Photosystem I (PSI, or plastocyanin-ferredoxin oxidoreductase) is the second photosystem in the photosynthetic light reactions of algae, plants, and some bacteria. Photosystem I  is an integral membrane protein complex that uses light energy to produce the high energy carriers ATP and NADPH. PSI comprises more than 110 cofactors, significantly more than photosystem II.
Plant photosystem I, PDB 2001
|PDB structures||RCSB PDB PDBe PDBsum|
This photosystem is known as PSI because it was discovered before photosystem II. Aspects of PSI were discovered in the 1950s, but the significances of these discoveries was not yet known. 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 cohesive theory of serial photosynthetic reactions. Hill and Bendall's hypothesis was later justified in experiments conducted in 1961 by Duysens and Witt groups.
Components and actionEdit
Two main subunits of PSI, PsaA and PsaB, are closely related proteins involved in the binding of P700, A0, A1, and Fx. PsaA and PsaB are both integral membrane proteins of 730 to 750 amino acids that seem to contain 11 transmembrane segments. The Fx 4Fe-4S iron-sulfur center is coordinated by four cysteines; two of these cysteines are provided by the PsaA protein and the two others by PsaB. The two cysteines in both proteins are proximal and located in a loop between the ninth and tenth transmembrane segments. A leucine zipper motif seems to be present  downstream of the cysteines and could contribute to dimerisation of psaA/psaB. The terminal electron acceptors, FA and FB, are located in a 9 kDa protein called PsaC.
|PsaA||Related large transmembrane proteins involved in the binding of P700, A0, A1, and Fx. Structually related to the photosynthetic reaction centre protein family.|
|PsaC||Iron-sulfur center; apoprotein for Fa and Fb|
|Cytochrome b6f complex||Soluble protein|
|Fa||In electron transport chain (ETC)|
|Ferredoxin||Electron carrier in ETC|
|MGDG II||Monogalactosyldiglyceride lipid|
|PG I||Phosphatidylglycerol phospholipid|
|PG III||Phosphatidylglycerol phospholipid|
|PG IV||Phosphatidylglycerol phospholipid|
|Chlorophyll a||90 pigment molecules in antenna system|
|Chlorophyll a||5 pigment molecules in ETC|
|Chlorophyll a0||Early electron acceptor of modified chlorophyll in ETC|
|Chlorophyll a′||1 pigment molecule in ETC|
|β-Carotene||22 carotenoid pigment molecules|
|Coenzymes and cofactors||Description|
|QK-A||Early electron acceptor vitamin K1 phylloquinone in ETC|
|QK-B||Early electron acceptor vitamin K1 phylloquinone in ETC|
The antenna complex is composed of molecules of chlorophyll and carotenoids mounted on two proteins. 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. Located within the antenna complex of PSI are molecules of chlorophyll called P700 reaction centers. The energy passed around by antenna molecules is directed to the reaction center. There may be as many as 120 or as few as 25 chlorophyll molecules per P700.
P700 reaction centerEdit
The P700 reaction center is composed of modified chlorophyll a that best absorbs light at a wavelength of 700 nm, with higher wavelengths causing bleaching. P700 receives energy from antenna molecules and uses the energy from each photon to raise an electron to a higher energy level. These electrons are moved in pairs in an oxidation/reduction process from P700 to electron acceptors. 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. The dimer is thought to be composed of one chlorophyll a molecule and one chlorophyll a′ molecule (P700, webber). However, if P700 forms a complex with other antenna molecules, it can no longer be a dimer.
Modified chlorophyll a0Edit
Modified chlorophyll a0 is an early electron acceptor in PSI. Chlorophyll a0 accepts electrons from P700 before passing them along to another early electron acceptor.
Phylloquinone A1 is the next early electron acceptor in PSI. Phylloquinone is also sometimes called vitamin K1. Phylloquinone A1 oxidizes a0 in order to receive the electron and in turn reduces Fx in order to pass the electron to Fb and Fa.
Three proteinaceous iron–sulfur reaction centers are found in PSI. Labeled Fx, Fa, and Fb, they serve as electron relays. Fa and Fb are bound to protein subunits of the PSI complex and Fx is tied to the PSI complex. Various experiments have shown some disparity between theories of iron–sulfur cofactor orientation and operation order.
Ferredoxin (Fd) is a soluble protein that facilitates reduction of NADP+
to NADPH. Fd moves to carry an electron either to a lone thylakoid or to an enzyme that reduces NADP+
. Thylakoid membranes have one binding site for each function of Fd. The main function of Fd is to carry an electron from the iron-sulfur complex to the enzyme ferredoxin–NADP+
Ycf4 protein domainEdit
The Ycf4 protein domain is found on the thylakoid membrane and 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, however 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 is derived from the analogous photosystem of green sulfur bacteria.
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