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Second protein complex in photosynthetic light reactions

Photosystem I (PSI, or plastocyanin–ferredoxin oxidoreductase) is one of two photosystems in the photosynthetic light reactions of algae, plants, and cyanobacteria. Photosystem I 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. The photon energy absorbed by Photosystem I also produces a proton motive force that is used to generate ATP. PSI is composed of more than 110 cofactors, significantly more than Photosystem II.

This photosystem is known as PSI because it was discovered before Photosystem II, although future experiments showed that Photosystem II is actually the first enzyme of the photosynthetic electron transport chain. Aspects of PSI were discovered in the 1950s, but the significance of these discoveries was not yet recognized at the time. Louis Duysens first proposed the concepts of Photosystems I and II in 1960, and, in the same year, a proposal by Fay Bendall and Robert Hill assembled earlier discoveries into a coherent theory of serial photosynthetic reactions. downstream of the cysteines and could contribute to dimerisation of PsaA/PsaB. The terminal electron acceptors F and F, also [4Fe 4S] iron sulfur clusters, are located in a 9 kDa protein called PsaC that binds to the PsaA/PsaB core near F.

+ Components of PSI (protein subunits, lipids, pigments, coenzymes, and cofactors). Protein subunits Description PsaA Related large transmembrane proteins involved in the binding of P700, A0, A1, and Fx. Part of the photosynthetic reaction centre protein family. PsaBPsaCIron sulfur center; apoprotein for Fa and FbPsaDRequired for assembly, helps bind ferredoxin. PsaEPsaIMay stabilize PsaL. Stabilizes light harvesting complex II binding. PsaJ PsaK PsaLPsaMPsaXcytochrome b6f complexSoluble proteinFaFrom PsaC; In electron transport chain (ETC) FbFrom PsaC; In ETCFxFrom PsaAB; In ETCFerredoxinElectron carrier in ETCPlastocyaninSoluble protein Lipids DescriptionMGDG IIMonogalactosyldiglyceride lipidPG IPhosphatidylglycerol phospholipidPG IIIPhosphatidylglycerol phospholipidPG IVPhosphatidylglycerol phospholipid Pigments DescriptionChlorophyll a90 pigment molecules in antenna systemChlorophyll a5 pigment molecules in ETCChlorophyll a0Early electron acceptor of modified chlorophyll in ETCChlorophyll a′1 pigment molecule in ETCβ Carotene22 carotenoid pigment molecules Coenzymes and cofactors DescriptionQK AEarly electron acceptor vitamin K1 phylloquinone in ETCQK BEarly electron acceptor vitamin K1 phylloquinone in ETCFNRFerredoxin oxidoreductase enzymeCalcium ionMagnesium ion

Photoexcitation of the pigment molecules in the antenna complex induces electron and energy transfer. These pigment molecules transmit the resonance energy from photons when they become photoexcited. Antenna molecules can absorb all wavelengths of light within the visible spectrum. The number of these pigment molecules varies from organism to organism. For instance, the cyanobacterium Synechococcus elongatus (Thermosynechococcus elongatus) has about 100 chlorophylls and 20 carotenoids, whereas spinach chloroplasts have around 200 chlorophylls and 50 carotenoids.

The P700 reaction center is composed of modified chlorophyll a that best absorbs light at a wavelength of 700 nm. P700 receives energy from antenna molecules and uses the energy from each photon to raise an electron to a higher energy level (P700*). These electrons are moved in pairs in an oxidation/reduction process from P700* to electron acceptors, leaving behind P700. The pair of P700* P700 has an electric potential of about −1.2 volts. The reaction center is made of two chlorophyll molecules and is therefore referred to as a dimer.

A phylloquinone, sometimes called vitamin K, is the next early electron acceptor in PSI. It oxidizes A in order to receive the electron and in turn is re oxidized by F, from which the electron is passed to F and F. The reduction of Fx appears to be the rate limiting step. In one model, F passes an electron to F, which passes it on to F to reach the ferredoxin. Fd moves to carry an electron either to a lone thylakoid or to an enzyme that reduces FNR may also accept an electron from NADPH by binding to it.

The Ycf4 protein domain found on the thylakoid membrane is vital to photosystem I. This thylakoid transmembrane protein helps assemble the components of photosystem I. Without it, photosynthesis would be inefficient.

Molecular data show that PSI likely evolved from the photosystems of green sulfur bacteria. The photosystems of green sulfur bacteria and those of cyanobacteria, algae, and higher plants are not the same, but there are many analogous functions and similar structures. Three main features are similar between the different photosystems. First, redox potential is negative enough to reduce ferredoxin. Next, the electron accepting reaction centers include iron–sulfur proteins. Last, redox centres in complexes of both photosystems are constructed upon a protein subunit dimer. The photosystem of green sulfur bacteria even contains all of the same cofactors of the electron transport chain in PSI. The number and degree of similarities between the two photosystems strongly indicates that PSI and the analogous photosystem of green sulfur bacteria evolved from a common ancestral photosystem.