A Truncated Mutant of the Extrinsic 23-kDa Protein that Absolutely Requires the Extrinsic 17-kDa Protein for Ca2+ Retention in Photosystem II | Zendy

Kentaro Ifuku | Zendy; Fumihiko Sato | Zendy

Open Access

A Truncated Mutant of the Extrinsic 23-kDa Protein that Absolutely Requires the Extrinsic 17-kDa Protein for Ca2+ Retention in Photosystem II

Author(s) -

Kentaro Ifuku,

Fumihiko Sato

Publication year - 2002

Publication title -

plant and cell physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.975

H-Index - 152

eISSN - 1471-9053

pISSN - 0032-0781

DOI - 10.1093/pcp/pcf136

Subject(s) - photosystem ii , mutant , photosystem i , photosynthesis , oxygen evolution , chemistry , biophysics , biochemistry , cofactor , photosystem , oxygen , biology , enzyme , gene , electrode , electrochemistry , organic chemistry

One function of the extrinsic 23-kDa protein in photosystem II (OEC23) is to retain Ca(2+ )and Cl(-), two essential cofactors for photosynthetic oxygen evolution. A truncated mutant of OEC23 (OEC23 Delta19) revealed that 19 residues of the N-terminus of OEC23 were necessary for Ca(2+ )retention but not for its proper interaction with OEC17, the extrinsic 17-kDa protein in photosystem II. The lost ability of OEC23 Delta19 to reconstitute the oxygen-evolving activity was partially restored by OEC17 binding, suggesting the involvement of OEC17 in Ca(2+ )retention in photosystem II.

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