Photosystem I(PSI) in higher plants consists of 17 polypeptide subunit
s. Cofactors are chlorophyll a and b, beta-carotene, phylloquinone and
iron-sulfur clusters. Eight subunits are specific for higher plants w
hile the remaining ones are also present in cyanobacteria, Two 80-kDa
subunits (PSI-A and -B) constitute the major part of PSI and bind most
of the pigments and electron donors and accepters. The 9-kDa PSI-C ca
rries the remaining electron accepters which are [4Fe-4S] iron sulfur
clusters. PSI-D, -E and -H have importance for integrity and function
at the stromal face of PSI while PSI-F has importance for function at
the lumenal face. PSI-N is localized at the lumenal side, but its func
tion is unknown. Four subunits are light-harvesting chlorophyll alb-bi
nding proteins. The remaining subunits are integral membrane proteins
with poorly understood function. Subunit interactions have been studie
d in reconstitution experiments and by cross-linking studies. Based on
these data, it is concluded that iron-sulfur cluster F-B is proximal
to F-X and that F-A is the terminal acceptor in PSI. Similarities betw
een PSI and the reaction center from green sulfur bacteria are discuss
ed.