 625 nm and 452, 585, 627 nm in diethyl ether and acetone respectively. [6]
Chlorophyll c synthesis branches off early from the typical Chlorophyllide synthesis pathway, after divinylprotochlorophyllide (DV-PChlide) is formed. DV-PChlide can be processed directly by an unidentified 171 oxidase into Chl c2. An 8-vinyl reductase (elaborating on the promiscous behavior of ferredoxin-type 3,8-divinyl chlorophyllide reductase) could then convert Chl c2 into Chl c1. The two steps could be swapped for the same effect. [8]
The 171 oxidtion appears to proceed by "hydroxylation of the 17-propionate reside at the 171-position and successive dehydration to the 17-acrylate residue." [9]
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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.
Photosynthesis is a system of biological processes by which photosynthetic organisms, such as most plants, algae, and cyanobacteria, convert light energy, typically from sunlight, into the chemical energy necessary to fuel their activities. Photosynthetic organisms use intracellular organic compounds to store the chemical energy they produce in photosynthesis. Photosynthesis is usually used to refer to oxygenic photosynthesis, a form of photosynthesis where the photosynthetic processes produce oxygen as a byproduct and synthesize carbohydrate molecules like sugars, starches, glycogen, and cellulose to store the chemical energy. To use the chemical energy stored in these organic compounds, the organisms' cells metabolize the organic compounds through another process called cellular respiration. Photosynthesis is largely responsible for producing and maintaining the oxygen content of the Earth's atmosphere, and it supplies most of the biological energy necessary for complex life on Earth.
Fucoxanthin is a xanthophyll, with formula C42H58O6. It is found as an accessory pigment in the chloroplasts of brown algae and most other heterokonts, giving them a brown or olive-green color. Fucoxanthin absorbs light primarily in the blue-green to yellow-green part of the visible spectrum, peaking at around 510-525 nm by various estimates and absorbing significantly in the range of 450 to 540 nm.
Bacteriochlorophylls (BChl) are photosynthetic pigments that occur in various phototrophic bacteria. They were discovered by C. B. van Niel in 1932. They are related to chlorophylls, which are the primary pigments in plants, algae, and cyanobacteria. Organisms that contain bacteriochlorophyll conduct photosynthesis to sustain their energy requirements, but the process is anoxygenic and does not produce oxygen as a byproduct. They use wavelengths of light not absorbed by plants or cyanobacteria. Replacement of Mg2+ with protons gives bacteriophaeophytin (BPh), the phaeophytin form.
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.
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 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.
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.
Chlorophyll d is a form of chlorophyll, identified by Harold Strain and Winston Manning in 1943. It was unambiguously identified in Acaryochloris marina in the 1990s. It is present in cyanobacteria which use energy captured from sunlight for photosynthesis. Chl d absorbs far-red light, at 710 nm wavelength, just outside the optical range. An organism that contains Chl d is adapted to an environment such as moderately deep water, where it can use far red light for photosynthesis, although there is not a lot of visible light.
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.
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.
The photosynthetic efficiency is the fraction of light energy converted into chemical energy during photosynthesis in green plants and algae. Photosynthesis can be described by the simplified chemical reaction
In enzymology, protochlorophyllide reductases (POR) are enzymes that catalyze the conversion from protochlorophyllide to chlorophyllide a. They are oxidoreductases participating in the biosynthetic pathway to chlorophylls.
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.
Protochlorophyllide, or monovinyl protochlorophyllide, is an intermediate in the biosynthesis of chlorophyll a. It lacks the phytol side-chain of chlorophyll and the reduced pyrrole in ring D. Protochlorophyllide is highly fluorescent; mutants that accumulate it glow red if irradiated with blue light. In angiosperms, the later steps which convert protochlorophyllide to chlorophyll are light-dependent, and such plants are pale (chlorotic) if grown in the darkness. Gymnosperms, algae, and photosynthetic bacteria have another, light-independent enzyme and grow green in the darkness as well.
Light-dependent reactions refers to 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).
Chlorophyll f is a type form of chlorophyll that absorbs further in the red than other chlorophylls. In 2010, it was reported by Min Chen to be present in stromatolites from Western Australia's Shark Bay.
Chlorophyll(ide) b reductase (EC 1.1.1.294), chlorophyll b reductase, Chl b reductase) is an enzyme with systematic name 71-hydroxychlorophyllide-a:NAD(P)+ oxidoreductase. This enzyme catalyses the following chemical reaction
Chlorophyllide a and Chlorophyllide b are the biosynthetic precursors of chlorophyll a and chlorophyll b respectively. Their propionic acid groups are converted to phytyl esters by the enzyme chlorophyll synthase in the final step of the pathway. Thus the main interest in these chemical compounds has been in the study of chlorophyll biosynthesis in plants, algae and cyanobacteria. Chlorophyllide a is also an intermediate in the biosynthesis of bacteriochlorophylls.
