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The interaction between the 33 kDa manganese‐stabilising protein and the D 1 /D 2 cytochrome b ‐559 complex
Author(s) -
Gounaris Kleoniki,
Chapman David J.,
Barber James
Publication year - 1988
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(88)80119-4
Subject(s) - photosystem ii , chemistry , ligand (biochemistry) , cytochrome , manganese , affinity chromatography , photosynthetic reaction centre , cytochrome c , photosystem i , cytochrome b , stereochemistry , biochemistry , enzyme , receptor , photosynthesis , mitochondrion , organic chemistry , gene , mitochondrial dna
Using affinity chromatography with the extrinsic 33 kDa protein as the immobilised ligand, it was demonstrated that the reaction centre complex of photosystem II, composed of the D 1 , D 2 and cytochrome b ‐559 polypeptides, can directly interact with the 33 kDa protein. By this approach it was possible to purify the reaction centre from solubilised photosystem II core complexes since neither the 47 kDa nor the 43 kDa protein would bind to the ligand.