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Photosystem II (or water-plastoquinone oxidoreductase) is the first protein complex in the energy-dependent reactions of oxygenic photosynthesis. It is located in the thylakoid membrane of plants , algae , and cyanobacteria .
The energy of absorbed light (in the form of delocalized, high-energy electrons) is funneled into the reaction center, where it excites special chlorophyll molecules (P700, with maximum light absorption at 700 nm) to a higher energy level. The process occurs with astonishingly high efficiency.
The role that plastoquinone plays in photosynthesis, more specifically in the light-dependent reactions of photosynthesis, is that of a mobile electron carrier through the membrane of the thylakoid. [2] Plastoquinone is reduced when it accepts two electrons from photosystem II and two hydrogen cations (H +) from the stroma of the chloroplast ...
The thylakoid membranes of higher plants are composed primarily of phospholipids [5] and galactolipids that are asymmetrically arranged along and across the membranes. [6] Thylakoid membranes are richer in galactolipids rather than phospholipids; also they predominantly consist of hexagonal phase II forming monogalacotosyl diglyceride lipid.
The electrons then pass through Cyt b 6 and Cyt f to plastocyanin, using energy from photosystem I to pump hydrogen ions (H +) into the thylakoid space. This creates a H + gradient, making H + ions flow back into the stroma of the chloroplast, providing the energy for the (re)generation of ATP.
This funneling of energy is performed via resonance transfer, which occurs when energy from an excited molecule is transferred to a molecule in the ground state. This ground state molecule will be excited, and the process will continue between molecules all the way to the reaction center.
Photosystem I [1] 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. [2]
The cytochrome b 6 f complex is a dimer, with each monomer composed of eight subunits. [3] These consist of four large subunits: a 32 kDa cytochrome f with a c-type cytochrome, a 25 kDa cytochrome b 6 with a low- and high-potential heme group, a 19 kDa Rieske iron-sulfur protein containing a [2Fe-2S] cluster, and a 17 kDa subunit IV; along with four small subunits (3-4 kDa): PetG, PetL, PetM ...