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Related Experiment Videos

Manganese-binding proteins of the oxygen-evolving complex.

R Mei1, J P Green, R T Sayre

  • 1Department of Biology, University of Michigan, Ann Arbor 48109-1048.

Biochemistry
|June 27, 1989
PubMed
Summary

The extrinsic 33-kDa protein (P33) binds to D1 and D2 proteins in Photosystem II (PSII) preparations, retaining manganese and catalyzing water oxidation. This complex

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Area of Science:

  • Biochemistry
  • Photosynthesis research
  • Protein complex analysis

Background:

  • Photosynthetic water oxidation is crucial for life.
  • The extrinsic 33-kDa protein (P33) plays a role in Photosystem II (PSII) water oxidation.
  • PSII preparations depleted of P33 lose water-oxidation activity.

Purpose of the Study:

  • To identify the proteins responsible for manganese binding in the oxygen-evolving complex.
  • To characterize the functional complex formed by P33 and other PSII proteins.

Main Methods:

  • Covalent cross-linking of P33 to P33-depleted PSII preparations.
  • Purification of cross-linked protein complexes using SDS-PAGE.
  • Assay of catalase activity (H2O2 to O2 conversion) and manganese content.

Main Results:

  • A functional complex containing P33, D1, D2, and a 34-kDa protein was reconstituted.
  • The cross-linked complex retained manganese and catalyzed H2O2 oxidation.
  • Calcium and chloride enhanced activity, while lanthanum and hydroxylamine inhibited it.
  • High manganese content (0.34 µg Mn/180 µg protein) was found, with Mn/protein ratios of 3.6–4.5.

Conclusions:

  • Direct evidence shows that D1, D2, and/or the 34-kDa protein bind manganese in the oxygen-evolving complex.
  • The reconstituted complex provides a model for studying manganese binding and water oxidation mechanisms.

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