Oxygen activating nonheme iron enzymes

Steven J. Lange, Lawrence Que

Research output: Contribution to journalArticlepeer-review

169 Scopus citations


The past year has witnessed significant advances in the study of oxygen-activating nonheme iron enzymes. Thirteen crystal structures of substrate and substrate analog complexes of protocatechuate 3,4-dioxygenase have revealed intimate details about changes at the enzyme active site during catalysis. Crystallographic data have established a 2-His-1-carboxylate facial triad as a structural motif common to a number of mononuclear nonheme iron enzymes, including isopenicillin N synthase, tyrosine hydroxylase and naphthalene dioxygenase. The first metrical data has been obtained for the high valent intermediates Q and X of methane monooxygenase and ribonucleotide reductase, respectively. The number of enzymes thought to have nonheme diiron sites has been expanded to include alkene monooxygenase from Xanthobacter strain Py2 and the membrane-bound alkane hydroxylase from Pseudomonas oleovorans (AlkB). Finally, synthetic complexes have successfully mimicked chemistry performed by both mono- and dinuclear nonheme iron enzymes, such as the extradiol-cleaving catechol dioxygenases, lipoxygenase, alkane and alkene monoxygenases and fatty acid desaturases.

Original languageEnglish (US)
Pages (from-to)159-172
Number of pages14
JournalCurrent opinion in chemical biology
Issue number2
StatePublished - Apr 1998

Bibliographical note

Funding Information:
National Institutes of Health (GM-33162 and GM-38767) and the National ,Science Foundation (MCB-9405723). We thank Allen Orville and Douglas Ohlcndorf for providing the coordinates to the structures shown m Figure 1.


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