Photosystem II is the photosystem that generates the two electrons that will eventually reduce NADP in ferredoxin-NADP-reductase. Photosystem II is present on the thylakoid membranes inside chloroplasts, the site of photosynthesis in green plants. The structure of Photosystem II is remarkably similar to the bacterial reaction center, and it is theorized that they share a common ancestor.
The core of Photosystem II consists of two subunits referred to as D1 and D2. These two subunits are similar to the L and M subunits present in the bacterial reaction center. Photosystem II differs from the bacterial reaction center in that it has many additional subunits that bind additional chlorophylls to increase efficiency. The overall reaction catalyzed by Photosystem II is:
:2Q + 2HO + hν → O + 2QH
Q represents the oxidized form of plastoquinone while QH represents its reduced form. This process of reducing quinone is comparable to that which takes place in the bacterial reaction center. Photosystem II obtains electrons by oxidizing water in a process called photolysis. Molecular oxygen is a byproduct of this process, and it is this reaction that supplies the atmosphere with oxygen. The fact that the oxygen from green plants originated from water was first deduced by the Canadian-born American biochemist Martin David Kamen. He used a stable isotope of oxygen, O, to trace the path of the oxygen from water to gaseous molecular oxygen. This reaction is catalyzed by a reactive center in Photosystem II containing four manganese ions.
The reaction begins with the excitation of a pair of chlorophyll molecules similar to those in the bacterial reaction center. Due to the presence of chlorophyll a, as opposed to bacteriochlorophyll, Photosystem II absorbs light at a shorter wavelength. The pair of chlorophyll molecules at the reaction center are often referred to as P680. When the photon has been absorbed, the resulting high-energy electron is transferred to a nearby pheophytin molecule. This is above and to the right of the pair on the diagram and is coloured grey. The electron travels from the pheophytin molecule through two plastoquinone molecules, the first tightly bound, the second loosely bound. The tightly bound molecule is shown above the pheophytin molecule and is colored red. The loosely bound molecule is to the left of this and is also colored red. This flow of electrons is similar to that of the bacterial reaction center. Two electrons are required to fully reduce the loosely bound plastoquinone molecule to QH as well as the uptake of two protons.
The difference between Photosystem II and the bacterial reaction center is the source of the electron that neutralizes the pair of chlorophyll a molecules. In the bacterial reaction center, the electron is obtained from a reduced compound haem group in a cytochrome subunit or from a water-soluble cytochrome-c protein.
Every time the P680 absorbs a photon, it gives off an electron to pheophytin, gaining a positive charge. After this photoinduced charge separation, P680 is a very strong oxidant of high energy. It passes its energy to water molecules that are bound at the manganese center directly below the pair and extracts an electron from them. This center, below and to the left of the pair in the diagram, contains four manganese ions, a calcium ion, a chloride ion, and a tyrosine residue. Manganese is adept at these reactions because it is capable of existing in four oxidation states: Mn, Mn, Mn and Mn. Manganese also forms strong bonds with oxygen-containing molecules such as water. The process of oxidizing two molecules of water to form an oxygen molecule requires four electrons. The water molecules that are oxidized in the manganese center are the source of the electrons that reduce the two molecules of Q to QH. To date, this water splitting catalytic center has not been reproduced by any man-made catalyst.