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Photoactivation of NH 2 OH‐treated leaves: reassembly of released extrinsic PS II polypeptides and religation of Mn into the polynuclear Mn catalyst of water oxidation
Author(s) -
Becker David W.,
Callahan Franklin E.,
Cheniae G.M.
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)80109-5
Subject(s) - oxidizing agent , chemistry , thylakoid , hydroxylamine , photosystem ii , photophosphorylation , catalysis , enzyme , tricine , photochemistry , inorganic chemistry , biochemistry , photosynthesis , chloroplast , organic chemistry , gene
Inactivation of the water‐oxidizing enzyme by exposure of leaf segments to hydroxylamine results in a disassembly/perturbation of photosystem (PS) II extrinsic polypeptides (17>23 kDa) and solubilization of the tetra‐Mn complex. Religation of the tetra‐Mn complex, reassembly of these PS II extrinsic polypeptides with thylakoid membranes and reappearance of active water‐oxidizing activity all require light, and all are unaffected by inhibitors of protein synthesis and photophosphorylation. The results indicate, however, that the reassembly of these PS II extrinsic polypeptides into the multimeric water oxidizing enzyme occurs more rapidly than the photoligation of Mn as the tetra‐Mn complex.