Partial Characterization of the Iodination Site in D1 Protein of Manganese-Retaining and Manganese-Depleted Photosystem II Membranes
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概要
- 論文の詳細を見る
In manganese-retaining PS II membranes, photooxidized iodide-125 labels a site close to the Cl^- and/or manganese (in S_2 state)-binding sites in D1 protein, whereas in manganese-depleted PS II membranes it labels a site close to the Z^+-binding site in D1 protein (Ikeuchi et al. (1988) Biochim. Biophys. Acta 932:160-169). Amino acid analysis revealed that monoiodotyrosine is the sole amino acid iodinated, and peptide mapping analysis showed that the iodination site is located between proline-141 and methionine-172 of D1 in both samples. These results imply that the tyrosine residue at 147 and/or 161 of D1 is the target of iodination irrespective of the presence or absence of manganese. Although both of the two tyrosine residues stay in membrane-spanning α-helix based on proposed D1 structure, only the tyrosine-161 residue is close to the lumen surface and seems to be the most likely candidate for iodination site. It could be also assumed in turn that Cl^-, manganese- and Z^+-binding sites are close to this tyrosine-161 residue in D1 protein.
- 日本植物生理学会の論文
著者
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Inoue Yorinao
Solar Energy Research Group, Institute for Physical and Chemical Research
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Ikeuchi Masahiko
Solar Energy Research Group, The Institute of Physical and Chemical Research (RIKEN)
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Ikeuchi Masahiko
Dept.life Sci. Univ.of Tokyo
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Ikeuchi M
Dept.life Sci. Univ.of Tokyo
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Inoue Yorinao
Solar Energy Research Group Riken
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Ikeuchi Masahiko
Solar Energy Research Group Riken (the Institute Of Physical And Chemical Research)
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Inoue Yorinao
Solar Ener.res.group Riken
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