The function of 33-kDa protein in the photosynthetic oxygen-evolution system studied by reconstitution experiments
- 1 February 1985
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Vol. 806 (2) , 283-289
- https://doi.org/10.1016/0005-2728(85)90107-0
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- The role of lipids and 17‐kDa protein in enhancing the recovery of O2 evolution in cholate‐treated thylakoid membranesFEBS Letters, 1984
- Role of the 33‐kDa polypeptide in preserving Mn in the photosynthetic oxygen‐evolution system and its replacement by chloride ionsFEBS 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 IIFEBS Letters, 1984
- Photosynthetic oxygen evolution does not require the participation of polypeptides of 16 and 24 kilodaltonsBiochemical and Biophysical Research Communications, 1984
- Calcium reconstitutes high rates of oxygen evolution in polypeptide depleted Photosystem II preparationsFEBS Letters, 1984
- Reconstitution of photosynthetic oxygen evolving activity by rebinding of 33 kDa protein to CaCl2‐extracted PS II particlesFEBS Letters, 1984
- Partial reconstitution of the photosynthetic oxygen evolution system by rebinding of the 33‐kDa polypeptideFEBS Letters, 1983
- Mn‐preserving extraction of 33‐, 24‐ and 16‐kDa proteins from O2‐evolving PS II particles by divalent salt‐washingFEBS Letters, 1983
- Release of polypeptides from highly active O2‐evolving photosystem‐2 preparation by this treatmentFEBS Letters, 1981
- Localization of a 34 000 and a 23 000 Mr polypeptide to the lumenal side of the thylakoid membraneFEBS Letters, 1981