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Carboxylate-Bridged Dinuclear Active Sites in Oxygenases: Diiron, Dimanganese, or is Heterodinuclear Better?

Arne Roth Dr.

Institut für Anorganische und Analytische Chemie, Friedrich-Schiller-Universität Jena, Carl-Zeiss-Promenade 10, 07745 Jena (Germany), Fax: (+49) 3641-948-132 http://www.acp.uni-jena.de

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Winfried Plass Prof. Dr.,

Winfried Plass Prof. Dr.

[email protected]

Institut für Anorganische und Analytische Chemie, Friedrich-Schiller-Universität Jena, Carl-Zeiss-Promenade 10, 07745 Jena (Germany), Fax: (+49) 3641-948-132 http://www.acp.uni-jena.de

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Arne Roth Dr.,

Arne Roth Dr.

Institut für Anorganische und Analytische Chemie, Friedrich-Schiller-Universität Jena, Carl-Zeiss-Promenade 10, 07745 Jena (Germany), Fax: (+49) 3641-948-132 http://www.acp.uni-jena.de

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Winfried Plass Prof. Dr.,

Winfried Plass Prof. Dr.

[email protected]

Institut für Anorganische und Analytische Chemie, Friedrich-Schiller-Universität Jena, Carl-Zeiss-Promenade 10, 07745 Jena (Germany), Fax: (+49) 3641-948-132 http://www.acp.uni-jena.de

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First published: 22 September 2008

https://doi.org/10.1002/anie.200802366

Citations: 11

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Graphical Abstract

To mix or not to mix: The N-oxygenase AurF of S. thioluteus has an unusual carboxylate-bridged dinuclear active site (see picture; gray C, blue N, red O, green Mn, turquoise Mn/Fe). The similarity with a recently discovered Mn/Fe-oxygenase subunit of the ribonucleotide reductase of C. trachomatis suggests that it might contain both Mn and Fe. The N-oxygenase of S. thioluteus very likely represents the first member of a new family of Mn/Fe-oxygenases.

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Volume47, Issue40

September 22, 2008

Pages 7588-7591

Carboxylate-Bridged Dinuclear Active Sites in Oxygenases: Diiron, Dimanganese, or is Heterodinuclear Better?

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Carboxylate-Bridged Dinuclear Active Sites in Oxygenases: Diiron, Dimanganese, or is Heterodinuclear Better?

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