Abstract
Fd is a 2Fe-2S protein, which is the final electron acceptor of the photosynthetic electron transport chain and the only soluble electron transport protein in the chloroplast stroma. Following photoreduction, Fd donates electrons to many plastid enzymes essential for cellular processes, including carbon assimilation, nitrogen assimilation, sulphur assimilation, amino acid synthesis, fatty acid synthesis, haem synthesis and redox regulation. The purpose of our work is to identify all proteins involved in Fd electron donation within the chloroplast proteome, including novel interactions. Using a column comprising recombinant Arabidopsis Fd, we have developed a technique to rapidly isolate soluble proteins that interact with Fd from Arabidopsis leaves. Exploiting the abundant genomic information for Arabidopsis, these proteins were identified by MALDI-TOF mass spectrometry.
