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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 ]
X-ray crystal structure of the Mn 4 O 5 Ca core of the oxygen evolving complex of Photosystem II at a resolution of 1.9 Å. [2] The oxygen-evolving complex (OEC), also known as the water-splitting complex, is a water-oxidizing enzyme involved in the photo-oxidation of water during the light reactions of photosynthesis. [3]
Electron micrograph of a 2D crystal of the LH1-Reaction center photosynthetic unit. A photosynthetic reaction center is a complex of several proteins, biological pigments, and other co-factors that together execute the primary energy conversion reactions of photosynthesis.
In oxygenic photosynthesis, the first electron donor is water, creating oxygen (O 2) as a by-product. In anoxygenic photosynthesis , various electron donors are used. Cytochrome b 6 f and ATP synthase work together to produce ATP ( photophosphorylation ) in two distinct ways.
Oxygenic photosynthesis can be performed by plants and cyanobacteria; cyanobacteria are believed to be the progenitors of the photosystem-containing chloroplasts of eukaryotes. Photosynthetic bacteria that cannot produce oxygen have only one photosystem, which is similar to either PSI or PSII .
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 photosynthetic efficiency (i.e. oxygenic photosynthesis efficiency) is the fraction of light energy converted into chemical energy during photosynthesis in green plants and algae. Photosynthesis can be described by the simplified chemical reaction 6 H 2 O + 6 CO 2 + energy → C 6 H 12 O 6 + 6 O 2
However, PSII has an additional function over the bacterial system. At the oxidising side of PSII, a redox-active residue in the D1 protein reduces P680, the oxidised tyrosine then withdrawing electrons from a manganese cluster, which in turn withdraw electrons from water, leading to the splitting of water and the formation of molecular oxygen.
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