Formation of the S2 state and structure of the Mn complex in photosystem II lacking the extrinsic 33 kilodalton polypeptide

Anne Frances Miller, Julio C. de Paula, Gary W Brudvig

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

Electron paramagnetic resonance (EPR) spectroscopy and O2 evolution assays were performed on photosystem II (PSII) membranes which had been treated with 1 M CaCl2 to release the 17, 23 and 33 kilodalton (kDa) extrinsic polypeptides. Manganese was not released from PSII membranes by this treatment as long as a high concentration of chloride was maintained. We have quantitated the EPR signals of the several electron donors and acceptors of PSII that are photooxidized or reduced in a single stable charge separation over the temperature range of 77 to 240 K. The behavior of the samples was qualitatively similar to that observed in samples depleted of only the 17 and 23 kDa polypeptides (de Paula et al. (1986) Biochemistry 25, 6487-6494). In both cases, the S2 state multiline EPR signal was observed in high yield and its formation required bound Ca2+. The lineshape of the S2 state multiline EPR signal and the magnetic properties of the manganese site were virtually identical to those of untreated PSII membranes. These results suggest that the structure of the manganese site is unaffected by removal of the 33 kDa polypeptide. Nevertheless, in samples lacking the 33 kDa polypeptide a stable charge separation could only be produced in about one half of the reaction centers below 160 K, in contrast to the result obtained in untreated or 17 and 23 kDa polypeptide-depleted PSII membranes. This suggests that one function of the 33 kDa polypeptide is to stabilize conformations of PSII that are active in secondary electron transfer events.

Original languageEnglish
Pages (from-to)205-218
Number of pages14
JournalPhotosynthesis Research
Volume12
Issue number3
DOIs
Publication statusPublished - Jan 1987

Fingerprint

Photosystem II Protein Complex
photosystem II
polypeptides
electron paramagnetic resonance spectroscopy
Electron Spin Resonance Spectroscopy
Peptides
Paramagnetic resonance
Manganese
Membranes
manganese
Electrons
magnetic properties
Biochemistry
sampling
calcium chloride
biochemistry
electron transfer
Conformations
Chlorides
Assays

Keywords

  • 33 kilodalton polypeptide
  • manganese
  • photosystem II
  • S state

ASJC Scopus subject areas

  • Plant Science

Cite this

Formation of the S2 state and structure of the Mn complex in photosystem II lacking the extrinsic 33 kilodalton polypeptide. / Miller, Anne Frances; de Paula, Julio C.; Brudvig, Gary W.

In: Photosynthesis Research, Vol. 12, No. 3, 01.1987, p. 205-218.

Research output: Contribution to journalArticle

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