Rhodopsin in the context of "Vitamin A"

Halobacterium (common abbreviation Hbt.), from Ancient Greek ἅλς (háls), meaning "salt", and "bacterium", is a genus in the family Halobacteriaceae.

The genus Halobacterium ("salt" or "ocean bacterium") consists of several species of Archaea with an aerobic metabolism which requires an environment with a high concentration of salt; many of their proteins will not function in low-salt environments. They grow on amino acids in their aerobic conditions. Their cell walls are also quite different from those of bacteria, as ordinary lipoprotein membranes fail in high salt concentrations. In shape, they may be either rods or cocci, and in color, either red or purple. They reproduce via binary fission (constriction), and are motile. Halobacterium grows best in a 42 °C environment. The genome of an unspecified Halobacterium species, sequenced by Shiladitya DasSarma, comprises 2,571,010 bp (base pairs) of DNA compiled into three circular strands: one large chromosome with 2,014,239 bp, and two smaller ones with 191,346 and 365,425 bp. This species, called Halobacterium sp. NRC-1, has been extensively used for postgenomic analysis. Halobacterium species can be found in the Great Salt Lake, the Dead Sea, Lake Magadi, and any other waters with high salt concentration. Purple Halobacterium species owe their color to bacteriorhodopsin, a light-sensitive membrane protein which acts as a proton pump, providing chemical energy with the proton gradient for the cell using light energy. The resulting proton gradient across the cell membrane is used to drive ATP synthase to generate adenosine triphosphate (ATP). Bacteriorhodopsin is very similar to rhodopsin, light-sensitive receptor proteins found in the retina of most animals.

Photoreceptor proteins are light-sensitive proteins involved in the sensing and response to light in a variety of organisms. Some examples are rhodopsin in the photoreceptor cells of the vertebrate retina, phytochrome in plants, and bacteriorhodopsin and bacteriophytochromes in some bacteria. They mediate light responses as varied as visual perception, phototropism and phototaxis, as well as responses to light-dark cycles such as circadian rhythm and other photoperiodisms including control of flowering times in plants and mating seasons in animals.

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.

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).

G protein-coupled receptors (GPCRs), also known as seven-(pass)-transmembrane domain receptors, 7TM receptors, heptahelical receptors, serpentine receptors, and G protein-linked receptors (GPLR), form a large group of evolutionarily related proteins that are cell surface receptors that detect molecules outside the cell and activate cellular responses. They are coupled with G proteins. They pass through the cell membrane seven times in the form of six loops (three extracellular loops interacting with ligand molecules, three intracellular loops interacting with G proteins, an N-terminal extracellular region and a C-terminal intracellular region) of amino acid residues, which is why they are sometimes referred to as seven-transmembrane receptors. Ligands can bind either to the extracellular N-terminus and loops (e.g. glutamate receptors) or to the binding site within transmembrane helices (rhodopsin-like family). They are all activated by agonists, although a spontaneous auto-activation of an empty receptor has also been observed.

G protein-coupled receptors are found only in eukaryotes, including yeast, and choanoflagellates. The ligands that bind and activate these receptors include light-sensitive compounds, odors, pheromones, hormones, and neurotransmitters. They vary in size from small molecules to peptides, to large proteins. G protein-coupled receptors are involved in many diseases.