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Relationship between the 43 kDa chlorophyll‐protein of PS II and the rapidly metabolized 32 kDa Q B protein
Author(s) -
Machold O.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80844-4
Subject(s) - cycloheximide , chlorophyll , vicia faba , biochemistry , photosynthetic reaction centre , protein subunit , chlorophyll a , biology , thylakoid , methionine , homology (biology) , molecular mass , chemistry , protein biosynthesis , amino acid , photosynthesis , chloroplast , botany , enzyme , gene
The chlorophyll‐proteins of L‐[ 35 S]methionine‐labelled thylakoid membranes isolated from cycloheximide‐treated Vicia faba plants were electrophoretically separated and correlated to the rapidly metabolized Q B protein. Additionally, the chlorophyll a ‐protein band with the highest specific radioactivity was excised and subjected to denaturing re‐electrophoresis. Based on these experiments it is presumed that the native Q B protein is associated with pigments and represents a protein moiety of the 43 kDa chlorophyll a ‐protein (Chl a‐P3) of PS II. This is reconcilable with the hypothesis that the Q B protein carries the reaction center of PS II as deduced from its homology to the L and M subunits of the bacterial reaction center complex.