Coordination sphere and structure of the Mn cluster of the oxygen-evolving complex in photosynthetic organisms

Boris K. Semin; Fritz Parak

doi:10.1016/S0014-5793(96)01345-2

Coordination sphere and structure of the Mn cluster of the oxygen-evolving complex in photosynthetic organisms

Boris K. Semin, Fritz Parak

Chair of Biomedical Physics

Moscow State University

Research output: Contribution to journal › Article › peer-review

13 Scopus citations

Abstract

The great similarity between the binding of Fe(II) and the high-affinity Mn-binding site in the Mn-depleted PSII membranes (Semin et al. (1996) FEBS Lett. 375, 223-226) suggests that the coordination sphere of Mn in PSII is also suitable for iron. A comparison is performed between the primary amino acid sequences of D1 and D2 and diiron-oxo enzymes with the function of oxygen activation. All conservative motifs (EXXH) and residues binding and stabilizing the diiron cluster in diiron-oxo enzymes have been found in the C-terminal domains of D1 and D2 polypeptides. On the basis of these sequence similarities we suggest a structural model for the manganese cluster in the oxygen-evolving complex.

Original language	English
Pages (from-to)	259-262
Number of pages	4
Journal	FEBS Letters
Volume	400
Issue number	3
DOIs	https://doi.org/10.1016/S0014-5793(96)01345-2
State	Published - 6 Jan 1997

Keywords

Binuclear iron protein
Iron
Manganese complex
Oxygen-evolving complex
Photosystem II

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10.1016/S0014-5793(96)01345-2

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title = "Coordination sphere and structure of the Mn cluster of the oxygen-evolving complex in photosynthetic organisms",

abstract = "The great similarity between the binding of Fe(II) and the high-affinity Mn-binding site in the Mn-depleted PSII membranes (Semin et al. (1996) FEBS Lett. 375, 223-226) suggests that the coordination sphere of Mn in PSII is also suitable for iron. A comparison is performed between the primary amino acid sequences of D1 and D2 and diiron-oxo enzymes with the function of oxygen activation. All conservative motifs (EXXH) and residues binding and stabilizing the diiron cluster in diiron-oxo enzymes have been found in the C-terminal domains of D1 and D2 polypeptides. On the basis of these sequence similarities we suggest a structural model for the manganese cluster in the oxygen-evolving complex.",

keywords = "Binuclear iron protein, Iron, Manganese complex, Oxygen-evolving complex, Photosystem II",

author = "Semin, {Boris K.} and Fritz Parak",

note = "Funding Information: This work was supported by grants from the Deutsche Forschungsgemeinschaft and the Fonds der Chemischen Industrie.",

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T1 - Coordination sphere and structure of the Mn cluster of the oxygen-evolving complex in photosynthetic organisms

AU - Semin, Boris K.

AU - Parak, Fritz

N1 - Funding Information: This work was supported by grants from the Deutsche Forschungsgemeinschaft and the Fonds der Chemischen Industrie.

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Y1 - 1997/1/6

N2 - The great similarity between the binding of Fe(II) and the high-affinity Mn-binding site in the Mn-depleted PSII membranes (Semin et al. (1996) FEBS Lett. 375, 223-226) suggests that the coordination sphere of Mn in PSII is also suitable for iron. A comparison is performed between the primary amino acid sequences of D1 and D2 and diiron-oxo enzymes with the function of oxygen activation. All conservative motifs (EXXH) and residues binding and stabilizing the diiron cluster in diiron-oxo enzymes have been found in the C-terminal domains of D1 and D2 polypeptides. On the basis of these sequence similarities we suggest a structural model for the manganese cluster in the oxygen-evolving complex.

AB - The great similarity between the binding of Fe(II) and the high-affinity Mn-binding site in the Mn-depleted PSII membranes (Semin et al. (1996) FEBS Lett. 375, 223-226) suggests that the coordination sphere of Mn in PSII is also suitable for iron. A comparison is performed between the primary amino acid sequences of D1 and D2 and diiron-oxo enzymes with the function of oxygen activation. All conservative motifs (EXXH) and residues binding and stabilizing the diiron cluster in diiron-oxo enzymes have been found in the C-terminal domains of D1 and D2 polypeptides. On the basis of these sequence similarities we suggest a structural model for the manganese cluster in the oxygen-evolving complex.

KW - Binuclear iron protein

KW - Iron

KW - Manganese complex

KW - Oxygen-evolving complex

KW - Photosystem II

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JF - FEBS Letters

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Coordination sphere and structure of the Mn cluster of the oxygen-evolving complex in photosynthetic organisms

Abstract

Keywords

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