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J Inorg Biochem. 2006 Apr;100(4):644-69. Epub 2006 Mar 2.

Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins.

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1
The Oxford Centre for Molecular Sciences and the Department of Chemistry, Chemistry Research Laboratory, University of Oxford, Mansfield Road, Oxford, Oxon OX1 3TA, UK.

Abstract

Mononuclear non-heme ferrous iron dependent oxygenases and oxidases constitute an extended enzyme family that catalyze a wide range of oxidation reactions. The largest known sub-group employs 2-oxoglutarate as a cosubstrate and catalysis by these and closely related enzymes is proposed to proceed via a ferryl intermediate coordinated to the active site via a conserved HXD/E...H motif. Crystallographic studies on the 2-oxoglutarate oxygenases and related enzymes have revealed a common double-stranded beta-helix core fold that supports the residues coordinating the iron. This fold is common to proteins of the cupin and the JmjC transcription factor families. The crystallographic studies on 2-oxoglutarate oxygenases and closely related enzymes are reviewed and compared with other metallo-enzymes/related proteins containing a double-stranded beta-helix fold. Proposals regarding the suitability of the active sites and folds of the 2-oxoglutarate oxygenases to catalyze reactions involving reactive oxidizing species are described.

PMID:
16513174
DOI:
10.1016/j.jinorgbio.2006.01.024
[Indexed for MEDLINE]
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