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Crystal Structures of Fe 2+ Dioxygenase Superoxo, Alkylperoxo, and Bound Product Intermediates
Open accessAbstract
We report the structures of three intermediates in the O 2 activation and insertion reactions of an extradiol ring-cleaving dioxygenase. A crystal of Fe 2+ -containing homoprotocatechuate 2,3-dioxygenase was soaked in the slow substrate 4-nitrocatechol in a low O 2 atmosphere. The x-ray crystal structure shows that three different intermediates reside in different subunits of a single homotetrameric enzyme molecule. One of these is the key substrate-alkylperoxo-Fe 2+ intermediate, which has been predicted, but not structurally characterized, in an oxygenase. The intermediates define the major chemical steps of the dioxygenase mechanism and point to a general mechanistic strategy for the diverse 2-His-1-carboxylate enzyme family.
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Metadata
- Authors
- Kovaleva, E. G., & Lipscomb, J. D.
- Venue
- Science
- Published
- 2007-04-20
- Volume
- 316
- Issue
- 5823
- Pages
- 453-457
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2083280040
- Cited by
- 395
- References
- 0
- FWCI
- 20.77
- Type
- journal article
- Language
- en
- Open access
- green
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- Kovaleva, E. G., & Lipscomb, J. D. (2007). Crystal Structures of Fe 2+ Dioxygenase Superoxo, Alkylperoxo, and Bound Product Intermediates. Science. https://doi.org/10.1126/science.1134697
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