The N-terminal sequence of the extrinsic PsbP protein modulates the redox potential of Cyt b559 in photosystem II

• Nishimura, Taishi

• 佐藤, 文彦

• Noguchi, Takumi

• Nield, Jon

• Sato, Fumihiko

• Ifuku, Kentaro

抄録

The PsbP protein, an extrinsic subunit of photosystem II (PSII) in green plants, is known to induce a conformational change around the catalytic Mn[4]CaO[5] cluster securing the binding of Ca[2+] and Cl[-] in PSII. PsbP has multiple interactions with the membrane subunits of PSII, but how these affect the structure and function of PSII requires clarification. Here, we focus on the interactions between the N-terminal residues of PsbP and the α subunit of Cytochrome (Cyt) b[559] (PsbE). A key observation was that a peptide fragment formed of the first N-terminal 15 residues of PsbP, 'pN15', was able to convert Cyt b[559] into its HP form. Interestingly, addition of pN15 to NaCl-washed PSII membranes decreased PSII's oxygen-evolving activity, even in the presence of saturating Ca[2+] and Cl[-] ions. In fact, pN15 reversibly inhibited the S[1] to S[2] transition of the OEC in PSII. These data suggest that pN15 can modulate the redox property of Cyt b[559] involved in the side-electron pathway in PSII. This potential change of Cyt b[559], in the absence of the C-terminal domain of PsbP, however, would interfere with any electron donation from the Mn[4]CaO[5] cluster, leading to the possibility that multiple interactions of PsbP, binding to PSII, have distinct roles in regulating electron transfer within PSII.

収録刊行物

• Scientific Reports

  Scientific Reports 6 21490-, 2016-02-18

  Nature Publishing Group

キーワード

• Multidisciplinary

詳細情報

• CRID: 1050564285789086976
• NII論文ID: 120005818272
• ISSN: 20452322
• DOI: 10.1038/srep21490
• HANDLE: 2433/216010
• Web Site: https://www.nature.com/articles/srep21490
• Web Site: https://www.nature.com/articles/srep21490.pdf
• 本文言語コード: en
• 資料種別: journal article
• データソース種別:
  • IRDB
  • Crossref
  • CiNii Articles
  • KAKEN