Surface-charge related actions of polylysine on thylakoid membranes.

Abstract:

:Polycation binding to the negatively charged surface of chloroplast thylakoid membranes is known to cause an inhibition of photosystem I activity. It also interferes with the cation-dependent rearrangement of chlorophyll proteins in the thylakoid membrane. It was shown that added anions prevented or reversed the inhibition of photosystem I by polylysine without decreasing its binding to the membranes. Anions also caused a change in the interaction of the chlorophyll proteins in polylysine-treated thylakoids as indicated by an increase in the relative fluorescence intensity from photosystem II. In both cases, the relative effectiveness of the anions tested depended on their valence; for example, the tetravalent species Fe(CN)4-(6) was effective at concentration at least 2 orders of magnitude lower than the divalent species SO2-(4). These results suggest that anions act by screening the positive charge of the polylysine-coated membrane surface. Measurements of the response of the anionic fluorescent probe 1-anilinonapthalene-8-sulfonate to an addition of anions to polylysine-treated thylakoids supported this contention. It was concluded that the action of polylysine on photosystem I and on the chlorophyll proteins is mediated by changes of the electrical properties of the thylakoid membrane and may not involve a direct binding of the polycation to the affected membrane proteins.

journal_name

Arch Biochem Biophys

authors

Richter ML,Homann PH

doi

10.1016/0003-9861(83)90503-9

subject

Has Abstract

pub_date

1983-04-01 00:00:00

pages

67-77

issue

1

eissn

0003-9861

issn

1096-0384

pii

0003-9861(83)90503-9

journal_volume

222

pub_type

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