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Glycinebetaine stabilizes the association of extrinsic proteins with the photosynthetic oxygen‐evolving complex
Author(s) -
Murata N.,
Mohanty P.S.,
Hayashi H.,
Papageorgiou G.C.
Publication year - 1992
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(92)80376-r
Subject(s) - oxygen evolving complex , photosystem ii , photosynthesis , dissociation (chemistry) , chemistry , photosystem i , oxygen evolution , spinach , oxygen , biophysics , biochemistry , photochemistry , biology , organic chemistry , electrode , electrochemistry
The photosynthetic oxygen‐evolving activity of the photosystem 2 complex, prepared from spinach, was labile when the complex was exposed to high‐salt conditions under which the extrinsic proteins were dissociated from the complex. Glycinebetaine prevented the dissociation of the 18‐kDa and the 23‐kDa extrinsic proteins from the photosystem 2 complex in the presence of 1 M NaCl. It also prevented the dissociation of the 33‐kDa extrinsic protein from the complex in the presence of 1 M MgCl 2 or 1 M CaCl 2 . The oxygen‐evolving activity of the photosystem 2 complex was stabilized by glycinebetaine when the complex was subjected to treatment with NaCl and MgCl 2 .