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Glycerol stabilizes oxygen evolution and maintains binding of a 9 kDa polypeptide in photosystem II particles from the cyanobacterium, Phormidium laminosum
Author(s) -
Stewart Alison C.,
Siczkowski Martin,
Ljungberg Ulf
Publication year - 1985
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(85)80145-9
Subject(s) - photosystem ii , oxygen evolution , glycerol , chemistry , biochemistry , cyanobacteria , biophysics , photosynthesis , oxygen , manganese , bioorganic chemistry , cytochrome , biology , bacteria , enzyme , organic chemistry , electrode , electrochemistry , genetics
High concentrations of glycerol (⩾20% ) stabilize oxygen evolution in photosystem (PS) II particles from the thermophilic cyanobacterium, Phormidium laminosum . Treating PS II particles with lower glycerol concentrations inhibits activity and, in parallel, detaches a 9 kDa polypeptide from PS II. These results suggest that the 9 kDa polypeptide is essential for PS II activity, and that it is bound to PS II primarily by hydrophobic interactions that are strengthened in vitro by glycerol. The 9 kDa polypeptide is distinct from cytochrome b ‐559 and does not appear to be associated with manganese or with the calcium or chloride requirements for oxygen evolution.