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L protein, encoded by psbL , restores normal functioning of the primary quinone acceptor, Q A , in isolated D1/D2/CP47/Cytb‐559/I photosystem II reaction center core complex
Author(s) -
Kitamura Kohji,
Ozawa Shinichiro,
Shiina Takashi,
Toyoshima Yoshinori
Publication year - 1994
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(94)01089-7
Subject(s) - plastoquinone , thylakoid , photosystem ii , photosynthetic reaction centre , spinach , chemistry , quinone , photosynthesis , biochemistry , chloroplast , photochemistry , biophysics , biology , gene
Plastoquinone‐9(PQ‐9)‐depleted PSII reaction center core complex, consisting of CP47/D1/D2/Cytb‐55911, was isolated from spinach PSII particles. PQ‐9, lipids and several proteins were extracted from the original PSII particles and separated by several steps of chromatography to be reconstituted into the isolated complex. PQ‐9 reconstituted in the complex with the help of thylakoid lipids (digalactosyldiglyceride) did not function as Q A by itself. However, PQ‐9 simultaneously reconstituted with L protein and the thylakoid lipids successfully functioned as Q A in the complex. Other proteins of PSII origin, such as CP43, H, K, nuclear encoded 4.1 and 5.0 kDa proteins, are unable to restore the Q A activity in the complex.