Ca2+‐dependent restoration of O2‐evolving activity in CaCl2‐washed PS II particles depleted of 33, 24 and 16 kDa proteins

FEBS Letters

Ono, Taka-aki¹  Inoue, Yorinao¹ 

[1] Solar Energy Research Group, The Institute of Physical and Chemical Research (RIKEN), Wako-shi, Saitama 351, Japan

关键词: O2-evolution;    CaCl2-washing;    PS II particle;    Manganese;    33 kDa protein;    Ca2+-specific restoration;    PS II;    Photosystem II;    Mes;    4-morpholineethanesulfonic acid;    SDS—PAGE;    sodium dodecyl sulfate polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(84)80263-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown