Abstract
We have studied the binding sites of the electron donor and acceptor proteins of vascular plant photosystem I by electron microscopy/crystallography. Previously, we identified the binding site for the electron acceptor (ferredoxin). In this paper we complete these studies with the characterization of the electron donor (plastocyanin) binding site. After cross-linking, plastocyanin is detected using Fourier difference analysis of two dimensionally ordered arrays of photosystem I located at the periphery of chloroplast grana. Plastocyanin binds in a small cavity on the lumenal surface of photosystem I, close to the center and with a slight bias toward the PsaL subunit of the complex. The recent release of the full coordinates for the cyanobacterial photosystem I reaction center has allowed a detailed comparison between the structures of the eukaryotic and prokaryotic systems. This reveals a very close homology, which is particularly striking for the lumenal side of photosystem I.
Original language | English |
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Pages (from-to) | 25692-25696 |
Number of pages | 4 |
Journal | Journal of Biological Chemistry |
Volume | 277 |
Issue number | 28 |
DOIs | |
Publication status | Published - 12 Jul 2002 |
Keywords
- CHEMICAL CROSS-LINKING; FLASH ABSORPTION-SPECTROSCOPY; SITE-DIRECTED
- MUTAGENESIS; SYNECHOCYSTIS SP PCC-6803; PSI-H SUBUNIT; 3-DIMENSIONAL
- STRUCTURE; ANGSTROM RESOLUTION; ELECTRON-TRANSFER;
- SYNECHOCOCCUS-ELONGATUS; CYTOCHROME C(6)