Control of electron transport in photosystem I by the iron-sulfur cluster Fx in response to intra- and intersubunit interactions

Xiao Min Gong, Rufat Agalarov, Klaus Brettel, Chanoch Carmeli*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Photosystem I (PS I) is a transmembraneal multisub-unit complex that mediates light-induced electron transfer from plactocyanine to ferredoxin. The electron transfer proceeds from an excited chlorophyll a dimer (P700) through a chlorophyll a (A0), a phylloquinone (A1), and a [4Fe-4S] iron-sulfur cluster Fx, all located on the core subunits PsaA and PsaB, to iron-sulfur clusters FA and FB, located on subunit PsaC. Earlier, it was attempted to determine the function of Fx in the absence of FA/B mainly by chemical dissociation of subunit PsaC. However, not all PsaC subunits could be removed from the PS I preparations by this procedure without partially damaging Fx. We therefore removed subunit PsaC by interruption of the psaC2 gene of PS I in the cyanobacterium Synechocystis sp. PCC 6803. Cells could not grow under photosynthetic conditions when subunit PsaC was deleted, yet the PsaC-deficient mutant cells grew under heterotrophic conditions and assembled the core subunits of PS I in which light-induced electron transfer from P700 to A1 occurred. The photoreduction of Fx was largely inhibited, as seen from direct measurement of the extent of electron transfer from A1 to Fx. From the crystal structure it can be seen that the removal of subunits PsaC, PsaD, and PsaE in the PsaC-deficient mutant resulted in the braking of salt bridges between these subunits and PsaB and PsaA and the formation of a net of two negative surface charges on PsaA/B. The potential induced on Fx by these surface charges is proposed to inhibit electron transport from the quinone. In the complete PS I complex, replacement of a cysteine ligand of Fx by serine in site-directed mutation C565S/D566E in subunit PsaB caused an ∼10-fold slow down of electron transfer from the quinone to Fx without much affecting the extent of this electron transfer compared with wild type. Based on these and other results, we propose that Fx might have a major role in controlling electron transfer through PS I.

Original languageEnglish
Pages (from-to)19141-19150
Number of pages10
JournalJournal of Biological Chemistry
Issue number21
StatePublished - 23 May 2003


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