Isolation of a manganese-containing protein complex from photosystem II preparations of spinach

Neil R. Bowlby, Wayne Frasch

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

Purified 125I-labeled 33-kDa protein binds to calcium-washed photosystem II preparations at high-affinity and low-affinity binding sites. Filling 70% of the high-affinity site with 33-kDa protein induces 63% of the maximum achievable reconstitution of O2-evolving activity. When N-succinimidyl [(4-azidophenyl)dithio]propionate modified 33-kDa protein was reconstituted into Ca(II)-washed membranes under conditions that primarily filled the high-affinity site and then cross-linked to adjacent proteins by illumination of the photoaffinity label, a cross-linked protein complex was formed that could be solubilized from the membranes with sodium dodecyl sulfate. The protein complex consisted of 22-, 24-, 26-, 28-, 29-, and 31-kDa proteins cross-linked to the 33-kDa protein and contained about 3-4 mol of Mn/mol of protein.

Original languageEnglish (US)
Pages (from-to)1402-1407
Number of pages6
JournalBiochemistry
Volume25
Issue number6
StatePublished - 1986
Externally publishedYes

Fingerprint

Photosystem II Protein Complex
Spinacia oleracea
Manganese
Proteins
Photoaffinity Labels
Membranes
Propionates
Lighting
Sodium Dodecyl Sulfate
Binding Sites
Calcium

ASJC Scopus subject areas

  • Biochemistry

Cite this

Isolation of a manganese-containing protein complex from photosystem II preparations of spinach. / Bowlby, Neil R.; Frasch, Wayne.

In: Biochemistry, Vol. 25, No. 6, 1986, p. 1402-1407.

Research output: Contribution to journalArticle

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AU - Frasch, Wayne

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AB - Purified 125I-labeled 33-kDa protein binds to calcium-washed photosystem II preparations at high-affinity and low-affinity binding sites. Filling 70% of the high-affinity site with 33-kDa protein induces 63% of the maximum achievable reconstitution of O2-evolving activity. When N-succinimidyl [(4-azidophenyl)dithio]propionate modified 33-kDa protein was reconstituted into Ca(II)-washed membranes under conditions that primarily filled the high-affinity site and then cross-linked to adjacent proteins by illumination of the photoaffinity label, a cross-linked protein complex was formed that could be solubilized from the membranes with sodium dodecyl sulfate. The protein complex consisted of 22-, 24-, 26-, 28-, 29-, and 31-kDa proteins cross-linked to the 33-kDa protein and contained about 3-4 mol of Mn/mol of protein.

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