Ca2+‐dependent restoration of O2‐evolving activity in CaCl2‐washed PS II particles depleted of 33, 24 and 16 kDa proteins
Authors:
- Taka-Aki OnoTOTaka-Aki Ono
- Yorinao InoueYIYorinao Inoue
- 26 March 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 168 (2) , 281-286
Abstract
CaCl2‐washing of O2‐evolving PS II particles liberated 33, 24 and 16 kDa proteins concomitant with inactivation of O2 evolution, whereas almost all Mn remained associated with membranes [FEBS Lett. 164 (1983) 252–260], and the lost O2 evolution was significantly restored when 33 kDa protein rebound to the washed membranes [FEBS Lett. 166 (1984) 381–384]. Half of the Mn atoms retained in CaCl2‐washed particles were unstably associated with the membrane, being gradually released during incubation in the absence of Ca2+, whereas in the presence of Ca2+ the release of Mn was suppressed concomitant with partial reactivation of O2 evolution. These results were interpreted as indicating that Ca2+ as well as 33 kDa protein maintains the conformation around the Mn‐binding sites as required for O2 evolution.Keywords
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