Biomimetic nonheme iron catalysts for alkane hydroxylation

Miquel Costas, Kui Chen, Lawrence Que

Research output: Contribution to journalReview articlepeer-review

501 Scopus citations


The catalytic functionalization of alkanes under mild conditions is a subject of great current interest. Nature has evolved a number of metalloenzymes such as the heine-containing cytochrome P450 and the nonheme methane monooxygenase, which are capable of effecting such transformations. There has thus been significant interest in modeling such enzyme active sites and developing biomimetic alkane hydroxylation catalysts. In this review, the efforts of the last 10 years in the development of nonheme iron catalysts are summarized and discussed. These catalysts typically act in concert with ROOH or H2O2. With ROOH as oxidant, it is clear from mechanistic studies that alkoxyl radicals are the principal agents that cleave the alkane C-H bond to generate long-lived alkyl radicals. This conclusion, for the most part, applies also for oxidations involving H2O2. In a few cases, however, stereospecific alkane hydroxylation is observed. For these instances, there is evidence from H2/18O exchange experiments that a high-valent iron-oxo species is involved. (C) 2000 Elsevier Science S.A.

Original languageEnglish (US)
Pages (from-to)517-544
Number of pages28
JournalCoordination Chemistry Reviews
StatePublished - 2000

Bibliographical note

Funding Information:
This work was supported by the National Institutes of Health (GM-33162 and GM-38767). M.C. wishes to thank the Fundacio La Caixa for financial support. K.C. wishes to thank the Department of Chemistry, University of Minnesota for a thesis fellowship.


  • Alkane hydroxylation
  • Biomimetic
  • Iron catalysts
  • Nonheme iron enzymes
  • Peroxide


Dive into the research topics of 'Biomimetic nonheme iron catalysts for alkane hydroxylation'. Together they form a unique fingerprint.

Cite this