Photosystem ii how does it work

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The reaction center responsible for transfer of electrons from the lumen to the stromal surface contains the Mn 4 Ca O 5 cluster, Y z chlorophylls , pheophytins , plastoquinones , and a non-heme iron Fe , liganded by a bicarbonate as well as by histidine ligands from both D1 and D2 subunits not shown. Light energy captured by antennal cofactors is transferred to P chlorophylls , one of which begins the transfer of electrons towards the stromal suface. These electrons are restored by electrons donated by H 2 O in the water splitting reactions discussed above.

The electron transfer pathway is illustrated beginning with the Mn 4 Ca O 5 cluster, proceeding through Y z , chlorophylls , a pheophytin , a plastoquinone , to the final electron acceptor, plastoquinone QB.

Once QB is reduced by 2 electrons, it is released by PSII and will be oxidized as it reduces cytochrome b6f see the cytb6f exhibit.

An extensive hydrogen bonded network , from the Mn 4 Ca O 5 cluster through Y z and extending though water molecules and amino acid sidechains, leads away from the reaction center towards the lumen, in a direction opposite to electron transfer toward the stromal surface. This H-bonded network as well as two others involving chloride ions that may help maintain the coordination environment of the Mn 4 Ca O 5 cluster and that lie at the network entrances, form likely pathways to carry protons to the lumen as water is split.

The latter two networks may also function as inlet channels for water. Architecture of the photosynthetic oxygen-evolving center. Science Crystal structure of oxygen-evolving photosystem II at resolution of 1. In PSII, P undergoes charge separation and the generated electrons are transferred to the quinone acceptor pheophytin and plastoquinone sequentially Grabolle and Dau, ; Johnson, Meanwhile, water molecule, the authentic electron donor, is oxidized to molecular oxygen and P is eventually reduced.

After the reaction, the electrons are ultimately transferred to the thylakoid-embedded cytochrome b 6 f, which oxidizes plastoquinols to plastoquinones and reduces plastocyanins Cramer et al.

The core complex is largely conserved from cyanobacteria to plants with nine membrane-embedded subunits, whereas the LHCI complexes are variable in subunit composition, binding pigments and sizes due to the different habitats of cyanobacteria, algae, and plants Ben-Shem et al. However, although PSI and PSII evolved from the same ancestor, belonging to the same superfamily, their structures are largely different. The structures of D1 and D2 are similar to each other, both containing five helices all tilted against the membrane planes Zouni et al.

Afterward, Loll et al. They displayed the positions of 20 protein subunits and their interactions with 77 cofactors Figure 1A. The overall structures of the supercomplex and protein subunits are similar to those previously reported Zouni et al.

Lipids have long been thought to play a role in the assembly and function of PSII, and for the first time the authors showed the lipid integrally bound to PSII.

Eleven lipids surrounding the RC form a belt to separate it from the antenna and small protein subunits, while the remaining lipids are mostly located at the monomer-monomer interface. The lipid-rich property renders PSII both structural flexibility for local mobility and convenience in subunit-subunit recognition Guskov et al.

In the study by Guskov et al. A summary of the subunit composition information, including the subunit-cofactor interactions in PSII from T. In , Broser et al. The assembly of the protein subunits, tetrapyrrole cofactors and the non-heme iron in the monomeric PSIIcc are all identical to those in the dimer structure.

The monomer-monomer interface is indicated by a black dashed line. Only the four large subunits and the intrinsic subunits of PSIIs are shown. The subunits D1 blue , D2 lime , CP43 yellow , and CP47 cyan and the other small subunits are labeled in the monomer on the left. Cofactors are shown in sticks, including Chl green , Car orange , heme light magenta and lipids red. The Mn cluster is shown in spheres.

TABLE 1. During photosynthesis, water oxidation happens in the oxygen-evolving complex OEC , which comprises the Mn 4 CaO 5 cluster as the catalytic center. Water splitting is a process fulfilled in five consecutive stages named S 0 to S 4. It has been a model system for synthesizing catalysts for inorganic water oxidation and dioxygen evolution Kanady and Agapie, ; Mukherjee et al. In the work of Ferreira et al. However, neither water nor hydroxide could be observed to find the water oxidation site accurately in their study.

Then a 1. Subsequently, a simultaneous femtosecond X-ray spectroscopy and diffraction of the PSII system showed that the electron density maps of the dark and illuminated states are similar with an overall correlation coefficient CC of 0.

However, with a serial time-resolved crystallography, the authors acquired PSII structures in the dark S 1 and putative S 3 states, in which they found that the distance between the Mn 3 O x Ca cubane and the distant protruding Mn dangler Mn increased in the putative S 3 state, allowing the binding of the second water molecule during the S 2 to S 3 state transition Kupitz et al.

In addition, the position of O5 is also unusual. The results showed that it functions more as a hydroxide ion instead of a normal oxygen dianion to serve as one of the substrate oxygen atoms Suga et al.

Furthermore, it was reported that the chloride ion is essential for oxygen evolution, and there are two anion binding sites positioned on the two sides of the MnCa cluster with the same distance from the cluster to stabilize its structure Kawakami et al.

Compared to the structure of the spinach C 2 S 2 -type supercomplex, the structure reported by Su et al. The plant PSII indeed exhibits the same composition and organizations of the subunits and cofactors as their cyanobacterial counterparts Table 1. Specifically, D1 and D2 form the photochemical RC, which is responsible for the charge separation and electron transfer, and CP47 and CP43 act as internal antenna proteins involved in light harvesting and energy transportation from peripheral antenna to the RC.

In the core complex, there are also 12 low molecular-mass MM membrane-spanning subunits surrounding the reaction center, forming a belt-like structure. Most of these subunits are structurally conserved with a single transmembrane helix except PsbZ with two helices.

These subunits are essential for both the dimerization and stabilization of the core complex and the association between the core complex and the peripheral antenna complex. In addition, they bind cytochrome b to protect the PSII complex from photo-damage. Among them, PsbO stabilizes the Mn complex while PsbP and PsbQ are involved in optimizing the oxygen evolution at physical concentration of calcium and chloride ions.

Structure comparison also revealed that the flexible regions of these subunits experience significant conformational changes when they bind to the core complex Wei et al. Each polypeptide spans the thylakoid membrane three times with its C terminus positioned on the luminal side Kuhlbrandt et al. For the second function, the stromal surface of the LHCII trimer is negatively charged whereas its N-terminal first 15 residues contain 4 positively charged residues.

It has been reported that constitutively expression of Lhcb1 robustly increased grana stacks in the transgenic tobacco plants Labate et al. This study provided new insights into how adjacent thylakoids might be linked to mediate the stacking of grana membranes by interactions between pairs of PSII-LHCII supercomplexes.

Similar to those in cyanobacteria, these cofactors mainly include chlorophylls, carotenoids, lipids etc. Table 1. Interestingly, the LHCII monomer shows both amino acid sequence and structure similarities to those of CP29, however, the type, quantity and location of the chlorophylls they bind are significantly different Liu et al. Photosynthesis plays very important roles in molecular oxygen production, atmospheric carbon dioxide control and global food supply.

Structural information of the photosystems is invaluable for our understanding of photosynthesis, probably the most important process on earth. The information will also help design artificial photosynthetic system for the improvement of bioenergy production and the enhancement of agricultural productivity. Most recently, the structure of the largest light-harvesting complex, the phycobilisome PBS from Griffithsia pacifica was also reported Zhang et al.

As the main light-harvesting antenna in cyanobacteria and red algae, it exhibits a very fast energy transfer rate with a high quantum yield Glazer, The structural information of the PBS will provide a firm basis for understanding its energy transfer pathways and further applications in the designs of artificial light-harvesting machineries.

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