Structure-function studies on the interaction of PsaC with the Photosystem 1 heterodimer : The site directed change R561E in PsaB destabilizes the subunit interaction in Synechocystis sp. PCC 6803.

Abstract:

:The interaction of PsaC with the core heterodimer of Photosystem 1 was studied in wild type Synechocystis sp. PCC 6803 and the site-directed mutant R561E of PsaB. The mutant reaction center was much less stable in urea and the functional reconstitution of the mutant core using PsaC was impaired. However, the extent of reconstitution increased in the presence of divalent cations whereas that of the wild type was inhibited. We conclude that the reaction center in the mutant is unstable, most likely due to the introduction of an unfavorable electrostatic interaction between surface-exposed residues on PsaC and the binding site for the subunit on the core heterodimer in support of the model proposed previously (Rodday et al. (1993) Photosynth Res 36: 1-9).

journal_name

Photosynth Res

journal_title

Photosynthesis research

authors

Rodday SM,Schulz R,McLntosh L,Biggins J

doi

10.1007/BF00018261

subject

Has Abstract

pub_date

1994-12-01 00:00:00

pages

185-90

issue

3

eissn

0166-8595

issn

1573-5079

journal_volume

42

pub_type

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