The mode of binding of three extrinsic proteins of 33 kDa, 23 kDa and 18 kDa in the photosystem II complex of spinach

This publication has 27 references indexed in Scilit:

• Nucleotide sequence of cDNA clones encoding the complete ‘23 kDa’ and ‘16 kDa’ precursor proteins associated with the photosynthetic oxygen‐evolving complex from spinach
  FEBS Letters, 1987
• Complete amino acid sequence of 33 kDa protein isolated from spinach photosystem II particles
  FEBS Letters, 1986
• The Cl⁻ effect on photosynthetic oxygen evolution: interaction of Cl⁻ with 18‐kDa, 24‐kDa and 33‐kDa proteins
  FEBS Letters, 1985
• The role of lipids and 17‐kDa protein in enhancing the recovery of O₂ evolution in cholate‐treated thylakoid membranes
  FEBS Letters, 1984
• Role of the 33‐kDa polypeptide in preserving Mn in the photosynthetic oxygen‐evolution system and its replacement by chloride ions
  FEBS Letters, 1984
• Water‐soluble 17 and 23 kDa polypeptides restore oxygen evolution activity by creating a high‐affinity binding site for Ca²⁺ on the oxidizing side of Photosystem II
  FEBS Letters, 1984
• Mn‐preserving extraction of 33‐, 24‐ and 16‐kDa proteins from O₂‐evolving PS II particles by divalent salt‐washing
  FEBS Letters, 1983
• A highly resolved, oxygen‐evolving photosystem II preparation from spinach thylakoid membranes
  FEBS Letters, 1981
• Release of polypeptides from highly active O₂‐evolving photosystem‐2 preparation by this treatment
  FEBS Letters, 1981
• Localization of a 34 000 and a 23 000 M_r polypeptide to the lumenal side of the thylakoid membrane
  FEBS Letters, 1981