Retinal in the context of Chlorophyll

Photosynthesis (/ˌfoʊtəˈsɪnθəsɪs/ FOH-tə-SINTH-ə-sis) is a system of biological processes by which photopigment-bearing autotrophic organisms, such as most plants, algae and cyanobacteria, convert light energy — typically from sunlight — into the chemical energy necessary to fuel their metabolism. The term photosynthesis usually refers to oxygenic photosynthesis, a process that releases oxygen as a byproduct of water splitting. Photosynthetic organisms store the converted chemical energy within the bonds of intracellular organic compounds (complex compounds containing carbon), typically carbohydrates like sugars (mainly glucose, fructose and sucrose), starches, phytoglycogen and cellulose. When needing to use this stored energy, an organism's cells then metabolize the organic compounds through cellular respiration. Photosynthesis plays a critical role in 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.

Some organisms also perform anoxygenic photosynthesis, which does not produce oxygen. Some bacteria (e.g. purple bacteria) uses bacteriochlorophyll to split hydrogen sulfide as a reductant instead of water, releasing sulfur instead of oxygen, which was a dominant form of photosynthesis in the euxinic Canfield oceans during the Boring Billion. Archaea such as Halobacterium also perform a type of non-carbon-fixing anoxygenic photosynthesis, where the simpler photopigment retinal and its microbial rhodopsin derivatives are used to absorb green light and produce a proton (hydron) gradient across the cell membrane, and the subsequent ion movement powers transmembrane proton pumps to directly synthesize adenosine triphosphate (ATP), the "energy currency" of cells. Such archaeal photosynthesis might have been the earliest form of photosynthesis that evolved on Earth, as far back as the Paleoarchean, preceding that of cyanobacteria (see Purple Earth hypothesis).

The Boring Billion, otherwise known as the Mid Proterozoic and Earth's Middle Ages, is an informal geological time period between 1.8 and 0.8 billion years ago (Ga) during the middle Proterozoic eon spanning from the Statherian to the Tonian periods, characterized by more or less tectonic stability, climatic stasis and slow biological evolution. Although it is bordered by two different oxygenation events (the Great Oxygenation Event and Neoproterozoic Oxygenation Event) and two global glacial events (the Huronian and Cryogenian glaciations), the Boring Billion period itself actually had very low oxygen levels and no geological evidence of glaciations.

The oceans during the Boring Billion may have been oxygen-poor, nutrient-poor and sulfidic (euxinia), populated by mainly anoxygenic purple bacteria, a type of bacteriochlorophyll-based photosynthetic bacteria which uses hydrogen sulfide (H₂S) for carbon fixation instead of water and produces sulfur as a byproduct instead of oxygen. This is known as a Canfield ocean, and such composition may have caused the oceans to be colored black-and-milky-turquoise instead of blue or green as later. (By contrast, during the much earlier Purple Earth phase during the Archean, photosynthesis was performed mostly by archaeal colonies using retinal-based proton pumps that absorb green light, and the oceans would be magenta-purple.)

Microbial rhodopsins, also known as bacterial rhodopsins, are retinal-binding proteins that provide light-dependent ion transport and sensory functions in halophilic and other bacteria. They are integral membrane proteins with seven transmembrane helices, the last of which contains the attachment point (a conserved lysine) for retinal. Most microbial rhodopsins pump inwards, however "mirror rhodopsins" which function outwards have been discovered.

This protein family includes light-driven proton pumps, ion pumps and ion channels, as well as light sensors. For example, the proteins from halobacteria include bacteriorhodopsin and archaerhodopsin, which are light-driven proton pumps; halorhodopsin, a light-driven chloride pump; and sensory rhodopsin, which mediates both photoattractant (in the red) and photophobic (in the ultra-violet) responses. Proteins from other bacteria include proteorhodopsin.

The Purple Earth hypothesis (PEH) is an astrobiological hypothesis, first proposed by molecular biologist Shiladitya DasSarma in 2007, that the earliest photosynthetic life forms of Early Earth were based on the simpler molecule retinal rather than the more complex porphyrin-based chlorophyll, making the surface biosphere appear purplish rather than its current greenish color. It is estimated to have occurred between 3.5 and 2.4 billion years ago during the Archean eon, prior to the Great Oxygenation Event and Huronian glaciation.

Retinal-containing cell membranes exhibit a single light absorption peak centered in the energy-rich green-yellow region of the visible spectrum, but transmit and reflect red and blue light, resulting in a magenta color. Chlorophyll pigments, in contrast, absorb red and blue light, but little or no green light, which results in the characteristic green reflection of plants, cyanobacteria, green algae, and other organisms with chlorophyllic organelles. The simplicity of retinal pigments in comparison to the more complex chlorophyll, their association with isoprenoid lipids in the cell membrane, as well as the discovery of archaeal membrane components in ancient sediments on the Early Earth are consistent with an early appearance of life forms with purple membranes prior to the turquoise of the Canfield ocean and later green photosynthetic organisms.

Visual phototransduction is the sensory transduction process of the visual system by which light is detected by photoreceptor cells (rods and cones) in the vertebrate retina. A photon is absorbed by a retinal chromophore (each bound to an opsin), which initiates a signal cascade through several intermediate cells, then through the retinal ganglion cells (RGCs) comprising the optic nerve.

Animal opsins are G-protein-coupled receptors and a group of proteins made light-sensitive via a chromophore, typically retinal. When bound to retinal, opsins become retinylidene proteins, but are usually still called opsins regardless. Most prominently, they are found in photoreceptor cells of the retina. Five classical groups of opsins are involved in vision, mediating the conversion of a photon of light into an electrochemical signal, the first step in the visual transduction cascade. Another opsin found in the mammalian retina, melanopsin, is involved in circadian rhythms and pupillary reflex but not in vision. Humans have in total nine opsins. Beside vision and light perception, opsins may also sense temperature, sound, or chemicals.

Retinol, also called vitamin A₁, is a fat-soluble vitamin in the vitamin A family that is found in food and used as a dietary supplement. Retinol or other forms of vitamin A are needed for vision, cellular development, maintenance of skin and mucous membranes, immune function and reproductive development. Dietary sources include fish, dairy products, and meat. As a supplement it is used to treat and prevent vitamin A deficiency, especially that which results in xerophthalmia. It is taken by mouth or by injection into a muscle. As an ingredient in skin-care products, it is used to reduce wrinkles and other effects of skin aging.

Retinol at normal doses is well tolerated. High doses may cause enlargement of the liver, dry skin, and hypervitaminosis A. High doses during pregnancy may harm the fetus. The body converts retinol to retinal and retinoic acid, through which it acts.

Retinylidene proteins, or rhodopsins in a broad sense, are proteins that use retinal as a chromophore for light reception. They are the molecular basis for a variety of light-sensing systems from phototaxis in flagellates to eyesight in animals. Retinylidene proteins include all forms of opsin and rhodopsin (in the broad sense). While rhodopsin in the narrow sense refers to a dim-light visual pigment found in vertebrates, usually on rod cells, rhodopsin in the broad sense (as used here) refers to any molecule consisting of an opsin and a retinal chromophore in the ground state. When activated by light, the chromophore is isomerized, at which point the molecule as a whole is no longer rhodopsin, but a related molecule such as metarhodopsin. However, it remains a retinylidene protein. The chromophore then separates from the opsin, at which point the bare opsin is a retinylidene protein. Thus, the molecule remains a retinylidene protein throughout the phototransduction cycle.

Archaerhodopsin proteins are a family of retinal-containing photoreceptors found in the archaea genera Halobacterium and Halorubrum. Like the homologous bacteriorhodopsin (bR) protein, archaerhodopsins harvest energy from sunlight to pump H ions out of the cell, establishing a proton motive force that is used for ATP synthesis. They have some structural similarities to the mammalian G protein-coupled receptor protein rhodopsin, but are not true homologs.

Archaerhodopsins differ from bR in that the claret membrane, in which they are expressed, includes bacterioruberin, a second chromophore thought to protect against photobleaching. Also, bR lacks the omega loop structure observed at the N-terminus of the structures of several archaerhodopsins.

Halorhodopsin is a seven-transmembrane retinylidene protein from microbial rhodopsin family. It is a chloride-specific light-activated ion pump found in archaea known as halobacteria. It is activated by green light wavelengths of approximately 578 nm. Halorhodopsin also shares sequence similarity to channelrhodopsin, a light-gated ion channel.

Halorhodopsin contains the essential light-isomerizable vitamin A derivative all-trans-retinal. Due to the dedication towards discovering the structure and function of this moleculc, halorhodopsin is one of the few membrane proteins whose crystal structure is known. Halorhodopsin uses the energy of green/yellow light to move chloride ions into the cell, overcoming the membrane potential. Beside chlorides it transports other halides and nitrates into the cell. Potassium chloride uptake by cells helps to maintain osmotic balance during cell growth. By performing the same task, light-driven anion pumps can considerably reduce the use of metabolic energy. Halorhodopsin has been the subject of much study and its structure is accurately known. Its properties are similar to those of bacteriorhodopsin, and these two light-driven ion pumps transport cations and anions in opposite directions.

Proteorhodopsin (PR or pRhodopsin) belongs to the family of bacterial transmembrane rhodopsins (retinylidene proteins). In 1971, the first microbial transmembrane rhodopsin - Bacteriorhodopsin was discovered in archea domain by Dieter Oesterhelt and Walther Stoeckenius. Later in 2000, the first bacterial transmembrane rhodopsins was discovered by Oded Béjà and Edward DeLong. The Proteorhodopsin is widely expressed in various type of aquatic habitats. It functions as light-driven proton pumps with the help of retinal chromophore at the active site. The light-driven proton pump gives bacteria energy in the form of adenosine triphosphate (ATP).

Diterpenes are a class of terpenes composed of four isoprene units, often with the molecular formula C₂₀H₃₂. They are biosynthesized by plants, animals and fungi via the HMG-CoA reductase pathway, with geranylgeranyl pyrophosphate being a primary intermediate. Diterpenes form the basis for biologically important compounds such as retinol, retinal, and phytol. Some diterpenes are antimicrobial and anti-inflammatory.

Hypervitaminosis A refers to the toxic effects of ingesting too much preformed vitamin A (retinyl esters, retinol, and retinal). Symptoms arise as a result of altered bone metabolism and altered metabolism of other fat-soluble vitamins. Hypervitaminosis A is believed to have occurred in early humans, and the problem has persisted throughout human history. Toxicity results from ingesting too much preformed vitamin A from foods (such as liver), supplements, or prescription medications and can be prevented by ingesting no more than the recommended daily amount.

Diagnosis can be difficult as serum retinol is not sensitive to toxic levels of vitamin A, but there are effective tests available. Hypervitaminosis A is usually treated by stopping intake of the offending food(s), supplement(s), or medication. Most people make a full recovery. High intake of provitamin carotenoids (such as beta-carotene) from vegetables and fruits does not cause hypervitaminosis A.