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J Biol Chem, Vol. 273, Issue 8, 4629-4634, February 20, 1998

Intramolecular Cross-linking of the Extrinsic 33-kDa Protein Leads to Loss of Oxygen Evolution but Not Its Ability of Binding to Photosystem II and Stabilization of the Manganese Cluster

Isao Enami, Masaharu Kamo^¶, Hisataka Ohta, Seitaro Takahashi, Taro Miura, Miho Kusayanagi, Sizuko Tanabe, Ayako Kamei, Akihiro Motoki, Masahiko Hirano, Tatsuya Tomo^**, and Kimiyuki Satoh^**

From the  Department of Biology, Faculty of Science, Science University of Tokyo, Kagurazaka 1-3, Shinjuku-ku, Tokyo 162, Japan, the ^¶ Research Institute for Biosciences, Science University of Tokyo, Yamazaki, Noda, Chiba 278, Japan, the  Biological Sciences Department, Toray Research Center Inc., Kamakura 248, Japan, and the ^** Department of Biology, Okayama University, Okayama 700, Japan

The extrinsic 33-kDa protein of photosystem II (PSII) was intramolecularly cross-linked by a zero-length cross-linker, 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide. The resulting cross-linked 33-kDa protein rebound to urea/NaCl-washed PSII membranes, which stabilized the binding of manganese as effectively as the untreated 33-kDa protein. In contrast, the oxygen evolution was not restored by binding of the cross-linked protein, indicating that the binding and manganese-stabilizing capabilities of the 33-kDa protein are retained but its reactivating ability is lost by intramolecular cross-linking of the protein. From measurements of CD spectra at high temperatures, the secondary structure of the intramolecularly cross-linked 33-kDa protein was found to be stabilized against heat treatment at temperatures 20 °C higher than that of the untreated 33-kDa protein, suggesting that structural flexibility of the 33-kDa protein was much decreased by the intramolecular cross-linking. The rigid structure is possibly responsible for the loss of the reactivating ability of the 33-kDa protein, which implies that binding of the 33-kDa protein to PSII is accompanied by a conformational change essential for the reactivation of oxygen evolution. Peptide mapping, N-terminal sequencing, and mass spectroscopic analysis of protease-digested products of the intramolecularly cross-linked 33-kDa protein revealed that cross-linkings occurred between the amino group of Lys⁴⁸ and the carboxyl group of Glu²⁴⁶, and between the carboxyl group of Glu¹⁰ and the amino group of Lys¹⁴. These cross-linked amino acid residues are thus closely associated with each other through electrostatic interactions.

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