Analysis of the proposed Fe-SX binding region of Photosystem 1 by site directed mutation of PsaA in Chlamydomonas reinhardtii.

Abstract:

:The psaA and psaB genes of the chloroplast genome in oxygenic photosynthetic organisms code for the major peptides of the Photosystem 1 reaction center. A heterodimer of the two polypeptides PsaA and PsaB is thought to bind the reaction center chlorophyll, P700, and the early electron acceptors A0, A1 and Fe-SX. Fe-SX is a 4Fe4S center requiring 4 cysteine residues as ligands from the protein. As PsaA and PsaB have only three and two conserved cysteine residues respectively, it has been proposed by several groups that Fe-SX is an unusual inter-peptide center liganded by two cysteines from each peptide. This hypothesis has been tested by site directed mutagenesis of PsaA residue C575 and the adjacent D576. The C575D mutant does not assemble Photosystem 1. The C575H mutant contains a photoxidisable chlorophyll with EPR properties of P700, but no other Photosystem 1 function has been detected. The D576L mutant assembles a modified Photosystem 1 in which the EPR properties of the Fe-SA/B centers are altered. The results confirm the importance of the conserved cysteine motif region in Photosystem 1 structure.

journal_name

Photosynth Res

journal_title

Photosynthesis research

authors

Hallahan BJ,Purton S,Ivison A,Wright D,Evans MC

doi

10.1007/BF00020438

subject

Has Abstract

pub_date

1995-11-01 00:00:00

pages

257-64

issue

1-2

eissn

0166-8595

issn

1573-5079

journal_volume

46

pub_type

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