Retinalophototroph
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Retinalophototroph
A retinalophototroph is one of two different types of photoautotrophs, a subcategory of phototrophs, and are named for retinal-binding proteins they utilize for cell signaling and converting light into energy. Like all photoautotrophs, retinalophototrophs absorb photons to initiate their cellular processes. However, unlike all photoautotrophs, retinalophototrophs do not use chlorophyll or an electron transport chain to power their chemical reactions. This means retinalophototrophs are incapable of traditional carbon fixation, a fundamental photosynthetic process that transforms inorganic carbon (carbon contained in molecular compounds like carbon dioxide) into organic compounds. For this reason, experts consider them to be less efficient than their photoautotrophic counterparts, chlorophototrophs. Energy conversion Retinalophototrophs achieve adequate energy conversion via a proton-motive force Chemiosmosis is the movement of ions across a semipermeable membrane bound structure, d ...
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Proton-motive Force
Chemiosmosis is the movement of ions across a semipermeable membrane bound structure, down their electrochemical gradient. An important example is the formation of adenosine triphosphate, adenosine triphosphate (ATP) by the movement of hydrogen ions (H+) across a Inner nuclear membrane, membrane during cellular respiration or photosynthesis. Hydrogen ions, or protons, will diffusion, diffuse from a region of high proton concentration to a region of lower proton concentration, and an electrochemical gradient, electrochemical concentration gradient of protons across a membrane can be harnessed to make ATP. This process is related to osmosis, the movement of water across a selective membrane, which is why it is called "chemiosmosis". ATP synthase is the enzyme that makes ATP by chemiosmosis. It allows protons to pass through the membrane and uses the Thermodynamic free energy, free energy difference to phosphorylate adenosine diphosphate (ADP), making ATP. The generation of ATP by c ...
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