Met246 and Asn250 in the D2 protein are essential for the operation of the quinone-Fe-acceptor complex of Photosystem II.
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| Titel: | Met246 and Asn250 in the D2 protein are essential for the operation of the quinone-Fe-acceptor complex of Photosystem II. |
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| Autoren: | Zhong V; Department of Biochemistry, University of Otago, P.O. Box 56, Dunedin 9054, New Zealand., Vass I; HUN-REN, Biological Research Center, Institute of Plant Biology, P.O. Box 521, Temesvári krt. 62, Szeged H-6726, Hungary., Patil PP; HUN-REN, Biological Research Center, Institute of Plant Biology, P.O. Box 521, Temesvári krt. 62, Szeged H-6726, Hungary.; Faculty of Science and Informatics, Doctoral School of Biology, University of Szeged, P.O. Box 652, Dóm tér 10, Szeged H-6720, Hungary., Eaton-Rye JJ; Department of Biochemistry, University of Otago, P.O. Box 56, Dunedin 9054, New Zealand. |
| Quelle: | Plant & cell physiology [Plant Cell Physiol] 2025 Nov 28; Vol. 66 (11), pp. 1730-1749. |
| Publikationsart: | Journal Article |
| Sprache: | English |
| Info zur Zeitschrift: | Publisher: Oxford University Press Country of Publication: Japan NLM ID: 9430925 Publication Model: Print Cited Medium: Internet ISSN: 1471-9053 (Electronic) Linking ISSN: 00320781 NLM ISO Abbreviation: Plant Cell Physiol Subsets: MEDLINE |
| Imprint Name(s): | Publication: Tokyo : Oxford University Press Original Publication: Kyoto, Japan : Japanese Society of Plant Physiologists, |
| MeSH-Schlagworte: | Photosystem II Protein Complex*/metabolism , Photosystem II Protein Complex*/genetics , Synechocystis*/metabolism , Synechocystis*/genetics , Bacterial Proteins*/metabolism , Bacterial Proteins*/genetics , Quinones*/metabolism, Electron Transport ; Plastoquinone/metabolism ; Mutation ; Binding Sites ; Thylakoids/metabolism |
| Abstract: | The chemical properties of the primary (QA) and secondary (QB) plastoquinone electron acceptors of Photosystem II (PS II) depend on their protein environments. The DE loop of the D2 protein (residues 222-262) contributes to the QA-binding site while the DE loop of the D1 protein (residues 233-266) contributes to the QB-binding environment. The roles of the invariant D2-Met246 and D2-Asn250 residues in the vicinity of the QA-binding site have been investigated in the cyanobacterium Synechocystis sp. PCC 6803 using mutants targeting both residues. The M246F strain was phenotypically similar to control cells; however, the M246A, N250A, and N250H strains had slowed photoautotrophic growth and were sensitive to high light and the addition of formate. In addition, the M246K and N250N strains were unable to assemble PS II. Chlorophyll a fluorescence measurements indicated electron transfer between QA and QB was modified in the M246A, N250A, and N250H strains, and the exchange of plastoquinol between the QB-binding site and the plastoquinone pool in the thylakoid membrane was impaired. Modified electron transfer in these mutants in the presence or absence of formate was restored by the addition of bicarbonate. In addition, thermoluminescence measurements showed a down shift in the redox midpoint potential of the QA/QA- couple in the N250A and N250H strains. These results demonstrate that Met246 and Asn250 play indispensable roles in the quinone-iron-acceptor complex, influencing both QA binding and the binding of the bicarbonate ligand to the non-heme iron that is located between QA and QB. (© The Author(s) 2025. Published by Oxford University Press on behalf of the Japanese Society of Plant Physiologists.) |
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| Contributed Indexing: | Keywords: Synechocystis sp. PCC 6803; D2; Photosystem II; QA; QB; bicarbonate |
| Substance Nomenclature: | 0 (Photosystem II Protein Complex) OAC30J69CN (Plastoquinone) 0 (Bacterial Proteins) 0 (Quinones) |
| Entry Date(s): | Date Created: 20250714 Date Completed: 20251128 Latest Revision: 20251130 |
| Update Code: | 20251130 |
| PubMed Central ID: | PMC12661319 |
| DOI: | 10.1093/pcp/pcaf078 |
| PMID: | 40657803 |
| Datenbank: | MEDLINE |
Nájsť tento článok vo Web of Science | Abstract: | The chemical properties of the primary (QA) and secondary (QB) plastoquinone electron acceptors of Photosystem II (PS II) depend on their protein environments. The DE loop of the D2 protein (residues 222-262) contributes to the QA-binding site while the DE loop of the D1 protein (residues 233-266) contributes to the QB-binding environment. The roles of the invariant D2-Met246 and D2-Asn250 residues in the vicinity of the QA-binding site have been investigated in the cyanobacterium Synechocystis sp. PCC 6803 using mutants targeting both residues. The M246F strain was phenotypically similar to control cells; however, the M246A, N250A, and N250H strains had slowed photoautotrophic growth and were sensitive to high light and the addition of formate. In addition, the M246K and N250N strains were unable to assemble PS II. Chlorophyll a fluorescence measurements indicated electron transfer between QA and QB was modified in the M246A, N250A, and N250H strains, and the exchange of plastoquinol between the QB-binding site and the plastoquinone pool in the thylakoid membrane was impaired. Modified electron transfer in these mutants in the presence or absence of formate was restored by the addition of bicarbonate. In addition, thermoluminescence measurements showed a down shift in the redox midpoint potential of the QA/QA- couple in the N250A and N250H strains. These results demonstrate that Met246 and Asn250 play indispensable roles in the quinone-iron-acceptor complex, influencing both QA binding and the binding of the bicarbonate ligand to the non-heme iron that is located between QA and QB.<br /> (© The Author(s) 2025. Published by Oxford University Press on behalf of the Japanese Society of Plant Physiologists.) |
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| ISSN: | 1471-9053 |
| DOI: | 10.1093/pcp/pcaf078 |