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Specific 125 I labeling of D1 (herbicide‐binding protein)
Author(s) -
Ikeuchi M.,
Inoue Y.
Publication year - 1987
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(87)81300-5
Subject(s) - spinach , chemistry , atrazine , thylakoid , photosynthetic reaction centre , photosystem ii , photoaffinity labeling , binding site , synechococcus , cyanobacteria , thermophile , stereochemistry , biochemistry , electron transfer , chloroplast , photochemistry , enzyme , photosynthesis , biology , bacteria , genetics , pesticide , gene , agronomy
When 125 I − was given as an artificial electron donor to non‐O 2 ‐evolving thylakoids of spinach, a 29 kDa polypeptide was specifically tagged by 125 I due to its photooxidation by PS II [(1985) Plant Cell Physiol. 26, 1093–1100]. We examined precisely the 125 I‐labeling pattern in comparison with azido[ 14 C]atrazine photoaffinity labeling of D1 and immunoblotting with anti‐D1 and anti‐D2, and found that D1 (herbicidebinding protein) of PS II reaction center complex is specifically tagged by 125 I in three different species of higher plants (spinach, pea and wheat) and a thermophilic cyanobacterium ( Synechococcus vulcanus ). It was suggested that D1 bears the photooxidation site or has a domain very close to the photooxidation site on the donor side of PS II, in addition to the well established binding site for Q b and herbicides on the acceptor side of PS II.