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

Roth Arne | Zendy; Plass Winfried | Zendy

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

Author(s) -

Roth Arne,

Plass Winfried

Publication year - 2008

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.200802366

Subject(s) - oxygenase , ribonucleotide reductase , carboxylate , chemistry , active site , stereochemistry , protein subunit , crystallography , catalysis , biochemistry , enzyme , gene

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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