Details

Autor(en) / Beteiligte

• Mantri, Monica
• Zhang, Zhihong
• McDonough, Michael A.
• Schofield, Christopher J.

Titel

Autocatalysed oxidative modifications to 2‐oxoglutarate dependent oxygenases

Ist Teil von

• The FEBS journal, 2012-05, Vol.279 (9), p.1563-1575

Ort / Verlag

Oxford, UK: Blackwell Publishing Ltd

Erscheinungsjahr

2012

Quelle

Wiley Online Library All Journals

Beschreibungen/Notizen

• Ferrous iron and 2‐oxoglutarate‐dependent oxygenases and related enzymes catalyse a range of oxidative reactions, possibly the widest of any enzyme family. Their catalytic flexibility is proposed to be related to their nonhaem iron‐binding site, which utilizes two or three protein‐based ligands. A possible penalty for this flexibility is that they may be more prone to oxidative damage than the P450 oxidases, where the iron is arguably located in a more controlled environment. We review the evidence for autocatalysed oxidative modifications to 2‐oxoglutarate‐dependent oxygenases, including the recently reported studies on human enzymes, as well as the oxidative fragmentations observed in the case of the plant ethylene‐forming enzyme (1‐aminocyclopropane‐1‐carboxylic acid oxidase). Iron and 2‐oxoglutarate dependent oxygenases catalyse a range of oxidative reactions. Their catalytic flexibility is proposed to be related to their nonhaem iron binding site which employs two or three protein ligands. A possible penalty for this flexibility is that they may be more prone to oxidative damage. Here we review the evidence for auto‐catalysed oxidative modifications to 2‐oxoglutarate‐dependent oxygenases.