Phytoene desaturase (lycopene-forming) Phytoene desaturase (lycopene-forming) Phytoene desaturase (lycopene-forming) (CrtI, "four-step phytoene desaturase") (, "15-cis-phytoene:acceptor oxidoreductase (lycopene-forming)") are enzymes found in archaea, bacteria and fungi that are involved in carotenoid biosynthesis. They catalyze the conversion of colorless 15-"cis"-phytoene into a bright red lycopene in a biochemical pathway called the poly-trans pathway. The same process in plants and cyanobacteria utilizes four separate enzymes in a poly-cis pathway. Bacterial phytoene desaturases were shown to require FAD as a cofactor for their function. During the chemical reaction in total four additional double bonds are introduced into phytoene: In 2000 it was discovered that the gene insertion
Photosynthetic pigment other groups of bacteria use the bacteriochlorophyll pigments (similar to the chlorophylls) for photosynthesis. Unlike the cyanobacteria, these bacteria do not produce oxygen; they typically use hydrogen sulfide rather than water as the electron donor. Recently, a very different pigment has been found in some marine γ-proteobacteria: proteorhodopsin. It is similar to and probably originated from bacteriorhodopsin (see below: under Archaea). Bacterial chlorophyll b has been isolated from Rhodopseudomonas spp. but its structure is not yet known to us. Halobacteria use the pigment bacteriorhodopsin which acts directly as a proton pump when exposed to light. Photosynthetic pigment A photosynthetic pigment