H. Bottin et al., Role of acidic amino acid residues of PsaD subunit on limiting the affinity of photosystem I for ferredoxin, BIOC BIOP R, 287(4), 2001, pp. 833-836
Citations number
23
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
The PsaD subunit of photosystem I is one of the central polypeptides for th
e interaction with ferredoxin, its acidic electron acceptor. In the cyanoba
cterium Synechocystis 6803, this role is partly performed by a sequence ext
ending approximately from histidine 97 to arginine 119, close to the C-term
inus. In the present work, acidic amino acids D100, E105, and E109 are show
n to moderate the affinity of Photosystem I for ferredoxin. Most single rep
lacements of these residues by neutral amino acids increased the affinity f
or 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 ac
ids from PsaD subunit. It highlights the occurrence of a negative control o
n the binding during the formation of transient complexes between electron
carriers. (C) 2001 Academic Press.