Role of acidic amino acid residues of PsaD subunit on limiting the affinity of photosystem I for ferredoxin

被引:20
作者
Bottin, H [1 ]
Hanley, J
Lagoutte, B
机构
[1] CEA, Dept Biol Cellulaire & Mol, Serv Bioenerget, F-91191 Gif Sur Yvette, France
[2] Ctr Etud Saclay, CNRS, URA 2096, F-91191 Gif Sur Yvette, France
关键词
cyanobacterium; Synechocystis sp PCC 6803; electron transfer; photosystem; 1; PsaD subunit; ferredoxin;
D O I
10.1006/bbrc.2001.5658
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The PsaD subunit of photosystem I is one of the central polypeptides for the interaction with ferredoxin, its acidic electron acceptor. In the cyanobacterium Synechocystis 6803, this role is partly performed by a sequence extending approximately from histidine 97 to arginine 119, close to the C-terminus. In the present work, acidic amino acids D100, E105, and E109 are shown to moderate the affinity of Photosystem I for ferredoxin. Most single replacements of these residues by neutral amino acids increased the affinity for ferredoxin, resulting in a dissociation constant as low as 0.015 muM for the E105Q mutant (wild-type K-D = 04 muM). This is the first report on the limitation of photosystem I affinity for ferredoxin due to acidic amino acids from PsaD subunit. It highlights the occurrence of a negative control on the binding during the formation of transient complexes between electron carriers. (C) 2001 Academic Press.
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页码:833 / 836
页数:4
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